{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:26:12Z","timestamp":1791296772510,"version":"4.1.0"},"reference-count":48,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,2,1]],"date-time":"2017-02-01T00:00:00Z","timestamp":1485907200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2017,2]]},"DOI":"10.1016\/j.toxicon.2016.12.010","type":"journal-article","created":{"date-parts":[[2016,12,23]],"date-time":"2016-12-23T08:19:27Z","timestamp":1482481167000},"page":"79-89","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":16,"special_numbering":"C","title":["Pitfalls to avoid when using phage display for snake toxins"],"prefix":"10.1016","volume":"126","author":[{"given":"Andreas Hougaard","family":"Laustsen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Line Pr\u00e6st","family":"Lauridsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2419-6469","authenticated-orcid":false,"given":"Bruno","family":"Lomonte","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mikael R\u00f8rdam","family":"Andersen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0479-8980","authenticated-orcid":false,"given":"Brian","family":"Lohse","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2016.12.010_bib1","doi-asserted-by":"crossref","first-page":"7978","DOI":"10.1073\/pnas.88.18.7978","article-title":"Assembly of combinatorial antibody libraries on phage surfaces: the gene III site","volume":"88","author":"Barbas","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.toxicon.2016.12.010_bib2","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/j.jim.2006.03.005","article-title":"A\u00a0fast mutagenesis procedure to recover soluble and functional scFvs containing amber stop codons from synthetic and semisynthetic antibody libraries","volume":"312","author":"Barderas","year":"2006","journal-title":"J.\u00a0Immunol. Methods"},{"key":"10.1016\/j.toxicon.2016.12.010_bib3","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1002\/prot.340080405","article-title":"Hormone phage: an enrichment method for variant proteins with altered binding properties","volume":"8","author":"Bass","year":"1990","journal-title":"Proteins"},{"key":"10.1016\/j.toxicon.2016.12.010_bib4","doi-asserted-by":"crossref","first-page":"3209","DOI":"10.1523\/JNEUROSCI.23-08-03209.2003","article-title":"Ligand-induced internalization of the p75 neurotrophin receptor: a slow route to the signaling endosome","volume":"23","author":"Bronfman","year":"2003","journal-title":"J.\u00a0Neurosci. Off. J. Soc. Neurosci."},{"key":"10.1016\/j.toxicon.2016.12.010_bib5","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1038\/7959","article-title":"Selection of high-affinity phage antibodies from phage display libraries","volume":"17","author":"Bruin","year":"1999","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.toxicon.2016.12.010_bib6","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.toxicon.2014.05.017","article-title":"A\u00a0neutralizing recombinant single chain antibody, scFv, against BaP1, A P-I hemorrhagic metalloproteinase from Bothrops asper snake venom","volume":"87","author":"Castro","year":"2014","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2016.12.010_bib7","doi-asserted-by":"crossref","first-page":"554","DOI":"10.3390\/toxins4070554","article-title":"Humanized-single domain antibodies (VH\/VHH) that bound specifically to Naja kaouthia phospholipase A2 and neutralized the enzymatic activity","volume":"4","author":"Chavanayarn","year":"2012","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2016.12.010_bib8","doi-asserted-by":"crossref","first-page":"165","DOI":"10.2147\/DDDT.S24754","article-title":"Emerging options for the management of scorpion stings","volume":"6","author":"Chippaux","year":"2012","journal-title":"Drug Des. devel. Ther."},{"key":"10.1016\/j.toxicon.2016.12.010_bib10","first-page":"1776","article-title":"Diversity of phage-displayed libraries of peptides during panning and amplification","volume":"16","author":"Derda","year":"2011","journal-title":"Mol. Basel Switz."},{"key":"10.1016\/j.toxicon.2016.12.010_bib11","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.toxicon.2013.05.005","article-title":"Bothropic antivenom based on monoclonal antibodies, is it possible?","volume":"71","author":"Frauches","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2016.12.010_bib12","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1038\/nbt1291-1373","article-title":"Fab assembly and enrichment in a monovalent phage display system","volume":"9","author":"Garrard","year":"1991","journal-title":"Biotechnol. Nat. Publ. Co."},{"key":"10.1016\/j.toxicon.2016.12.010_bib13","doi-asserted-by":"crossref","first-page":"369","DOI":"10.2174\/187152811797200669","article-title":"Antivenoms for snakebite envenomings","volume":"10","author":"Guti\u00e9rrez","year":"2011","journal-title":"Inflamm. Allergy Drug Targets"},{"key":"10.1016\/j.toxicon.2016.12.010_bib14","doi-asserted-by":"crossref","first-page":"2127","DOI":"10.1038\/nprot.2012.132","article-title":"Use of phage display to generate conformation-sensor recombinant antibodies","volume":"7","author":"Haque","year":"2012","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.toxicon.2016.12.010_bib15","doi-asserted-by":"crossref","first-page":"1648","DOI":"10.1016\/j.vaccine.2003.09.046","article-title":"Development of venom toxin-specific antibodies by DNA immunisation: rationale and strategies to improve therapy of viper envenoming","volume":"22","author":"Harrison","year":"2004","journal-title":"Vaccine"},{"key":"10.1016\/j.toxicon.2016.12.010_bib16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S1380-2933(98)00007-4","article-title":"Antibody phage display technology and its applications","volume":"4","author":"Hoogenboom","year":"1998","journal-title":"Immunotechnology"},{"key":"10.1016\/j.toxicon.2016.12.010_bib18","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.jprot.2008.12.007","article-title":"Human monoclonal ScFv neutralize lethal Thai cobra, Naja kaouthia, neurotoxin","volume":"72","author":"Kulkeaw","year":"2009","journal-title":"J.