{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,15]],"date-time":"2026-05-15T18:14:03Z","timestamp":1778868843001,"version":"3.51.4"},"reference-count":166,"publisher":"Springer Science and Business Media LLC","issue":"13","license":[{"start":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T00:00:00Z","timestamp":1684368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T00:00:00Z","timestamp":1684368000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Ciencia y Tecnolog\u00eda","doi-asserted-by":"publisher","award":["461347"],"award-info":[{"award-number":["461347"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Appl Microbiol Biotechnol"],"published-print":{"date-parts":[[2023,7]]},"DOI":"10.1007\/s00253-023-12578-1","type":"journal-article","created":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T11:03:03Z","timestamp":1684407783000},"page":"4133-4152","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Production of recombinant scorpion antivenoms in E. coli: current state and perspectives"],"prefix":"10.1007","volume":"107","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8290-1635","authenticated-orcid":false,"given":"Susana Mar\u00eda","family":"Alonso Villela","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8180-0573","authenticated-orcid":false,"given":"Hazar","family":"Kra\u00efem-Ghezal","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3147-245X","authenticated-orcid":false,"given":"Balkiss","family":"Bouhaouala-Zahar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9830-5093","authenticated-orcid":false,"given":"Carine","family":"Bideaux","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6291-3655","authenticated-orcid":false,"given":"C\u00e9sar Arturo","family":"Aceves Lara","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6389-5441","authenticated-orcid":false,"given":"Luc","family":"Fillaudeau","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2023,5,18]]},"reference":[{"key":"12578_CR1","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1042\/BJ20090697","volume":"424","author":"RB Abderrazek","year":"2009","unstructured":"Abderrazek RB, Hmila I, Vincke C, Benlasfar Z, Pellis M, Dabbek H, Saerens D, El Ayeb M, Muyldermans S, Bouhaouala-Zahar B (2009) Identification of potent nanobodies to neutralize the most poisonous polypeptide from scorpion venom. Biochem J 424:263\u2013272. https:\/\/doi.org\/10.1042\/BJ20090697","journal-title":"Biochem J"},{"key":"12578_CR2","doi-asserted-by":"publisher","first-page":"906","DOI":"10.1016\/S0140-6736(98)12083-4","volume":"354","author":"F Abroug","year":"1999","unstructured":"Abroug F, ElAtrous S, Nouria S, Haguiga H, Touzi N, Bouchoucha S (1999) Serotherapy in scorpion envenomation: a randomised controlled trial. Lancet 354:906\u2013909. https:\/\/doi.org\/10.1016\/S0140-6736(98)12083-4","journal-title":"Lancet"},{"key":"12578_CR3","doi-asserted-by":"publisher","first-page":"2955","DOI":"10.1016\/j.bbagen.2018.08.019","volume":"1862","author":"E Alirahimi","year":"2018","unstructured":"Alirahimi E, Kazemi-Lomedasht F, Shahbazzadeh D, Habibi-Anbouhi M, Hosseininejad Chafi M, Sotoudeh N, Ghaderi H, Muyldermans S, Behdani M (2018) Nanobodies as novel therapeutic agents in envenomation. Biochim Biophys Acta - Gen Subj 1862:2955\u20132965. https:\/\/doi.org\/10.1016\/j.bbagen.2018.08.019","journal-title":"Biochim Biophys Acta - Gen Subj"},{"key":"12578_CR4","doi-asserted-by":"publisher","first-page":"1017","DOI":"10.1007\/s00253-021-11093-5","volume":"105","author":"SM Alonso Villela","year":"2021","unstructured":"Alonso Villela SM, Ghezal-Kra\u00efem H, Bouhaouala-Zahar B, Bideaux C, Aceves Lara CA, Fillaudeau L (2021) Effect of temperature on the production of a recombinant antivenom in fed-batch mode. Appl Microbiol Biotechnol 105:1017\u20131030. https:\/\/doi.org\/10.1007\/s00253-021-11093-5","journal-title":"Appl Microbiol Biotechnol"},{"key":"12578_CR5","doi-asserted-by":"publisher","first-page":"2541","DOI":"10.3390\/toxins6082541","volume":"6","author":"L Alvarenga","year":"2014","unstructured":"Alvarenga L, Zahid M, Tommaso A, Juste M, Aubrey N, Billiald P, Muzard J (2014) Engineering venom\u2019s toxin-neutralizing antibody fragments and its therapeutic potential. Toxins (Basel) 6:2541\u20132567. https:\/\/doi.org\/10.3390\/toxins6082541","journal-title":"Toxins (Basel)"},{"key":"12578_CR6","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/j.imlet.2011.05.002","volume":"139","author":"I Amaro","year":"2011","unstructured":"Amaro I, Ria\u00f1o-Umbarila L, Becerril B, Possani LD (2011) Isolation and characterization of a human antibody fragment specific for Ts1 toxin from Tityus serrulatus scorpion. Immunol Lett 139:73\u201379. https:\/\/doi.org\/10.1016\/j.imlet.2011.05.002","journal-title":"Immunol Lett"},{"key":"12578_CR7","doi-asserted-by":"publisher","first-page":"298","DOI":"10.1515\/tjb-2015-0017","volume":"40","author":"AB Ariff","year":"2015","unstructured":"Ariff AB, Nelofer R, Rahman RNZRA, Basri M (2015) Kinetics and modelling of batch fermentation for the production of organic solvent tolerant and thermostable lipase by recombinant E. coli. Turkish J Biochem 40:298\u2013309. https:\/\/doi.org\/10.1515\/tjb-2015-0017","journal-title":"Turkish J Biochem"},{"key":"12578_CR8","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1186\/s40364-021-00332-6","volume":"9","author":"Y Asaadi","year":"2021","unstructured":"Asaadi Y, Jouneghani FF, Janani S, Rahbarizadeh F (2021) A comprehensive comparison between camelid nanobodies and single chain variable fragments. Biomark Res 9:87. https:\/\/doi.org\/10.1186\/s40364-021-00332-6","journal-title":"Biomark Res"},{"key":"12578_CR9","doi-asserted-by":"publisher","first-page":"617","DOI":"10.1007\/s000180300053","volume":"60","author":"N Aubrey","year":"2003","unstructured":"Aubrey N, Devaux C, Sizaret PY, Rochat H, Goyffon M, Billiald P (2003) Design and evaluation of a diabody to improve protection against a potent scorpion neurotoxin. Cell Mol Life Sci 60:617\u2013628. https:\/\/doi.org\/10.1007\/s000180300053","journal-title":"Cell Mol Life Sci"},{"key":"12578_CR10","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1016\/j.toxicon.2003.11.024","volume":"43","author":"N Aubrey","year":"2004","unstructured":"Aubrey N, Muzard J, Christophe J, Goyffon M, Devaux C, Billiald P (2004) Engineering of a recombinant Fab from a neutralizing IgG directed against scorpion neurotoxin AahI, and functional evaluation versus other antibody fragments. Toxicon 43:233\u2013241. https:\/\/doi.org\/10.1016\/j.toxicon.2003.11.024","journal-title":"Toxicon"},{"key":"12578_CR11","doi-asserted-by":"publisher","unstructured":"Aubrey N, Devaux C, Goyffon M, Rochat H, Billiald P (2001) A recombinant scFv\/streptavidin-binding peptide fusion protein for the quantitative determination of the scorpion venom neurotoxin AahI.https:\/\/doi.org\/10.1515\/BC.2001.197","DOI":"10.1515\/BC.2001.197"},{"key":"12578_CR12","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1016\/j.ymeth.2017.01.009","volume":"116","author":"BV Ayyar","year":"2017","unstructured":"Ayyar BV, Arora S, Ravi SS (2017) Optimizing antibody expression: the nuts and bolts. Methods 116:51\u201362. https:\/\/doi.org\/10.1016\/j.ymeth.2017.01.009","journal-title":"Methods"},{"key":"12578_CR13","doi-asserted-by":"publisher","first-page":"2366","DOI":"10.1007\/s12010-009-8718-5","volume":"160","author":"V Babaeipour","year":"2010","unstructured":"Babaeipour V, Shojaosadati SA, Khalilzadeh R, Maghsoudi N, Farnoud AM (2010) Enhancement of human \u03b3-Interferon production in recombinant E. coli using batch cultivation. Appl Biochem Biotechnol 160:2366\u20132376. https:\/\/doi.org\/10.1007\/s12010-009-8718-5","journal-title":"Appl Biochem Biotechnol"},{"key":"12578_CR14","doi-asserted-by":"publisher","first-page":"953","DOI":"10.4014\/jmb.1412.12079","volume":"25","author":"MN Baeshen","year":"2015","unstructured":"Baeshen MN, Al-Hejin AM, Bora RS, Ahmed MMM, Ramadan HAI, Saini KS, Baeshen NA, Redwan EM (2015) Production of biopharmaceuticals in E. coli: current scenario and future perspectives. J Microbiol Biotechnol 25:953\u2013962. https:\/\/doi.org\/10.4014\/jmb.1412.12079","journal-title":"J Microbiol Biotechnol"},{"key":"12578_CR15","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1016\/j.peptides.2005.06.023","volume":"27","author":"S Banerjee","year":"2006","unstructured":"Banerjee S, Curto EV, Beckman M, Brown GB, Zhong J, Krishna NR (2006) Expression of functional scorpion neurotoxin Lqq-V in E.coli. Peptides 27:49\u201354. https:\/\/doi.org\/10.1016\/j.peptides.2005.06.023","journal-title":"Peptides"},{"key":"12578_CR16","doi-asserted-by":"publisher","first-page":"1399","DOI":"10.1038\/nbt1029","volume":"22","author":"F Baneyx","year":"2004","unstructured":"Baneyx F, Mujacic M (2004) Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 22:1399\u20131408. https:\/\/doi.org\/10.1038\/nbt1029","journal-title":"Nat Biotechnol"},{"key":"12578_CR17","doi-asserted-by":"publisher","first-page":"42","DOI":"10.7705\/biomedica.v24i1.1247","volume":"24","author":"J Barona","year":"2004","unstructured":"Barona J, Otero R, N\u00fa\u00f1ez V (2004) Aspectos toxinol\u00f3gicos e inmunoqu\u00edmicos del veneno del escorpi\u00f3n Tityus pachyurus Pocock de Colombia: capacidad neutralizante de antivenenos producidos en Latinoam\u00e9rica. Biomedica 24:42. https:\/\/doi.org\/10.7705\/biomedica.v24i1.1247","journal-title":"Biomedica"},{"key":"12578_CR18","doi-asserted-by":"publisher","first-page":"164","DOI":"10.1580\/0953-9859-2.3.164","volume":"2","author":"HS Bawaskar","year":"1991","unstructured":"Bawaskar HS, Bawaskar PH (1991) Scorpion sting: a review of 121 cases. J Wilderness Med 2:164\u2013174. https:\/\/doi.org\/10.1580\/0953-9859-2.3.164","journal-title":"J Wilderness Med"},{"key":"12578_CR19","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1093\/protein\/gzr037","volume":"24","author":"R Ben Abderrazek","year":"2011","unstructured":"Ben Abderrazek R, Vincke C, Hmila I, Saerens D, Abidi N, El Ayeb M, Muyldermans S, Bouhaouala-Zahar B (2011) Development of Cys38 knock-out and humanized version of NbAahII10 nanobody with improved neutralization of AahII Scorpion toxin. Protein Eng Des Sel 24:727\u2013735. https:\/\/doi.org\/10.1093\/protein\/gzr037","journal-title":"Protein Eng Des Sel"},{"key":"12578_CR20","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fimmu.2022.863012","volume":"13","author":"R Ben Abderrazek","year":"2022","unstructured":"Ben Abderrazek R, Ksouri A, Idoudi F, Dhaouadi S, Hamdi E, Vincke C, Farah A, Benlasfar Z, Majdoub H, El Ayeb M, Muyldermans S, Bouhaouala-Zahar B (2022) Neutralizing dromedary-derived nanobodies against BotI-like toxin from the most hazardous scorpion venom in the Middle East and North Africa Region. Front Immunol 13:1\u201313. https:\/\/doi.org\/10.3389\/fimmu.2022.863012","journal-title":"Front Immunol"},{"key":"12578_CR21","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1006\/abbi.1995.1185","volume":"317","author":"P Billiald","year":"1995","unstructured":"Billiald P, Motta G, Vaux DJ (1995) Production of a functional anti-scorpion hemocyanin scFv in Escherichia coli. Arch Biochem Biophys 317:429\u2013438. https:\/\/doi.org\/10.1006\/abbi.1995.1185","journal-title":"Arch Biochem Biophys"},{"key":"12578_CR22","doi-asserted-by":"publisher","first-page":"468","DOI":"10.1146\/annurev.mi.39.100185.003151","volume":"5","author":"MA Blight","year":"1994","unstructured":"Blight MA, Chervaux C, Holland IB (1994) Protein secretion pathway in Escherichia coli. Curr Opin Biotechnol 5:468\u2013474. https:\/\/doi.org\/10.1146\/annurev.mi.39.100185.003151","journal-title":"Curr Opin Biotechnol"},{"key":"12578_CR23","doi-asserted-by":"publisher","first-page":"9971","DOI":"10.1007\/s00253-015-6836-2","volume":"99","author":"J Boldrini-Fran\u00e7a","year":"2015","unstructured":"Boldrini-Fran\u00e7a J, Rodrigues RS, Santos-Silva LK, de Souza DLN, Gomes MSR, Cologna CT, de Pauw E, Quinton L, Henrique-Silva F, de Melo RV, Arantes EC (2015) Expression of a new serine protease from Crotalus durissus collilineatus venom in Pichia pastoris and functional comparison with the native enzyme. Appl Microbiol Biotechnol 99:9971\u20139986. https:\/\/doi.org\/10.1007\/s00253-015-6836-2","journal-title":"Appl Microbiol Biotechnol"},{"key":"12578_CR24","doi-asserted-by":"publisher","first-page":"105346","DOI":"10.1016\/j.actatropica.2020.105346","volume":"204","author":"A Borges","year":"2020","unstructured":"Borges A, Lomonte B, Angulo Y, Acosta de Pati\u00f1o H, Pascale JM, Otero R, Miranda RJ, De Sousa L, Graham MR, G\u00f3mez A, Pardal PPO, Ishikawa E, Bonilla F, Castillo A, de Avila RAM, G\u00f3mez JP, Caro-L\u00f3pez JA (2020) Venom diversity in the Neotropical scorpion genus Tityus: Implications for antivenom design emerging from molecular and immunochemical analyses across endemic areas of scorpionism. Acta Trop 204:105346. https:\/\/doi.org\/10.1016\/j.actatropica.2020.105346","journal-title":"Acta Trop"},{"key":"12578_CR25","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1111\/j.1432-1033.1996.0653w.x","volume":"238","author":"B Bouhaouala-Zahar","year":"1996","unstructured":"Bouhaouala-Zahar B, Ducancel F, Zenouaki I, Khalifa R, Borchani L, Pelhate M, Boulain J-C, Ayeb M, Menez A, Karoui H (1996) A recombinant insect-specific alpha-toxin of Buthus occitanus tunetanus scorpion confers protection against homologous mammal toxins. Eur J Biochem 238:653\u2013660. https:\/\/doi.org\/10.1111\/j.1432-1033.1996.0653w.x","journal-title":"Eur J Biochem"},{"key":"12578_CR26","doi-asserted-by":"publisher","first-page":"358","DOI":"10.2174\/187152811797200713","volume":"10","author":"B Bouhaouala-Zahar","year":"2011","unstructured":"Bouhaouala-Zahar B, Ben Abderrazek R, Hmila I, Abidi N, Muyldermans S, El Ayeb M (2011) Immunological aspects of scorpion toxins: current status and perspectives. Inflamm Allergy Drug Targets 10:358\u2013368. https:\/\/doi.org\/10.2174\/187152811797200713","journal-title":"Inflamm Allergy Drug Targets"},{"key":"12578_CR27","doi-asserted-by":"publisher","first-page":"772","DOI":"10.1002\/bit.25842","volume":"113","author":"D Calleja","year":"2016","unstructured":"Calleja D, Kavanagh J, de Mas C, L\u00f3pez-Sant\u00edn J (2016) Simulation and prediction of protein production in fed-batch E. coli cultures: an engineering approach. Biotechnol Bioeng 113:772\u2013782. https:\/\/doi.org\/10.1002\/bit.25842","journal-title":"Biotechnol Bioeng"},{"key":"12578_CR28","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1590\/S1678-91992004000100007","volume":"10","author":"DM Candido","year":"2004","unstructured":"Candido DM, Lucas S (2004) Maintenance of scorpions of the genus Tityus Koch (Scorpiones, Buthidae) for venom obtention at Instituto Butantan, S\u00e3o Paulo, Brazil. J Venom Anim Toxins Incl Trop Dis 10:86\u201397. https:\/\/doi.org\/10.1590\/S1678-91992004000100007","journal-title":"J Venom Anim Toxins Incl Trop Dis"},{"key":"12578_CR29","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1016\/j.pep.2016.01.007","volume":"121","author":"JE Cantu-Bustos","year":"2016","unstructured":"Cantu-Bustos JE, Vargas-Cortez T, Morones-Ramirez JR, Balderas-Renteria I, Galbraith DW, McEvoy MM, Zarate X (2016) Expression and purification of recombinant proteins in Escherichia coli tagged with the metal-binding protein CusF. Protein Expr Purif 121:61\u201365. https:\/\/doi.org\/10.1016\/j.pep.2016.01.007","journal-title":"Protein Expr Purif"},{"key":"12578_CR30","doi-asserted-by":"publisher","first-page":"1240","DOI":"10.1002\/btpr.433","volume":"26","author":"P Cao","year":"2010","unstructured":"Cao P, Yu J, Lu W, Cai X, Wang Z, Gu Z, Zhang J, Ye T, Wang M (2010) Expression and purification of an antitumor-analgesic peptide from the venom of Mesobuthus martensii Karsch by small ubiquitin-related modifier fusion in Escherichia coli. Biotechnol Prog 26:1240\u20131244. https:\/\/doi.org\/10.1002\/btpr.433","journal-title":"Biotechnol Prog"},{"key":"12578_CR31","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1016\/j.toxicon.2015.02.007","volume":"97","author":"AO Carmo","year":"2015","unstructured":"Carmo AO, Chatzaki M, Horta CCR, Magalh\u00e3es BF, Oliveira-Mendes BBR, Ch\u00e1vez-Ol\u00f3rtegui C, Kalapothakis E (2015) Evolution of alternative methodologies of scorpion antivenoms production. Toxicon 97:64\u201374. https:\/\/doi.org\/10.1016\/j.toxicon.2015.02.007","journal-title":"Toxicon"},{"key":"12578_CR32","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1007\/s00253-011-3649-9","volume":"94","author":"RJ Carvalho","year":"2012","unstructured":"Carvalho RJ, Cabrera-Crespo J, Tanizaki MM, Gon\u00e7alves VM (2012) Development of production and purification processes of recombinant fragment of pneumococcal surface protein A in Escherichia coli using different carbon sources and chromatography sequences. Appl Microbiol Biotechnol 94:683\u2013694. https:\/\/doi.org\/10.1007\/s00253-011-3649-9","journal-title":"Appl Microbiol Biotechnol"},{"key":"12578_CR33","doi-asserted-by":"publisher","unstructured":"Chgoury F, Benabderrazek R, Tounsi H, Oukkach N, Hmila I, Boubaker S, Ayeb M, Sa\u00efle R, N G, Bouhaouala-Zahar B (2015) Effectiveness of the Androctonus Australis Hector nanobody Nbf12-10 antivenom to neutralize significantly the toxic effect and tissue damage provoked by fraction of Androctonus mauretanicus (Morocco) scorpion venom. Biochem Pharmacol (Los Angel) 4:174. https:\/\/doi.org\/10.4172\/2167-0501.1000174","DOI":"10.4172\/2167-0501.1000174"},{"key":"12578_CR34","doi-asserted-by":"publisher","first-page":"165","DOI":"10.2147\/DDDT.S24754","volume":"6","author":"J-P Chippaux","year":"2012","unstructured":"Chippaux J-P (2012) Emerging options for the management of scorpion stings. Drug Des Devel Ther 6:165. https:\/\/doi.org\/10.2147\/DDDT.S24754","journal-title":"Drug Des Devel Ther"},{"key":"12578_CR35","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1016\/S0041-0101(97)00160-8","volume":"36","author":"J-P Chippaux","year":"1998","unstructured":"Chippaux J-P, Goyffon M (1998) Venoms, antivenoms and immunotherapy. Toxicon 36:823\u2013846. https:\/\/doi.org\/10.1016\/S0041-0101(97)00160-8","journal-title":"Toxicon"},{"key":"12578_CR36","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1016\/j.actatropica.2008.05.021","volume":"107","author":"J-P Chippaux","year":"2008","unstructured":"Chippaux J-P, Goyffon M (2008) Epidemiology of scorpionism: a global appraisal. Acta Trop 107:71\u201379. https:\/\/doi.org\/10.1016\/j.actatropica.2008.05.021","journal-title":"Acta Trop"},{"key":"12578_CR37","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1007\/PL00009037","volume":"20","author":"A Cockshott","year":"1999","unstructured":"Cockshott A, Bogle I (1999) Modelling the effects of glucose feeding on a recombinant E-coli fermentation. Bioprocess Eng 20:83\u201390. https:\/\/doi.org\/10.1007\/PL00009037","journal-title":"Bioprocess Eng"},{"key":"12578_CR38","doi-asserted-by":"publisher","first-page":"2807","DOI":"10.1128\/AAC.45.10.2807-2812.2001","volume":"45","author":"KE Conrath","year":"2001","unstructured":"Conrath KE, Lauwereys M, Galleni M, Matagne A, Fr\u00e8re J-M, Kinne J, Wyns L, Muyldermans S (2001) \u03b2-lactamase inhibitors derived from single-domain antibody fragments