\u00a0Proteomics"},{"key":"10.1016\/j.toxicon.2016.12.010_bib19","series-title":"Recombinant Antivenoms","author":"Laustsen","year":"2016"},{"key":"10.1016\/j.toxicon.2016.12.010_bib20","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1080\/15569543.2016.1220397","article-title":"Toxin synergism in snake venoms","volume":"35","author":"Laustsen","year":"2016","journal-title":"Toxin Rev."},{"key":"10.1016\/j.toxicon.2016.12.010_bib21","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.toxicon.2015.03.001","article-title":"Snake venomics of monocled cobra (Naja kaouthia) and investigation of human IgG response against venom toxins","volume":"99","author":"Laustsen","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2016.12.010_bib22","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.toxicon.2015.07.008","article-title":"Danger in the reef: proteome, toxicity, and neutralization of the venom of the olive sea snake","volume":"107","author":"Laustsen","year":"2015","journal-title":"Aipysurus laevis, Toxicon"},{"key":"10.1016\/j.toxicon.2016.12.010_bib23","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.toxicon.2015.07.334","article-title":"Selecting key toxins for focused development of elapid snake antivenoms and inhibitors guided by a Toxicity Score","volume":"104","author":"Laustsen","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2016.12.010_bib24","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.jprot.2015.02.002","article-title":"Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: identification of key toxin targets for antivenom development","volume":"119","author":"Laustsen","year":"2015","journal-title":"J.\u00a0Proteomics"},{"key":"10.1016\/j.toxicon.2016.12.010_bib25","doi-asserted-by":"crossref","DOI":"10.2174\/1381612822666160623073438","article-title":"From fangs to pharmacology: the future of snakebite envenoming therapy","volume":"22","author":"Laustsen","year":"2016","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.toxicon.2016.12.010_bib26","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1038\/538041e","article-title":"Snakebites: costing recombinant antivenoms","volume":"538","author":"Laustsen","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.toxicon.2016.12.010_bib27","doi-asserted-by":"crossref","first-page":"226","DOI":"10.3390\/toxins8080226","article-title":"Biotechnological trends in spider and scorpion antivenom development","volume":"8","author":"Laustsen","year":"2016","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2016.12.010_bib28","doi-asserted-by":"crossref","first-page":"226","DOI":"10.3390\/toxins8080226","article-title":"Biotechnological trends in spider and scorpion antivenom development","volume":"8","author":"Laustsen","year":"2016","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2016.12.010_bib29","doi-asserted-by":"crossref","DOI":"10.3390\/toxins8090248","article-title":"Varespladib (LY315920) appears to be a potent, broad-spectrum, inhibitor of snake venom phospholipase A2 and a possible pre-referral treatment for envenomation","volume":"8","author":"Lewin","year":"2016","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2016.12.010_bib30","doi-asserted-by":"crossref","first-page":"10832","DOI":"10.1021\/bi00109a004","article-title":"Selecting high-affinity binding proteins by monovalent phage display","volume":"30","author":"Lowman","year":"1991","journal-title":"Biochem. (Mosc.)"},{"key":"10.1016\/j.toxicon.2016.12.010_bib17","series-title":"Phage Display of Peptides and Proteins","first-page":"261","article-title":"Phage display: factors affecting panning efficiency. Phage display of peptides and proteins: a laboratory manual","author":"McCafferty","year":"1996"},{"key":"10.1016\/j.toxicon.2016.12.010_bib31","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1038\/348552a0","article-title":"Phage antibodies: filamentous phage displaying antibody variable domains","volume":"348","author":"McCafferty","year":"1990","journal-title":"Nature"},{"key":"10.1016\/j.toxicon.2016.12.010_bib32","doi-asserted-by":"crossref","first-page":"1969","DOI":"10.1016\/0006-2952(95)02095-0","article-title":"Specificity and binding affinity of an anti-crotoxin combinatorial antibody selected from a phage-displayed library","volume":"50","author":"Meng","year":"1995","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.toxicon.2016.12.010_bib33","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nbt0409-331","article-title":"Development trends for therapeutic antibody fragments","volume":"27","author":"Nelson","year":"2009","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.toxicon.2016.12.010_bib34","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/0378-1119(88)90495-7","article-title":"Antibody-selectable filamentous fd phage vectors: affinity purification of target