elicited in the Camelidae. Antimicrob Agents Chemother 45:2807\u20132812. https:\/\/doi.org\/10.1128\/AAC.45.10.2807-2812.2001","journal-title":"Antimicrob Agents Chemother"},{"key":"12578_CR39","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1080\/15563650601005787","volume":"45","author":"G D\u2019Suze","year":"2007","unstructured":"D\u2019Suze G, Moncada S, Gonz\u00e1lez C, Sevcik C, Alag\u00f3n A (2007) Antigenic cross-reactivity between sixteen venoms from scorpions belonging to six genera. Clin Toxicol 45:158\u2013163. https:\/\/doi.org\/10.1080\/15563650601005787","journal-title":"Clin Toxicol"},{"key":"12578_CR40","doi-asserted-by":"publisher","unstructured":"D\u2019Suze G, Castillo C, Sevcik C, Braz\u00f3n J, Malave C, Hernandez D, Zerpa N (2013) Scorpionism and dangerous species of Venezuela. In: Gopalakrishnakone P (eds) Toxinology. Springer, Dordrecht, pp 1\u201323. https:\/\/doi.org\/10.1007\/978-94-007-6647-1_24-1","DOI":"10.1007\/978-94-007-6647-1_24-1"},{"key":"12578_CR41","doi-asserted-by":"publisher","first-page":"412","DOI":"10.1016\/j.molimm.2015.10.002","volume":"68","author":"M Darvish","year":"2015","unstructured":"Darvish M, Behdani M, Shokrgozar MA, Pooshang-Bagheri K, Shahbazzadeh D (2015) Development of protective agent against Hottentotta saulcyi venom using camelid single-domain antibody. Mol Immunol 68:412\u2013420. https:\/\/doi.org\/10.1016\/j.molimm.2015.10.002","journal-title":"Mol Immunol"},{"key":"12578_CR42","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1016\/j.toxicon.2022.06.001","volume":"215","author":"B Das","year":"2022","unstructured":"Das B, Patra A, Puzari U, Deb P, Mukherjee AK (2022) In vitro laboratory analyses of commercial anti-scorpion (Mesobuthus tamulus) antivenoms reveal their quality and safety but the prevalence of a low proportion of venom-specific antibodies. Toxicon 215:37\u201348. https:\/\/doi.org\/10.1016\/j.toxicon.2022.06.001","journal-title":"Toxicon"},{"key":"12578_CR43","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1186\/1475-2859-8-26","volume":"8","author":"A de Marco","year":"2009","unstructured":"de Marco A (2009) Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. Microb Cell Fact 8:26. https:\/\/doi.org\/10.1186\/1475-2859-8-26","journal-title":"Microb Cell Fact"},{"key":"12578_CR44","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1186\/s12934-015-0320-7","volume":"14","author":"A de Marco","year":"2015","unstructured":"de Marco A (2015) Recombinant antibody production evolves into multiple options aimed at yielding reagents suitable for application-specific needs. Microb Cell Fact 14:125. https:\/\/doi.org\/10.1186\/s12934-015-0320-7","journal-title":"Microb Cell Fact"},{"key":"12578_CR45","first-page":"2645","volume":"8","author":"K Deffar","year":"2009","unstructured":"Deffar K, Shi H, Li L, Wang X, Zhu X (2009) Nanobodies - the new concept in antibody engineering. African J Biotechnol 8:2645\u20132652","journal-title":"African J Biotechnol"},{"key":"12578_CR46","doi-asserted-by":"publisher","first-page":"1015","DOI":"10.1016\/0041-0101(94)90383-2","volume":"32","author":"M Dehesa-D\u00e1vila","year":"1994","unstructured":"Dehesa-D\u00e1vila M, Possani LD (1994) Scorpionism and serotherapy in Mexico. Toxicon 32:1015\u20131018. https:\/\/doi.org\/10.1016\/0041-0101(94)90383-2","journal-title":"Toxicon"},{"key":"12578_CR47","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.jtcme.2014.11.007","volume":"5","author":"R Dehghani","year":"2015","unstructured":"Dehghani R, Arani MG (2015) Scorpion sting prevention and treatment in ancient Iran. J Tradit Complement Med 5:75\u201380. https:\/\/doi.org\/10.1016\/j.jtcme.2014.11.007","journal-title":"J Tradit Complement Med"},{"key":"12578_CR48","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1002\/(SICI)1097-0290(19991005)65:1<54::AID-BIT7>3.0.CO;2-R","volume":"65","author":"MP DeLisa","year":"1999","unstructured":"DeLisa MP, Li J, Rao G, Weigand W, a, Bentley WE, (1999) Monitoring GFP-operon fusion protein expression during high cell density cultivation of Escherichia coli using an on-line optical sensor. Biotechnol Bioeng 65:54\u201364. https:\/\/doi.org\/10.1002\/(SICI)1097-0290(19991005)65:1%3c54::AID-BIT7%3e3.0.CO;2-R","journal-title":"Biotechnol Bioeng"},{"key":"12578_CR49","doi-asserted-by":"publisher","first-page":"694","DOI":"10.1046\/j.1432-1327.2001.01923.x","volume":"268","author":"C Devaux","year":"2001","unstructured":"Devaux C, Moreau E, Goyffon M, Rochat H, Billiald P (2001) Construction and functional evaluation of a single-chain antibody fragment that neutralizes toxin Aahl from the venom of the scorpion Androctonus australis hector. Eur J Biochem 268:694\u2013702. https:\/\/doi.org\/10.1046\/j.1432-1327.2001.01923.x","journal-title":"Eur J Biochem"},{"key":"12578_CR50","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1007\/BF01569997","volume":"16","author":"RS Donovan","year":"1996","unstructured":"Donovan RS, Robinson CW, Glick BR (1996) Review: optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter. J Ind Microbiol 16:145\u2013154. https:\/\/doi.org\/10.1007\/BF01569997","journal-title":"J Ind Microbiol"},{"key":"12578_CR51","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1016\/0005-2760(92)90188-2","volume":"1165","author":"T Dudler","year":"1992","unstructured":"Dudler T, Chen WQ, Wang S, Schneider T, Annand RR, Dempcy RO, Crameri R, Gmachl M, Suter M, Gelb MH (1992) High-level expression in Escherichia coli and rapid purification of enzymatically active honey bee venom phospholipase A2. Biochim Biophys Acta 1165:201\u2013210. https:\/\/doi.org\/10.1016\/0005-2760(92)90188-2","journal-title":"Biochim Biophys Acta"},{"key":"12578_CR52","first-page":"200","volume":"95","author":"B El Hafny","year":"2002","unstructured":"El Hafny B, Ghalim N (2002) Scorpion envenomations and antivenom therapy in Morocco. Bull La Soci\u00e9t\u00e9 Pathol Exot 95:200\u2013204","journal-title":"Bull La Soci\u00e9t\u00e9 Pathol Exot"},{"key":"12578_CR53","doi-asserted-by":"publisher","first-page":"6671","DOI":"10.1021\/bi00369a052","volume":"25","author":"M El Ayeb","year":"1986","unstructured":"El Ayeb M, Bahraoui EM, Granier C, Rochat H (1986) Use of antibodies specific to defined regions of scorpion.alpha.-toxin to study its interaction with its receptor site on the sodium channel. Biochemistry 25:6671\u20136678. https:\/\/doi.org\/10.1021\/bi00369a052","journal-title":"Biochemistry"},{"key":"12578_CR54","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1016\/j.molimm.2021.07.010","volume":"137","author":"G Fern\u00e1ndez-Taboada","year":"2021","unstructured":"Fern\u00e1ndez-Taboada G, Ria\u00f1o-Umbarila L, Olvera-Rodr\u00edguez A, G\u00f3mez-Ram\u00edrez IV, Losoya-Uribe LF, Becerril B (2021) The venom of the scorpion Centruroides limpidus, which causes the highest number of stings in Mexico, is neutralized by two recombinant antibody fragments. Mol Immunol 137:247\u2013255. https:\/\/doi.org\/10.1016\/j.molimm.2021.07.010","journal-title":"Mol Immunol"},{"key":"12578_CR55","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fimmu.2013.00217","volume":"4","author":"A Frenzel","year":"2013","unstructured":"Frenzel A, Hust M, Schirrmann T (2013) Expression of recombinant antibodies. Front Immunol 4:1\u201320. https:\/\/doi.org\/10.3389\/fimmu.2013.00217","journal-title":"Front Immunol"},{"key":"12578_CR56","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1007\/s13213-009-0014-7","volume":"60","author":"J Gao","year":"2010","unstructured":"Gao J, Wang Y, Liu Z, Wang Z (2010) Phage display and its application in vaccine design. Ann Microbiol 60:13\u201319. https:\/\/doi.org\/10.1007\/s13213-009-0014-7","journal-title":"Ann Microbiol"},{"key":"12578_CR57","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1016\/j.biotechadv.2008.10.006","volume":"27","author":"F Garcia-Ochoa","year":"2009","unstructured":"Garcia-Ochoa F, Gomez E (2009) Bioreactor scale-up and oxygen transfer rate in microbial processes: an overview. Biotechnol Adv 27:153\u2013176. https:\/\/doi.org\/10.1016\/j.biotechadv.2008.10.006","journal-title":"Biotechnol Adv"},{"key":"12578_CR58","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1016\/j.bej.2010.01.011","volume":"49","author":"F Garcia-Ochoa","year":"2010","unstructured":"Garcia-Ochoa F, Gomez E, Santos VE, Merchuk JC (2010) Oxygen uptake rate in microbial processes: an overview. Biochem Eng J 49:289\u2013307. https:\/\/doi.org\/10.1016\/j.bej.2010.01.011","journal-title":"Biochem Eng J"},{"key":"12578_CR59","doi-asserted-by":"publisher","first-page":"277","DOI":"10.4269\/ajtmh.2000.62.277","volume":"62","author":"N Ghalim","year":"2000","unstructured":"Ghalim N, El-Hafny B, Sebti F, Heikel J, Lazar N, Moustanir R, Benslimane A (2000) Scorpion envenomation and serotherapy in Morocco. Am J Trop Med Hyg 62:277\u2013283. https:\/\/doi.org\/10.4269\/ajtmh.2000.62.277","journal-title":"Am J Trop Med Hyg"},{"key":"12578_CR60","doi-asserted-by":"publisher","first-page":"164","DOI":"10.1002\/biot.200500051","volume":"1","author":"K Graumann","year":"2006","unstructured":"Graumann K, Premstaller A (2006) Manufacturing of recombinant therapeutic proteins in microbial systems. Biotechnol J 1:164\u2013186. https:\/\/doi.org\/10.1002\/biot.200500051","journal-title":"Biotechnol J"},{"key":"12578_CR61","doi-asserted-by":"publisher","first-page":"31","DOI":"10.3109\/1040841X.2016.1150959","volume":"43","author":"SK Gupta","year":"2017","unstructured":"Gupta SK, Shukla P (2017a) Microbial platform technology for recombinant antibody fragment production: a review. Crit Rev Microbiol 43:31\u201342. https:\/\/doi.org\/10.3109\/1040841X.2016.1150959","journal-title":"Crit Rev Microbiol"},{"key":"12578_CR62","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fphar.2017.00419","volume":"8","author":"SK Gupta","year":"2017","unstructured":"Gupta SK, Shukla P (2017b) Sophisticated cloning, fermentation, and purification technologies for an enhanced therapeutic protein production: a review. Front Pharmacol 8:1\u201317. https:\/\/doi.org\/10.3389\/fphar.2017.00419","journal-title":"Front Pharmacol"},{"key":"12578_CR63","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1089\/153685903771797048","volume":"22","author":"S Hamilton","year":"2003","unstructured":"Hamilton S, Odili J, Pacifico MD, Wilson GD, Kupsch JM (2003) Effect of imidazole on the solubility of a his-tagged antibody fragment. Hybrid Hybridomics 22:347\u2013355. https:\/\/doi.org\/10.1089\/153685903771797048","journal-title":"Hybrid Hybridomics"},{"key":"12578_CR64","first-page":"297","volume":"96","author":"D Hammoudi-Triki","year":"2003","unstructured":"Hammoudi-Triki D, Laraba-Djebari F (2003) Application of ELISA for the quantification of Androctonus australis hector venom in the envenomed serum of people and rats before and after immunotherapy. Bull Soc Pathol Exot 96:297\u2013301","journal-title":"Bull Soc Pathol Exot"},{"key":"12578_CR65","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1016\/j.bbrc.2016.09.047","volume":"482","author":"T Han","year":"2017","unstructured":"Han T, Ming H, Deng L, Zhu H, Liu Z, Zhang J, Song Y (2017) A novel expression vector for the improved solubility of recombinant scorpion venom in Escherichia coli. Biochem Biophys Res Commun 482:120\u2013125. https:\/\/doi.org\/10.1016\/j.bbrc.2016.09.047","journal-title":"Biochem Biophys Res Commun"},{"key":"12578_CR66","doi-asserted-by":"publisher","first-page":"1013","DOI":"10.2217\/nnm.13.86","volume":"8","author":"G Hassanzadeh-Ghassabeh","year":"2013","unstructured":"Hassanzadeh-Ghassabeh G, Devoogdt N, De Pauw P, Vincke C, Muyldermans S (2013) Nanobodies and their potential applications. Nanomedicine 8:1013\u20131026. https:\/\/doi.org\/10.2217\/nnm.13.86","journal-title":"Nanomedicine"},{"key":"12578_CR67","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1007\/s13149-012-0234-4","volume":"105","author":"H Hellal","year":"2012","unstructured":"Hellal H, Guerinik M, Griene L, Laid Y, Mesbah S, Merad R, Alamir B (2012) Donn\u00e9es \u00e9pid\u00e9miologiques sur l\u2019envenimation scorpionique en Alg\u00e9rie. Bull Soc Pathol Exot 105:189\u2013193. https:\/\/doi.org\/10.1007\/s13149-012-0234-4","journal-title":"Bull Soc Pathol Exot"},{"key":"12578_CR68","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1083\/jcb.201409074","volume":"209","author":"J Helma","year":"2015","unstructured":"Helma J, Cardoso MC, Muyldermans S, Leonhardt H (2015) Nanobodies and recombinant binders in cell biology. J Cell Biol 209:633\u2013644. https:\/\/doi.org\/10.1083\/jcb.201409074","journal-title":"J Cell Biol"},{"key":"12578_CR69","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fphar.2022.821181","volume":"13","author":"R Hmaidi","year":"2022","unstructured":"Hmaidi R, Ksouri A, Benabderrazek R, Antonietti V, Sonnet P, Gautier M, Bouhaouala-Zahar B, Ouadid-Ahidouch H (2022) The pharmacological and structural basis of the AahII\u2013NaV1.5 interaction and modulation by the anti-AahII Nb10 nanobody. Front Pharmacol 13:1\u201311. https:\/\/doi.org\/10.3389\/fphar.2022.821181","journal-title":"Front Pharmacol"},{"key":"12578_CR70","doi-asserted-by":"publisher","first-page":"3847","DOI":"10.1016\/j.molimm.2008.04.011","volume":"45","author":"I Hmila","year":"2008","unstructured":"Hmila I, Abdallah RBA-B, Saerens D, Benlasfar Z, Conrath K, El AM, Muyldermans S, Bouhaouala-Zahar B (2008) VHH, bivalent domains and chimeric heavy chain-only antibodies with high neutralizing efficacy for scorpion toxin AahI\u2019. Mol Immunol 45:3847\u20133856. https:\/\/doi.org\/10.1016\/j.molimm.2008.04.011","journal-title":"Mol Immunol"},{"key":"12578_CR71","doi-asserted-by":"publisher","first-page":"3479","DOI":"10.1096\/fj.09-148213","volume":"24","author":"I Hmila","year":"2010","unstructured":"Hmila I, Saerens D, Ben Abderrazek R, Vincke C, Abidi N, Benlasfar Z, Govaert J, El Ayeb M, Bouhaouala-Zahar B, Muyldermans S (2010) A bispecific nanobody to provide full protection against lethal scorpion envenoming. FASEB J 24:3479\u20133489. https:\/\/doi.org\/10.1096\/fj.09-148213","journal-title":"FASEB J"},{"key":"12578_CR72","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1016\/j.taap.2012.07.033","volume":"264","author":"I Hmila","year":"2012","unstructured":"Hmila I, Cosyns B, Tounsi H, Roosens B, Caveliers V, Ben AR, Boubaker S, Muyldermans S, El Ayeb M, Bouhaouala-Zahar B, Lahoutte T (2012) Pre-clinical studies of toxin-specific nanobodies: evidence of in vivo efficacy to prevent fatal disturbances provoked by scorpion envenoming. Toxicol Appl Pharmacol 264:222\u2013231. https:\/\/doi.org\/10.1016\/j.taap.2012.07.033","journal-title":"Toxicol Appl Pharmacol"},{"key":"12578_CR73","doi-asserted-by":"publisher","first-page":"646","DOI":"10.1006\/prep.1995.1085","volume":"6","author":"BJ Hoffman","year":"1995","unstructured":"Hoffman BJ, Broadwater JA, Johnson P, Harper J, Fox BG, Kenealy WR (1995) Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21(DE3): Process control yielding high levels of metal-incorporated, soluble protein. Protein Expr Purif 6:646\u2013654","journal-title":"Protein Expr Purif"},{"key":"12578_CR74","doi-asserted-by":"publisher","first-page":"4133","DOI":"10.1093\/nar\/19.15.4133","volume":"19","author":"HR Hoogenboom","year":"1991","unstructured":"Hoogenboom HR, Griffiths AD, Johnson KS, Chiswell DJ, Hudson P, Winter G (1991) Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res 19:4133\u20134137. https:\/\/doi.org\/10.1093\/nar\/19.15.4133","journal-title":"Nucleic Acids Res"},{"key":"12578_CR75","doi-asserted-by":"publisher","first-page":"1269","DOI":"10.1007\/s00449-012-0714-4","volume":"35","author":"ACL Horta","year":"2012","unstructured":"Horta ACL, Sargo CR, Da Silva AJ, De Carvalho GM, Dos Santos MP, Gon\u00e7alves VM, Zangirolami TC, De Campos GR (2012) Intensification of high cell-density cultivations of rE. coli for production of S. pneumoniae antigenic surface protein, PspA3, using model-based adaptive control. Bioprocess Biosyst Eng 35:1269\u20131280. https:\/\/doi.org\/10.1007\/s00449-012-0714-4","journal-title":"Bioprocess Biosyst Eng"},{"key":"12578_CR76","doi-asserted-by":"publisher","first-page":"821","DOI":"10.1590\/0104-6632.20150324s00003534","volume":"32","author":"ACL Horta","year":"2015","unstructured":"Horta ACL, Da Silva AJ, Sargo CR, Cavalcanti-Monta\u00f1o ID, Galeano-Suarez ID, Velez AM, Santos MP, Gon\u00e7alves VM, Giordano RC, Zangirolami TC (2015) On-line monitoring of biomass concentration based on a capacitance sensor: assessing the methodology for different bacteria and yeast high cell density fed-batch cultures. Braz J Chem Eng 32:821\u2013829. https:\/\/doi.org\/10.1590\/0104-6632.20150324s00003534","journal-title":"Braz J Chem Eng"},{"key":"12578_CR77","doi-asserted-by":"publisher","first-page":"242","DOI":"10.1016\/S1004-9541(06)60065-7","volume":"14","author":"X Hua","year":"2006","unstructured":"Hua X, Fan D, Luo Y, Zhang X, Shi H, Mi Y, Ma X, Shang L, Zhao G (2006) Kinetics of high cell density fed-batch culture of recombinant Escherichia coli producing human-like collagen. Chin J Chem Eng 14:242\u2013247. https:\/\/doi.org\/10.1016\/S1004-9541(06)60065-7","journal-title":"Chin J Chem Eng"},{"key":"12578_CR78","doi-asserted-by":"publisher","first-page":"383","DOI":"10.1007\/s10295-011-1082-9","volume":"39","author":"C-J Huang","year":"2012","unstructured":"Huang C-J, Lin H, Yang X (2012) Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements. J Ind Microbiol Biotechnol 39:383\u2013399. https:\/\/doi.org\/10.1007\/s10295-011-1082-9","journal-title":"J Ind Microbiol Biotechnol"},{"key":"12578_CR79","doi-asserted-by":"publisher","first-page":"825","DOI":"10.1016\/0041-0101(95)00005-7","volume":"33","author":"M Ismail","year":"1995","unstructured":"Ismail M (1995) The scorpion envenoming syndrome. Toxicon 33:825\u2013858. https:\/\/doi.org\/10.1016\/0041-0101(95)00005-7","journal-title":"Toxicon"},{"key":"12578_CR80","doi-asserted-by":"publisher","first-page":"5","DOI":"10.3390\/antib8010005","volume":"8","author":"L Jank","year":"2019","unstructured":"Jank L, Pinto-Espinoza C, Duan Y, Koch-Nolte F, Magnus T, Rissiek B (2019) Current approaches and future perspectives for nanobodies in stroke diagnostic and therapy. Antibodies 8:5. https:\/\/doi.org\/10.3390\/antib8010005","journal-title":"Antibodies"},{"key":"12578_CR81","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1093\/femsre\/fuab052","volume":"46","author":"W Jaroszewicz","year":"2022","unstructured":"Jaroszewicz W, Morcinek-Or\u0142owska J, Pierzynowska K, Gaffke L, W\u0119grzyn G (2022) Phage display and other peptide display technologies. FEMS Microbiol Rev 46:1\u201325. https:\/\/doi.org\/10.1093\/femsre\/fuab052","journal-title":"FEMS Microbiol Rev"},{"key":"12578_CR82","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1016\/j.jbiotec.2005.09.013","volume":"122","author":"M Jenzsch","year":"2006","unstructured":"Jenzsch M, Simutis R, Luebbert A (2006) Generic model control of the specific growth rate in recombinant Escherichia coli cultivations. J Biotechnol 122:483\u2013493. https:\/\/doi.org\/10.1016\/j.jbiotec.2005.09.013","journal-title":"J Biotechnol"},{"key":"12578_CR83","doi-asserted-by":"publisher","first-page":"767","DOI":"10.1016\/S0196-9781(00)00206-0","volume":"21","author":"TM