genes","volume":"73","author":"Parmley","year":"1988","journal-title":"Gene"},{"key":"10.1016\/j.toxicon.2016.12.010_bib35","doi-asserted-by":"crossref","first-page":"e69495","DOI":"10.1371\/journal.pone.0069495","article-title":"In\u00a0vivo neutralization of \u03b1-cobratoxin with high-affinity llama single-domain antibodies (VHHs) and a VHH-Fc antibody","volume":"8","author":"Richard","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1016\/j.toxicon.2016.12.010_bib36","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/S0958-1669(99)80016-0","article-title":"Phage-display technology \u2013 finding a needle in a vast molecular haystack","volume":"10","author":"Rodi","year":"1999","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.toxicon.2016.12.010_bib37","series-title":"Recombinant Neutralizing Antibodies, a New Generation of Antivenoms, in: Toxinology - Scorpion Venoms","first-page":"580","author":"Rodr\u00edguez Rodr\u00edguez","year":"2015"},{"key":"10.1016\/j.toxicon.2016.12.010_bib38","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.toxicon.2016.05.011","article-title":"Broadening the neutralizing capacity of a family of antibody fragments against different toxins from Mexican scorpions","volume":"119","author":"Rodr\u00edguez-Rodr\u00edguez","year":"2016","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2016.12.010_bib39","doi-asserted-by":"crossref","first-page":"160","DOI":"10.3109\/1547691X.2012.703253","article-title":"Human antibody fragments specific for Bothrops jararacussu venom reduce the toxicity of other Bothrops sp. venoms","volume":"10","author":"Roncolato","year":"2013","journal-title":"J.\u00a0Immunotoxicol."},{"key":"10.1016\/j.toxicon.2016.12.010_bib40","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.toxicon.2014.11.001","article-title":"Phage display as a novel promising antivenom therapy: a review","volume":"93","author":"Roncolato","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2016.12.010_bib41","doi-asserted-by":"crossref","first-page":"R254","DOI":"10.1186\/gb-2007-8-11-r254","article-title":"Application of phage display to high throughput antibody generation and characterization","volume":"8","author":"Schofield","year":"2007","journal-title":"Genome Biol."},{"key":"10.1016\/j.toxicon.2016.12.010_bib42","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1016\/S0958-1669(00)00152-X","article-title":"Phage display in pharmaceutical biotechnology","volume":"11","author":"Sidhu","year":"2000","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.toxicon.2016.12.010_bib43","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/j.toxicon.2006.11.023","article-title":"Isolation, characterization and pentamerization of alpha-cobrotoxin specific single-domain antibodies from a na\u03bfve phage display library: preliminary findings for antivenom development","volume":"49","author":"Stewart","year":"2007","journal-title":"Toxicon Off. J. Int. Soc. Toxinology"},{"key":"10.1016\/j.toxicon.2016.12.010_bib44","doi-asserted-by":"crossref","first-page":"1450","DOI":"10.1016\/j.bbagen.2006.04.008","article-title":"Expression of recombinant human antibody fragments capable of inhibiting the phospholipase and myotoxic activities of Bothrops jararacussu venom","volume":"1760","author":"Tamarozzi","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2016.12.010_bib45","doi-asserted-by":"crossref","first-page":"81","DOI":"10.2144\/000114256","article-title":"Introduction of plasmid encoding for rare tRNAs reduces amplification bias in phage display biopanning","volume":"58","author":"Umlauf","year":"2015","journal-title":"BioTechniques"},{"key":"10.1016\/j.toxicon.2016.12.010_bib46","doi-asserted-by":"crossref","first-page":"e184","DOI":"10.1371\/journal.pmed.0030184","article-title":"Bioinformatics and multiepitope DNA immunization to design rational snake antivenom","volume":"3","author":"Wagstaff","year":"2006","journal-title":"PLoS Med."},{"key":"10.1016\/j.toxicon.2016.12.010_bib9","series-title":"Rabies and Envenomings: a Neglected Public Health Issue: Report of a Consultative Meeting","author":"Warrell","year":"2007"},{"key":"10.1016\/j.toxicon.2016.12.010_bib47","doi-asserted-by":"crossref","first-page":"1735","DOI":"10.1016\/j.jprot.2011.05.027","article-title":"Ending the drought: new strategies for improving the flow of affordable, effective antivenoms in Asia and Africa","volume":"74","author":"Williams","year":"2011","journal-title":"J.\u00a0Proteomics."},{"key":"10.1016\/j.toxicon.2016.12.010_bib48","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.jim.2006.10.005","article-title":"A\u00a0fast and efficient procedure to produce scFvs specific for large macromolecular complexes","volume":"318","author":"Wu","year":"2007","journal-title":"J.\u00a0Immunol. Methods"}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010116306304?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010116306304?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,7,2]],"date-time":"2018-07-02T16:38:01Z","timestamp":1530549481000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010116306304"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,2]]},"references-count":48,"alternative-id":["S0041010116306304"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2016.12.010","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2017,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Pitfalls to avoid when using phage display for snake toxins","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2016.12.010","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}