Johnson","year":"2000","unstructured":"Johnson TM, Quick MW, Sakai TT, Krishna NR (2000) Expression of functional recombinant scorpion beta-neurotoxin Css II in E. coli. Peptides 21:767\u2013772. https:\/\/doi.org\/10.1016\/S0196-9781(00)00206-0","journal-title":"Peptides"},{"key":"12578_CR84","doi-asserted-by":"publisher","first-page":"1287","DOI":"10.1016\/j.jmb.2004.12.060","volume":"346","author":"VR Ju\u00e1rez-Gonz\u00e1lez","year":"2005","unstructured":"Ju\u00e1rez-Gonz\u00e1lez VR, Ria\u00f1o-Umbarila L, Quintero-Hern\u00e1ndez V, Olamendi-Portugal T, Ortiz-Le\u00f3n M, Ort\u00edz E, Possani LD, Becerril B (2005) Directed evolution, phage display and combination of evolved mutants: a strategy to recover the neutralization properties of the scFv version of BCF2 a neutralizing monoclonal antibody specific to scorpion toxin Cn2. J Mol Biol 346:1287\u20131297. https:\/\/doi.org\/10.1016\/j.jmb.2004.12.060","journal-title":"J Mol Biol"},{"key":"12578_CR85","doi-asserted-by":"publisher","first-page":"206","DOI":"10.1007\/s00018-006-6401-3","volume":"64","author":"M Juste","year":"2007","unstructured":"Juste M, Martin-Eauclaire MF, Devaux C, Billiald P, Aubrey N (2007) Using a recombinant bispecific antibody to block Na+-channel toxins protects against experimental scorpion envenoming. Cell Mol Life Sci 64:206\u2013218. https:\/\/doi.org\/10.1007\/s00018-006-6401-3","journal-title":"Cell Mol Life Sci"},{"key":"12578_CR86","doi-asserted-by":"publisher","unstructured":"Kangwa M, Yelemane V, Polat AN, Gorrepati KDD, Grasselli M, Fern\u00e1ndez-Lahore M (2015) High-level fed-batch fermentative expression of an engineered Staphylococcal protein A based ligand in E. coli: purification and characterization. AMB Express 5:70. https:\/\/doi.org\/10.1186\/s13568-015-0155-y","DOI":"10.1186\/s13568-015-0155-y"},{"key":"12578_CR87","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1016\/j.jbiosc.2012.09.015","volume":"115","author":"YP Khasa","year":"2013","unstructured":"Khasa YP, Khushoo A, Mukherjee KJ (2013) Enhancing toxic protein expression in Escherichia coli fed-batch culture using kinetic parameters: human granulocyte-macrophage colony-stimulating factor as a model system. J Biosci Bioeng 115:291\u2013297. https:\/\/doi.org\/10.1016\/j.jbiosc.2012.09.015","journal-title":"J Biosci Bioeng"},{"key":"12578_CR88","doi-asserted-by":"publisher","first-page":"1019","DOI":"10.1016\/S0032-9592(00)00137-0","volume":"35","author":"BV Kilikian","year":"2000","unstructured":"Kilikian BV, Su\u00e1rez ID, Liria CW, Gombert AK (2000) Process strategies to improve heterologous protein production in Escherichia coli under lactose or IPTG induction. Process Biochem 35:1019\u20131025. https:\/\/doi.org\/10.1016\/S0032-9592(00)00137-0","journal-title":"Process Biochem"},{"key":"12578_CR89","doi-asserted-by":"publisher","first-page":"2425","DOI":"10.1007\/s12010-013-0708-y","volume":"172","author":"C-K Kim","year":"2014","unstructured":"Kim C-K, Choi J-H, Lee S-B, Lee S-M, Oh J-W (2014) Expression and purification of recombinant human granulocyte colony-stimulating factor in fed-batch culture of Escherichia coli. Appl Biochem Biotechnol 172:2425\u20132435. https:\/\/doi.org\/10.1007\/s12010-013-0708-y","journal-title":"Appl Biochem Biotechnol"},{"key":"12578_CR90","doi-asserted-by":"publisher","first-page":"621","DOI":"10.1016\/j.pep.2006.01.009","volume":"47","author":"S Kischnick","year":"2006","unstructured":"Kischnick S, Weber B, Verdino P, Keller W, Sanders EA, Anspach FB, Fiebig H, Cromwell O, Suck R (2006) Bacterial fermentation of recombinant major wasp allergen Antigen 5 using oxygen limiting growth conditions improves yield and quality of inclusion bodies. Protein Expr Purif 47:621\u2013628. https:\/\/doi.org\/10.1016\/j.pep.2006.01.009","journal-title":"Protein Expr Purif"},{"key":"12578_CR91","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1007\/BF00184684","volume":"35","author":"G Korte","year":"1991","unstructured":"Korte G, Rinas U, Kracke-Helm H-A, Sch\u00fcgerl K (1991) Structured model for cell growth and enzyme production by recombinant Escherichia coli. Appl Microbiol Biotechnol 35:185\u2013188. https:\/\/doi.org\/10.1007\/BF00184684","journal-title":"Appl Microbiol Biotechnol"},{"key":"12578_CR92","unstructured":"Kra\u00efem H, Manon Y, Hmila I, Ben Abderrazek R, Alonso Villela SM, Luc F, Bouhaouala-Zahar B (2019) Expression of the recombinant NbF12\u201310 and its chimeric antibody format in Escherichia Coli\u202f: investigation of fed-batch bioprocess on minimal media. In: Second Mediterranean Congress on Biotechnology. Hammamet, Tunisia"},{"key":"12578_CR93","doi-asserted-by":"publisher","first-page":"v4","DOI":"10.1093\/ndt\/gfl474","volume":"21","author":"M Kuhlmann","year":"2006","unstructured":"Kuhlmann M, Covic A (2006) The protein science of biosimilars. Nephrol Dial Transplant 21:v4\u2013v8. https:\/\/doi.org\/10.1093\/ndt\/gfl474","journal-title":"Nephrol Dial Transplant"},{"key":"12578_CR94","doi-asserted-by":"publisher","first-page":"922","DOI":"10.1002\/prca.201600002","volume":"10","author":"P Kuhn","year":"2016","unstructured":"Kuhn P, F\u00fchner V, Unkauf T, Moreira GMSG, Frenzel A, Miethe S, Hust M (2016) Recombinant antibodies for diagnostics and therapy against pathogens and toxins generated by phage display. Proteomics - Clin Appl 10:922\u2013948. https:\/\/doi.org\/10.1002\/prca.201600002","journal-title":"Proteomics - Clin Appl"},{"key":"12578_CR95","unstructured":"La\u00efd Y, Oudjehane R, Bachiri K (2012) Envenimation scorpionique: Rapport Annuel sur la situation epidemiologique en Alg\u00e9rie. Institut National de Sant\u00e9 Publique. https:\/\/insp.dz\/images\/PDF\/Envenimation%20scorpionique\/rapport_scorpion_2009.pdf. Accessed 29 Apr 2023"},{"key":"12578_CR96","doi-asserted-by":"publisher","unstructured":"Laustsen A, Sol\u00e0 M, Jappe E, Oscoz S, Lauridsen L, Engmark M (2016) Biotechnological Trends in Spider and Scorpion Antivenom Development. Toxins (Basel) 8:226. https:\/\/doi.org\/10.3390\/toxins8080226","DOI":"10.3390\/toxins8080226"},{"key":"12578_CR97","doi-asserted-by":"publisher","first-page":"264","DOI":"10.1016\/j.toxicon.2015.10.018","volume":"108","author":"Z Le","year":"2015","unstructured":"Le Z, Li X, Yuan P, Liu P, Huang C (2015) Orthogonal optimization of prokaryotic expression of a natural snake venom phospholipase A2 inhibitor from Sinonatrix annularis. Toxicon 108:264\u2013271. https:\/\/doi.org\/10.1016\/j.toxicon.2015.10.018","journal-title":"Toxicon"},{"key":"12578_CR98","doi-asserted-by":"publisher","first-page":"236","DOI":"10.3390\/toxins10060236","volume":"10","author":"L Ledsgaard","year":"2018","unstructured":"Ledsgaard L, Kilstrup M, Karatt-Vellatt A, McCafferty J, Laustsen A (2018) Basics of antibody phage display technology. Toxins (basel) 10:236. https:\/\/doi.org\/10.3390\/toxins10060236","journal-title":"Toxins (basel)"},{"key":"12578_CR99","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1385\/ABAB:135:1:81","volume":"135","author":"K-M Lee","year":"2006","unstructured":"Lee K-M, Rhee C-H, Kang C-K, Kim J-H (2006) Statistical medium formulation and process modeling by mixture design of experiment for peptide overexpression in recombinant Escherichia coli. Appl Biochem Biotechnol 135:81\u2013110","journal-title":"Appl Biochem Biotechnol"},{"key":"12578_CR100","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1016\/S0014-5793(97)01177-0","volume":"417","author":"C Legros","year":"1997","unstructured":"Legros C, Feyfant E, Sampieri F, Rochat H, Bougis PE, Martin-Eauclaire MF (1997) Influence of a NH2-terminal extension on the activity of KTX2, a K+ channel blocker purified from Androctonus australis scorpion venom. FEBS Lett 417:123\u2013129. https:\/\/doi.org\/10.1016\/S0014-5793(97)01177-0","journal-title":"FEBS Lett"},{"key":"12578_CR101","doi-asserted-by":"publisher","first-page":"934","DOI":"10.1016\/S0264-410X(01)00379-6","volume":"20","author":"C Legros","year":"2001","unstructured":"Legros C, Kaabi H, El Ayeb M, C\u00e9ard B, Vacher H, Bougis PE, Martin-Eauclaire M-F (2001) Use of fusion protein constructs to generate potent immunotherapy and protection against scorpion toxins. Vaccine 20:934\u2013942. https:\/\/doi.org\/10.1016\/S0264-410X(01)00379-6","journal-title":"Vaccine"},{"key":"12578_CR102","doi-asserted-by":"publisher","first-page":"1401","DOI":"10.1016\/j.ces.2007.11.022","volume":"63","author":"SSJ Leong","year":"2008","unstructured":"Leong SSJ, Chen WN (2008) Preparing recombinant single chain antibodies. Chem Eng Sci 63:1401\u20131414. https:\/\/doi.org\/10.1016\/j.ces.2007.11.022","journal-title":"Chem Eng Sci"},{"key":"12578_CR103","first-page":"25","volume":"78","author":"N Mansour","year":"2001","unstructured":"Mansour N (2001) Delai et caracteristiques de la prise en charge des piqu\u00e9s par scorpion dans la region de Sidi-Bouzid. Arch Inst Pasteur Tunis 78:25\u201331","journal-title":"Arch Inst Pasteur Tunis"},{"key":"12578_CR104","doi-asserted-by":"publisher","first-page":"899","DOI":"10.1002\/btpr.1567","volume":"28","author":"PA Marichal-Gallardo","year":"2012","unstructured":"Marichal-Gallardo PA, \u00c1lvarez MM (2012) State-of-the-art in downstream processing of monoclonal antibodies: process trends in design and validation. Biotechnol Prog 28:899\u2013916. https:\/\/doi.org\/10.1002\/btpr.1567","journal-title":"Biotechnol Prog"},{"key":"12578_CR105","doi-asserted-by":"publisher","first-page":"785","DOI":"10.1016\/j.toxicon.2003.10.021","volume":"42","author":"F Meddeb-Mouelhi","year":"2003","unstructured":"Meddeb-Mouelhi F, Bouhaouala-Zahar B, Benlasfar Z, Hammadi M, Mejri T, Moslah M, Karoui H, Khorchani T, El AM (2003) Immunized camel sera and derived immunoglobulin subclasses neutralizing Androctonus australis hector scorpion toxins. Toxicon 42:785\u2013791. https:\/\/doi.org\/10.1016\/j.toxicon.2003.10.021","journal-title":"Toxicon"},{"key":"12578_CR106","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1016\/j.biotechadv.2004.11.003","volume":"23","author":"FJM Mergulh\u00e3o","year":"2005","unstructured":"Mergulh\u00e3o FJM, Summers DK, Monteiro GA (2005) Recombinant protein secretion in Escherichia coli. Biotechnol Adv 23:177\u2013202. https:\/\/doi.org\/10.1016\/j.biotechadv.2004.11.003","journal-title":"Biotechnol Adv"},{"key":"12578_CR107","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1016\/j.biochi.2016.06.003","volume":"128\u2013129","author":"AM Morgon","year":"2016","unstructured":"Morgon AM, Belisario-Ferrari MR, Trevisan-Silva D, Meissner GO, Vuitika L, Marin B, Tashima AK, Gremski LH, Gremski W, Senff-Ribeiro A, Veiga SS, Chaim OM (2016) Expression and immunological cross-reactivity of LALP3, a novel astacin-like metalloprotease from brown spider (Loxosceles intermedia) venom. Biochimie 128\u2013129:8\u201319. https:\/\/doi.org\/10.1016\/j.biochi.2016.06.003","journal-title":"Biochimie"},{"key":"12578_CR108","doi-asserted-by":"publisher","first-page":"348","DOI":"10.1016\/S0304-4165(98)00090-7","volume":"1425","author":"M Mousli","year":"1998","unstructured":"Mousli M, Goyffon M, Billiald P (1998) Production and characterization of a bivalent single chain Fv\/alkaline phosphatase conjugate specific for the hemocyanin of the scorpion Androctonus australis. Biochim Biophys Acta - Gen Subj 1425:348\u2013360. https:\/\/doi.org\/10.1016\/S0304-4165(98)00090-7","journal-title":"Biochim Biophys Acta - Gen Subj"},{"key":"12578_CR109","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1016\/S0014-5793(98)01647-0","volume":"442","author":"M Mousli","year":"1999","unstructured":"Mousli M, Devaux C, Rochat H, Goyffon M, Billiald P (1999) A recombinant single-chain antibody fragment that neutralizes toxin II from the venom of the scorpion Androctonus australis hector. FEBS Lett 442:183\u2013188. https:\/\/doi.org\/10.1016\/S0014-5793(98)01647-0","journal-title":"FEBS Lett"},{"key":"12578_CR110","doi-asserted-by":"publisher","first-page":"775","DOI":"10.1146\/annurev-biochem-063011-092449","volume":"82","author":"S Muyldermans","year":"2013","unstructured":"Muyldermans S (2013) Nanobodies: natural single-domain antibodies. Annu Rev Biochem 82:775\u2013797. https:\/\/doi.org\/10.1146\/annurev-biochem-063011-092449","journal-title":"Annu Rev Biochem"},{"key":"12578_CR111","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1007\/s00449-005-0008-1","volume":"28","author":"M Nadri","year":"2006","unstructured":"Nadri M, Trezzani I, Hammouri H, Dhurjati P, Longin R, Lieto J (2006) Modeling and observer design for recombinant Escherichia coli strain. Bioprocess Biosyst Eng 28:217\u2013225. https:\/\/doi.org\/10.1007\/s00449-005-0008-1","journal-title":"Bioprocess Biosyst Eng"},{"key":"12578_CR112","doi-asserted-by":"publisher","first-page":"B35","DOI":"10.1016\/0300-9467(93)80056-T","volume":"52","author":"N Nancib","year":"1993","unstructured":"Nancib N, Mosrati R, Boudrant J (1993) Modelling of batch fermentation of a recombinant Escherichia coli producing glyceraldehyde-3-phosphate dehydrogenase on a complex selective medium. Chem Eng J 52:B35\u2013B48. https:\/\/doi.org\/10.1016\/0300-9467(93)80056-T","journal-title":"Chem Eng J"},{"key":"12578_CR113","unstructured":"Nuebling CM, Williams DJ (2016) Guidelines for the production, control and regulation of snake antivenom immunoglobulins. World Health Organization. https:\/\/www.who.int\/publications\/m\/item\/snake-antivenom-immunoglobulins-annex-5-trs-no-1004. Accessed 29 Apr 2023"},{"key":"12578_CR114","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1016\/j.bbagen.2013.08.021","volume":"1840","author":"AO O\u2019Reilly","year":"2014","unstructured":"O\u2019Reilly AO, Cole AR, Lopes JLS, Lampert A, Wallace BA (2014) Chaperone-mediated native folding of a \u03b2-scorpion toxin in the periplasm of Escherichia coli. Biochim Biophys Acta - Gen Subj 1840:10\u201315. https:\/\/doi.org\/10.1016\/j.bbagen.2013.08.021","journal-title":"Biochim Biophys Acta - Gen Subj"},{"key":"12578_CR115","doi-asserted-by":"publisher","first-page":"590","DOI":"10.1016\/j.drudis.2013.11.008","volume":"19","author":"TW Overton","year":"2014","unstructured":"Overton TW (2014) Recombinant protein production in bacterial hosts. Drug Discov Today 19:590\u2013601. https:\/\/doi.org\/10.1016\/j.drudis.2013.11.008","journal-title":"Drug Discov Today"},{"key":"12578_CR116","doi-asserted-by":"publisher","first-page":"390","DOI":"10.1590\/S1678-91992006000300004","volume":"12","author":"O Ozkan","year":"2006","unstructured":"Ozkan O, Adig\u00fczel S, Ates C, Bozyigit I, Filazi A (2006) Optimization of antiscorpion venom production. J Venom Anim Toxins Incl Trop Dis 12:390\u2013399. https:\/\/doi.org\/10.1590\/S1678-91992006000300004","journal-title":"J Venom Anim Toxins Incl Trop Dis"},{"key":"12578_CR117","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1002\/bit.10107","volume":"78","author":"MA Palaiomylitou","year":"2002","unstructured":"Palaiomylitou MA, Matis KA, Zouboulis AI, Kyriakidis DA (2002) A kinetic model describing cell growth and production of highly active, recombinant ice nucleation protein in Escherichia coli. Biotechnol Bioeng 78:321\u2013332. https:\/\/doi.org\/10.1002\/bit.10107","journal-title":"Biotechnol Bioeng"},{"key":"12578_CR118","doi-asserted-by":"publisher","first-page":"674","DOI":"10.1038\/nprot.2014.039","volume":"9","author":"E Pardon","year":"2014","unstructured":"Pardon E, Laeremans T, Triest S, Rasmussen SGF, Wohlk\u00f6nig A, Ruf A, Muyldermans S, Hol WGJ, Kobilka BK, Steyaert J (2014) A general protocol for the generation of Nanobodies for structural biology. Nat Protoc 9:674\u2013693. https:\/\/doi.org\/10.1038\/nprot.2014.039","journal-title":"Nat Protoc"},{"key":"12578_CR119","doi-asserted-by":"publisher","unstructured":"Pipelzadeh MH, Jalali A, Taraz M, Pourabbas R, Zaremirakabadi A (2007) An epidemiological and a clinical study on scorpionism by the Iranian scorpion Hemiscorpius lepturus. Toxicon 50:984\u2013992. https:\/\/doi.org\/10.1016\/j.toxicon.2007.07.018","DOI":"10.1016\/j.toxicon.2007.07.018"},{"key":"12578_CR120","doi-asserted-by":"crossref","unstructured":"Pucca MB, Oliveira FN, Schwartz EF, Arantes EC, Lira-da-Silva RM (2015) Scorpionism and Dangerous Species of Brazil. In: Scorpion Venoms, Toxinology. Springer Netherlands, Dordrecht, pp 299\u2013324","DOI":"10.1007\/978-94-007-6404-0_20"},{"key":"12578_CR121","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1016\/j.jmb.2012.01.038","volume":"417","author":"H Qi","year":"2012","unstructured":"Qi H, Lu H, Qiu H-J, Petrenko V, Liu A (2012) Phagemid vectors for phage display: properties, characteristics and construction. J Mol Biol 417:129\u2013143. https:\/\/doi.org\/10.1016\/j.jmb.2012.01.038","journal-title":"J Mol Biol"},{"key":"12578_CR122","doi-asserted-by":"publisher","unstructured":"Queiroz AM, Sampaio VS, Mendon\u00e7a I, F\u00e9 NF, Sachett J, Ferreira LCL, Feitosa E, Wen FH, Lacerda M, Monteiro W (2015) Severity of Scorpion Stings in the Western Brazilian Amazon: A Case-Control Study. PLoS One 10:e0128819. https:\/\/doi.org\/10.1371\/journal.pone.0128819","DOI":"10.1371\/journal.pone.0128819"},{"key":"12578_CR123","doi-asserted-by":"publisher","first-page":"1307","DOI":"10.1016\/j.molimm.2006.05.009","volume":"44","author":"V Quintero-Hern\u00e1ndez","year":"2007","unstructured":"Quintero-Hern\u00e1ndez V, Ju\u00e1rez-Gonz\u00e1lez VR, Ort\u00edz-Le\u00f3n M, S\u00e1nchez R, Possani LD, Becerril B (2007) The change of the scFv into the Fab format improves the stability and in vivo toxin neutralization capacity of recombinant antibodies. Mol Immunol 44:1307\u20131315. https:\/\/doi.org\/10.1016\/j.molimm.2006.05.009","journal-title":"Mol Immunol"},{"key":"12578_CR124","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1016\/j.imlet.2012.01.010","volume":"143","author":"V Quintero-Hern\u00e1ndez","year":"2012","unstructured":"Quintero-Hern\u00e1ndez V, Del Pozo-Yauner L, Pedraza-Escalona M, Ju\u00e1rez-Gonz\u00e1lez VR, Alc\u00e1ntara-Recillas I, Possani LD, Becerril B (2012) Evaluation of three different formats of a neutralizing single chain human antibody against toxin Cn2: neutralization capacity versus thermodynamic stability. Immunol Lett 143:152\u2013160. https:\/\/doi.org\/10.1016\/j.imlet.2012.01.010","journal-title":"Immunol Lett"},{"key":"12578_CR125","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/S1046-5928(02)00644-7","volume":"28","author":"OHP Ramos","year":"2003","unstructured":"Ramos OHP, Carmona AK, Selistre-de-Araujo HS (2003) Expression, refolding, and in vitro activation of a recombinant snake venom pro-metalloprotease. Protein Expr Purif 28:34\u201341. https:\/\/doi.org\/10.1016\/S1046-5928(02)00644-7","journal-title":"Protein Expr Purif"},{"key":"12578_CR126","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/j.pep.2008.05.018","volume":"61","author":"G Ravi","year":"2008","unstructured":"Ravi G, Ella K, Lakshmi Narasu M (2008) Development of pilot scale production process and characterization of a recombinant multiepitope malarial vaccine candidate FALVAC-1A expressed in Escherichia coli. Protein Expr Purif 61:57\u201364. https:\/\/doi.org\/10.1016\/j.pep.2008.05.018","journal-title":"Protein Expr Purif"},{"key":"12578_CR127","doi-asserted-by":"publisher","unstructured":"Rezende N., Amaral CF., Freire-Maia L (1998) Immunotherapy for scorpion envenoming in Brazil. Toxicon 36:1507\u20131513. https:\/\/doi.org\/10.1016\/S0041-0101(98)00141-X","DOI":"10.1016\/S0041-0101(98)00141-X"},{"key":"12578_CR128","doi-asserted-by":"publisher","first-page":"2591","DOI":"10.1111\/j.1742-4658.2005.04687.x","volume":"272","author":"L Ria\u00f1o-Umbarila","year":"2005","unstructured":"Ria\u00f1o-Umbarila L, Ju\u00e1rez-Gonz\u00e1lez VR, Olamendi-Portugal T, Ort\u00edz-Le\u00f3n M, Possani LD, Becerril B (2005) A strategy for the generation of specific human antibodies by directed evolution and phage display. FEBS J 272:2591\u20132601. https:\/\/doi.org\/10.1111\/j.1742-4658.2005.04687.x","journal-title":"FEBS J"},{"key":"12578_CR129","doi-asserted-by":"publisher","first-page":"6143","DOI":"10.1074\/jbc.M110.189175","volume":"286","author":"L Ria\u00f1o-Umbarila","year":"2011","unstructured":"Ria\u00f1o-Umbarila L, Contreras-Ferrat G, Olamendi-Portugal T, Morelos-Ju\u00e1rez C, Corzo G, Possani LD, Becerril B (2011) Exploiting cross-reactivity to neutralize two different scorpion venoms with one single chain antibody fragment. J Biol Chem 286:6143\u20136151. https:\/\/doi.org\/10.1074\/jbc.M110.189175","journal-title":"J Biol Chem"},{"key":"12578_CR130","doi-asserted-by":"publisher","first-page":"370","DOI":"10.1016\/j.toxicon.2013.09.016","volume":"76","author":"L Ria\u00f1o-Umbarila","year":"2013","unstructured":"Ria\u00f1o-Umbarila L, Olamendi-Portugal T, Morelos-Ju\u00e1rez C, Gurrola GB, Possani LD, Becerril B (2013) A novel human recombinant antibody fragment capable of neutralizing Mexican scorpion toxins. Toxicon 76:370\u2013376. https:\/\/doi.org\/10.1016\/j.toxicon.2013.09.016","journal-title":"Toxicon"},{"key":"12578_CR131","doi-asserted-by":"publisher","first-page":"1619","DOI":"10.1074\/jbc.M115.685297","volume":"291","author":"L Ria\u00f1o-Umbarila","year":"2016","unstructured":"Ria\u00f1o-Umbarila L, Ledezma-Candanoza LM, Serrano-Posada H, Fern\u00e1ndez-Taboada G, Olamendi-Portugal T, Rojas-Trejo S, G\u00f3mez-Ram\u00edrez IV, Rudi\u00f1o-Pi\u00f1era E, Possani LD, Becerril B (2016) Optimal neutralization of Centruroides noxius venom is understood through a structural complex between two antibody fragments and the Cn2 toxin. J Biol Chem 291:1619\u20131630. https:\/\/doi.org\/10.1074\/jbc.M115.685297","journal-title":"J Biol Chem"},{"key":"12578_CR132","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1016\/j.molimm.2020.04.015","volume":"122","author":"L Ria\u00f1o-Umbarila","year":"2020","unstructured":"Ria\u00f1o-Umbarila L, Rojas-Trejo VM, Romero-Moreno JA, Costas M, Utrera-Esp\u00edndola I, Olamendi-Portugal T, Possani LD, Becerril B (2020) Comparative assessment of the VH-VL and VL-VH orientations of single-chain variable fragments of scorpion toxin-neutralizing antibodies. Mol Immunol 122:141\u2013147. https:\/\/doi.org\/10.1016\/j.molimm.2020.04.015","journal-title":"Mol Immunol"},{"key":"12578_CR133","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/toxins13100708","volume":"13","author":"L Ria\u00f1o-Umbarila","year":"2021","unstructured":"Ria\u00f1o-Umbarila L, Romero-Moreno JA, Ledezma-Candanoza LM, Olamendi-Portugal T, Possani LD, Becerril B (2021) Full neutralization of centruroides sculpturatus scorpion venom by combining two human antibody fragments. Toxins (basel) 13:1\u201313. https:\/\/doi.org\/10.3390\/toxins13100708","journal-title":"Toxins (basel)"},{"key":"12578_CR134","doi-asserted-by":"publisher","first-page":"102","DOI":"10.1016\/j.pep.2004.05.020","volume":"37","author":"PG Roberto","year":"2004","unstructured":"Roberto PG, Kashima S, Soares AM, Chioato L, Fa\u00e7a VM, Fuly AL, Astolfi-Filho S, Pereira JO, Fran\u00e7a SC (2004) Cloning and expression of an acidic platelet aggregation inhibitor phospholipase A2 cDNA from Bothrops jararacussu venom gland. Protein Expr Purif 37:102\u2013108. https:\/\/doi.org\/10.1016\/j.pep.2004.05.020","journal-title":"Protein Expr Purif"},{"key":"12578_CR135","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1016\/j.jmb.2012.07.007","volume":"423","author":"ER Rodr\u00edguez-Rodr\u00edguez","year":"2012","unstructured":"Rodr\u00edguez-Rodr\u00edguez ER, Ledezma-Candanoza LM, Contreras-Ferrat LG, Olamendi-Portugal T, Possani LD, Becerril B, Ria\u00f1o-Umbarila L (2012) A single mutation in framework 2 of the heavy variable domain improves the properties of a diabody and a related single-chain antibody. J Mol Biol 423:337\u2013350. https:\/\/doi.org\/10.1016\/j.jmb.2012.07.007","journal-title":"J Mol Biol"},{"key":"12578_CR136","doi-asserted-by":"publisher","first-page":"52","DOI":"10.1016\/j.toxicon.2016.05.011","volume":"119","author":"ER Rodr\u00edguez-Rodr\u00edguez","year":"2016","unstructured":"Rodr\u00edguez-Rodr\u00edguez ER, Olamendi-Portugal T, Serrano-Posada H, Arredondo-L\u00f3pez JN, G\u00f3mez-Ram\u00edrez I, Fern\u00e1ndez-Taboada G, Possani LD, Anguiano-Vega GA, Ria\u00f1o-Umbarila L, Becerril B (2016) Broadening the neutralizing capacity of a family of antibody fragments against different toxins from Mexican scorpions. Toxicon 119:52\u201363. https:\/\/doi.org\/10.1016\/j.toxicon.2016.05.011","journal-title":"Toxicon"},{"key":"12578_CR137","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fmicb.2014.00172","volume":"5","author":"GL Rosano","year":"2014","unstructured":"Rosano GL, Ceccarelli EA (2014) Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol 5:1\u201317. https:\/\/doi.org\/10.3389\/fmicb.2014.00172","journal-title":"Front Microbiol"},{"key":"12578_CR138","doi-asserted-by":"publisher","first-page":"1039","DOI":"10.1016\/j.procbio.2009.05.007","volume":"44","author":"J Ruiz","year":"2009","unstructured":"Ruiz J, Pinsach J, \u00c1lvaro G, Gonz\u00e1lez G, de Mas C, Resina D, L\u00f3pez-Sant\u00edn J (2009) Alternative production process strategies in E. coli improving protein quality and downstream yields. Process Biochem 44:1039\u20131045. https:\/\/doi.org\/10.1016\/j.procbio.2009.05.007","journal-title":"Process Biochem"},{"key":"12578_CR139","doi-asserted-by":"publisher","first-page":"82","DOI":"10.1016\/j.bej.2011.03.001","volume":"55","author":"J Ruiz","year":"2011","unstructured":"Ruiz J, Gonz\u00e1lez G, de Mas C, L\u00f3pez-Sant\u00edn J (2011) A semiempirical model to control the production of a recombinant aldolase in high cell density cultures of Escherichia coli. Biochem Eng J 55:82\u201391. https:\/\/doi.org\/10.1016\/j.bej.2011.03.001","journal-title":"Biochem Eng J"},{"key":"12578_CR140","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1371\/journal.pone.0075126","volume":"8","author":"V Salema","year":"2013","unstructured":"Salema V, Mar\u00edn E, Mart\u00ednez-Arteaga R, Ruano-Gallego D, Fraile S, Margolles Y, Teira X, Gutierrez C, Bodel\u00f3n G, Fern\u00e1ndez L\u00c1 (2013) Selection of single domain antibodies from immune libraries displayed on the surface of E. coli cells with two \u03b2-domains of opposite topologies. PLoS ONE 8:1\u201318. https:\/\/doi.org\/10.1371\/journal.pone.0075126","journal-title":"PLoS ONE"},{"key":"12578_CR141","doi-asserted-by":"publisher","first-page":"4576","DOI":"10.2741\/3024","volume":"13","author":"T Schirrmann","year":"2008","unstructured":"Schirrmann T, Al-Halabi L, D\u00fcbel S, Hust M (2008) Production systems for recombinant antibodies. Front Biosci 13:4576\u20134594","journal-title":"Front Biosci"},{"key":"12578_CR142","doi-asserted-by":"publisher","first-page":"1426","DOI":"10.1002\/btpr.2360","volume":"32","author":"A Schmideder","year":"2016","unstructured":"Schmideder A, Cremer JH, Weuster-Botz D (2016) Parallel steady state studies on a milliliter scale accelerate fed-batch bioprocess design for recombinant protein production with Escherichia coli. Biotechnol Prog 32:1426\u20131435. https:\/\/doi.org\/10.1002\/btpr.2360","journal-title":"Biotechnol Prog"},{"key":"12578_CR143","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1016\/j.ymeth.2014.02.031","volume":"70","author":"DJ Schofield","year":"2014","unstructured":"Schofield DJ, Lewis AR, Austin MJ (2014) Genetic methods of antibody generation and their use in immunohistochemistry. Methods 70:20\u201327. https:\/\/doi.org\/10.1016\/j.ymeth.2014.02.031","journal-title":"Methods"},{"key":"12578_CR144","unstructured":"Secretar\u00eda de Salud de M\u00e9xico (2014) Programa de Acci\u00f3n Espec\u00edfico: Prevenci\u00f3n y Control de la Intoxicaci\u00f3n por Picadura de Alacr\u00e1n 2013\u20132018. https:\/\/www.gob.mx\/salud\/documentos\/programa-de-accion-especifico-prevencion-y-control-de-la-intoxicacion-por-picadura-de-alacran-2013-2018. Accessed 29 Apr 2023"},{"key":"12578_CR145","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1093\/femsle\/fny162","volume":"365","author":"T Selas Casti\u00f1eiras","year":"2018","unstructured":"Selas Casti\u00f1eiras T, Williams SG, Hitchcock AG, Smith DC (2018) E. coli strain engineering for the production of advanced biopharmaceutical products. FEMS Microbiol Lett 365:1\u201310. https:\/\/doi.org\/10.1093\/femsle\/fny162","journal-title":"FEMS Microbiol Lett"},{"key":"12578_CR146","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1016\/j.toxicon.2003.10.015","volume":"43","author":"B Selisko","year":"2004","unstructured":"Selisko B, Cos\u00edo G, Garc\u00eda C, Becerril B, Possani LD, Horjales E (2004) Bacterial expression, purification and functional characterization of a recombinant chimeric Fab derived from murine mAb BCF2 that neutralizes the venom of the scorpion Centruroides noxius hoffmann. Toxicon 43:43\u201351. https:\/\/doi.org\/10.1016\/j.toxicon.2003.10.015","journal-title":"Toxicon"},{"key":"12578_CR147","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1007\/s10529-007-9499-y","volume":"30","author":"JH Shao","year":"2008","unstructured":"Shao JH, Wang YQ, Wu XY, Jiang R, Zhang R, Wu CF, Zhang JH (2008) Cloning, expression, and pharmacological activity of BmK AS, an active peptide from scorpion Buthus martensii Karsch. Biotechnol Lett 30:23\u201329. https:\/\/doi.org\/10.1007\/s10529-007-9499-y","journal-title":"Biotechnol Lett"},{"key":"12578_CR148","doi-asserted-by":"publisher","first-page":"1532","DOI":"10.1002\/biot.201000408","volume":"6","author":"C Sieblist","year":"2011","unstructured":"Sieblist C, Jenzsch M, Pohlscheidt M, L\u00fcbbert A (2011) Insights into large-scale cell-culture reactors: I. Liquid mixing and oxygen supply. Biotechnol J 6:1532\u20131546. https:\/\/doi.org\/10.1002\/biot.201000408","journal-title":"Biotechnol J"},{"key":"12578_CR149","doi-asserted-by":"publisher","unstructured":"Skerra A, Pluckthun A (1988) Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science (80- ) 240:1038\u20131041. https:\/\/doi.org\/10.1126\/science.3285470","DOI":"10.1126\/science.3285470"},{"key":"12578_CR150","doi-asserted-by":"publisher","first-page":"973","DOI":"10.1016\/S0022-3476(05)83196-8","volume":"124","author":"S Sofer","year":"1994","unstructured":"Sofer S, Shahak E, Gueron M (1994) Scorpion envenomation and antivenom therapy. J Pediatr 124:973\u2013978. https:\/\/doi.org\/10.1016\/S0022-3476(05)83196-8","journal-title":"J Pediatr"},{"key":"12578_CR151","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1016\/j.tibtech.2013.10.002","volume":"32","author":"O Spadiut","year":"2014","unstructured":"Spadiut O, Capone S, Krainer F, Glieder A, Herwig C (2014) Microbials for the production of monoclonal antibodies and antibody fragments. Trends Biotechnol 32:54\u201360. https:\/\/doi.org\/10.1016\/j.tibtech.2013.10.002","journal-title":"Trends Biotechnol"},{"key":"12578_CR152","doi-asserted-by":"publisher","first-page":"1076","DOI":"10.1016\/j.drudis.2016.04.003","volume":"21","author":"S Steeland","year":"2016","unstructured":"Steeland S, Vandenbroucke RE, Libert C (2016) Nanobodies as therapeutics: big opportunities for small antibodies. Drug Discov Today 21:1076\u20131113. https:\/\/doi.org\/10.1016\/j.drudis.2016.04.003","journal-title":"Drug Discov Today"},{"key":"12578_CR153","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1016\/S0041-0101(02)00393-8","volume":"41","author":"RD Theakston","year":"2003","unstructured":"Theakston RD, Warrell D, Griffiths E (2003) Report of a WHO workshop on the standardization and control of antivenoms. Toxicon 41:541\u2013557. https:\/\/doi.org\/10.1016\/S0041-0101(02)00393-8","journal-title":"Toxicon"},{"key":"12578_CR154","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1093\/jisesa\/iey081","volume":"18","author":"S Tobassum","year":"2018","unstructured":"Tobassum S, Tahir HM, Zahid MT, Gardner QA, Ahsan MM (2018) Effect of milking method, diet, and temperature on venom production in scorpions. J Insect Sci 18:1\u20137. https:\/\/doi.org\/10.1093\/jisesa\/iey081","journal-title":"J Insect Sci"},{"key":"12578_CR155","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1016\/S0032-9592(03)00077-3","volume":"39","author":"E Toksoy \u00d6ner","year":"2003","unstructured":"Toksoy \u00d6ner E, Kirdar B, \u00d6nsan ZI, \u00dclgen K\u00d6 (2003) Modeling of the induced expression for high-level production of a foreign protein by recombinant E. coli under the control of the T7 phage promoter. Process Biochem 39:315\u2013323. https:\/\/doi.org\/10.1016\/S0032-9592(03)00077-3","journal-title":"Process Biochem"},{"key":"12578_CR156","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1016\/0168-1656(94)90199-6","volume":"37","author":"K Tokugawa","year":"1994","unstructured":"Tokugawa K, Ishii T, Nakamura K, Masaki H, Uozumi T (1994) A model system for the continuous production of a heterologous protein using a novel secretion promoting factor which operates in Escherichia coli. J Biotechnol 37:33\u201337. https:\/\/doi.org\/10.1016\/0168-1656(94)90199-6","journal-title":"J Biotechnol"},{"key":"12578_CR157","doi-asserted-by":"publisher","first-page":"116","DOI":"10.1002\/cben.201600002","volume":"3","author":"NK Tripathi","year":"2016","unstructured":"Tripathi NK (2016) Production and purification of recombinant proteins from Escherichia coli. ChemBioEng Rev 3:116\u2013133. https:\/\/doi.org\/10.1002\/cben.201600002","journal-title":"ChemBioEng Rev"},{"key":"12578_CR158","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1002\/biot.201200018","volume":"8","author":"AL Tscheliessnig","year":"2013","unstructured":"Tscheliessnig AL, Konrath J, Bates R, Jungbauer A (2013) Host cell protein analysis in therapeutic protein bioprocessing - methods and applications. Biotechnol J 8:655\u2013670. https:\/\/doi.org\/10.1002\/biot.201200018","journal-title":"Biotechnol J"},{"key":"12578_CR159","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1006\/prep.1997.0724","volume":"10","author":"M Turkov","year":"1997","unstructured":"Turkov M, Rashi S, Noam Z, Gordon D, Ben KR, Stankiewicz M, Pelhate M, Gurevitz M (1997) In vitro folding and functional analysis of an anti-insect selective scorpion depressant neurotoxin produced in Escherichia coli. Protein Expr Purif 10:123\u2013131. https:\/\/doi.org\/10.1006\/prep.1997.0724","journal-title":"Protein Expr Purif"},{"key":"12578_CR160","doi-asserted-by":"publisher","first-page":"369","DOI":"10.3390\/toxins14060369","volume":"14","author":"H Valencia-Mart\u00ednez","year":"2022","unstructured":"Valencia-Mart\u00ednez H, Olamendi-Portugal T, Restano-Cassulini R, Serrano-Posada H, Zamudio F, Possani LD, Ria\u00f1o-Umbarila L, Becerril B (2022) Characterization of four medically important toxins from Centruroides huichol scorpion venom and its neutralization by a single recombinant antibody fragment. Toxins (basel) 14:369. https:\/\/doi.org\/10.3390\/toxins14060369","journal-title":"Toxins (basel)"},{"key":"12578_CR161","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/j.pep.2015.01.010","volume":"108","author":"S Vemula","year":"2015","unstructured":"Vemula S, Thunuguntla R, Dedaniya A, Kokkiligadda S, Palle C, Ronda SR (2015) Improved production and characterization of recombinant human granulocyte colony stimulating factor from E. coli under optimized downstream processes. Protein Expr Purif 108:62\u201372. https:\/\/doi.org\/10.1016\/j.pep.2015.01.010","journal-title":"Protein Expr Purif"},{"key":"12578_CR162","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1006\/prep.2000.1353","volume":"21","author":"RJ Ward","year":"2001","unstructured":"Ward RJ, De Oliveira AHC, Bortoleto RK, Rosa JC, Fa\u00e7a VM, Greene LJ (2001) Refolding and purification of bothropstoxin-I, a Lys49-phospholipase A2homologue, expressed as inclusion bodies in escherichia coli. Protein Expr Purif 21:134\u2013140. https:\/\/doi.org\/10.1006\/prep.2000.1353","journal-title":"Protein Expr Purif"},{"key":"12578_CR163","unstructured":"Warrell D, Gutierrez J-M, Padilla A (2007) Rabies and envenomings\u202f: a neglected public health issue\u202f: report of a Consultative Meeting. https:\/\/apps.who.int\/iris\/handle\/10665\/43858. Accessed 29 Apr 2023"},{"key":"12578_CR164","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1016\/0168-1656(92)90075-K","volume":"23","author":"XM Yang","year":"1992","unstructured":"Yang XM (1992) Optimization of a cultivation process for recombinant protein production by Escherichia coli. J Biotechnol 23:271\u2013289. https:\/\/doi.org\/10.1016\/0168-1656(92)90075-K","journal-title":"J Biotechnol"},{"key":"12578_CR165","first-page":"1550","volume":"10","author":"L Yee","year":"1992","unstructured":"Yee L, Blanch HW (1992) Recombinant protein expression in high cell density fed-batch cultures of Escherichia coli. Biotechnology (n y) 10:1550\u20131556","journal-title":"Biotechnology (n y)"},{"key":"12578_CR166","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1007\/s00449-004-0376-y","volume":"27","author":"ZY Zheng","year":"2005","unstructured":"Zheng ZY, Yao SJ, Lin DQ (2005) Using a kinetic model that considers cell segregation to optimize hEGF expression in fed-batch cultures of recombinant Escherichia coli. Bioprocess Biosyst Eng 27:143\u2013152. https:\/\/doi.org\/10.1007\/s00449-004-0376-y","journal-title":"Bioprocess Biosyst Eng"}],"container-title":["Applied Microbiology and Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00253-023-12578-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00253-023-12578-1\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00253-023-12578-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,6,30]],"date-time":"2023-06-30T05:02:29Z","timestamp":1688101349000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00253-023-12578-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,5,18]]},"references-count":166,"journal-issue":{"issue":"13","published-print":{"date-parts":[[2023,7]]}},"alternative-id":["12578"],"URL":"https:\/\/doi.org\/10.1007\/s00253-023-12578-1","relation":{},"ISSN":["0175-7598","1432-0614"],"issn-type":[{"value":"0175-7598","type":"print"},{"value":"1432-0614","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,5,18]]},"assertion":[{"value":"29 December 2022","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 May 2023","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 May 2023","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"18 May 2023","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"This article does not contain any studies with human participants or animals performed by any of the authors.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}},{"value":"The authors declare no competing interests.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}