{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,21]],"date-time":"2026-07-21T23:02:47Z","timestamp":1784674967485,"version":"3.55.0"},"reference-count":70,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,1,29]],"date-time":"2025-01-29T00:00:00Z","timestamp":1738108800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2025,1,29]],"date-time":"2025-01-29T00:00:00Z","timestamp":1738108800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100000691","name":"Academy of Medical Sciences","doi-asserted-by":"crossref","award":["SBF008\\1127"],"award-info":[{"award-number":["SBF008\\1127"]}],"id":[{"id":"10.13039\/501100000691","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Medical Research Council Impact Accelerator Account","award":["MR\/X502911\/1 to the Tropical Infectious Disease Consortium"],"award-info":[{"award-number":["MR\/X502911\/1 to the Tropical Infectious Disease Consortium"]}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["221780\/Z\/20\/Z"],"award-info":[{"award-number":["221780\/Z\/20\/Z"]}],"id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014013","name":"UKRI","doi-asserted-by":"crossref","award":["20197"],"award-info":[{"award-number":["20197"]}],"id":[{"id":"10.13039\/100014013","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000268","name":"BBSRC","doi-asserted-by":"crossref","award":["BB\/T001240\/1"],"award-info":[{"award-number":["BB\/T001240\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000266","name":"EPSRC","doi-asserted-by":"crossref","award":["V043811\/1"],"award-info":[{"award-number":["V043811\/1"]}],"id":[{"id":"10.13039\/501100000266","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Royal Society Wolfson Fellowship","award":["RSWF\\R1\\180013"],"award-info":[{"award-number":["RSWF\\R1\\180013"]}]},{"DOI":"10.13039\/501100000272","name":"NIHR","doi-asserted-by":"crossref","award":["NIHR2000907"],"award-info":[{"award-number":["NIHR2000907"]}],"id":[{"id":"10.13039\/501100000272","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000865","name":"Bill and Melinda Gates Foundation","doi-asserted-by":"publisher","award":["INV-048598"],"award-info":[{"award-number":["INV-048598"]}],"id":[{"id":"10.13039\/100000865","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000288","name":"Royal Society","doi-asserted-by":"crossref","award":["ICAO\\R1\\231068"],"award-info":[{"award-number":["ICAO\\R1\\231068"]}],"id":[{"id":"10.13039\/501100000288","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Parasites Vectors"],"abstract":"<jats:title>Abstract<\/jats:title>\n          <jats:p>Mosquitoes are responsible for the transmission of numerous pathogens, including <jats:italic>Plasmodium<\/jats:italic> parasites, arboviruses and filarial worms. They pose a significant risk to public health with over 200 million cases of malaria per annum and approximately 4 billion people at risk of arthropod-borne viruses (arboviruses). Mosquito populations are geographically expanding into temperate regions and their distribution is predicted to continue increasing. Mosquito symbionts, including fungi, bacteria and viruses, have desirable traits for mosquito disease control including spreading horizontally and vertically through mosquito populations and potentially colonising multiple important vector species. Paratransgenesis, genetic modification of mosquito symbionts with effectors to target the pathogen rather than the vector, is a promising strategy to prevent the spread of mosquito-borne diseases. A variety of effectors can be expressed but venom toxins are excellent effector candidates because they are target specific, potent and stable. However, the only toxins to be explored in mosquito paratransgenesis to date are scorpine and mutated phospholipase A2. To enhance the scope, effectiveness and durability of paratransgenesis, an expanded arsenal of effectors is required. This review discusses other potential toxin effectors for future paratransgenesis studies based on prior in vitro and in vivo antiparasitic and antiviral studies and highlights the need for further research and investment in this area. In terms of mosquito-borne diseases, paratransgenesis strategies have been developed to target <jats:italic>Plasmodium<\/jats:italic>. We postulate the potential to apply this principle to target arboviruses using antiviral toxin effectors.<\/jats:p>\n          <jats:p>\n            <jats:bold>Graphical Abstract<\/jats:bold>\n          <\/jats:p>","DOI":"10.1186\/s13071-025-06663-9","type":"journal-article","created":{"date-parts":[[2025,1,29]],"date-time":"2025-01-29T08:27:17Z","timestamp":1738139237000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Exploiting venom toxins in paratransgenesis to prevent mosquito-borne disease"],"prefix":"10.1186","volume":"18","author":[{"given":"Stephanie","family":"French","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rachael","family":"Da Silva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janet","family":"Storm","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christida E.","family":"Wastika","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"India","family":"Cullen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martijn ten","family":"Have","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Grant L.","family":"Hughes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cassandra M.","family":"Modahl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,1,29]]},"reference":[{"key":"6663_CR1","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1016\/j.pop.2018.05.001","volume":"45","author":"H Lee","year":"2018","unstructured":"Lee H, Halverson S, Ezinwa N. Mosquito-borne diseases. Prim Care. 2018;45:393\u2013407.","journal-title":"Prim Care"},{"key":"6663_CR2","unstructured":"World malaria report 2023. Geneva: World Health Organisation; 2023. Licence: CC BY-NC-SA 3.0 IGO."},{"key":"6663_CR3","unstructured":"Global arbovirus initiative: preparing for the next pandemic tackling mosquito-borne viruses with epidemic and pandemic potential. Geneva: World Health Organization; 2024. Licence: CC BY-NCSA 3.0 IGO."},{"key":"6663_CR4","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.envint.2015.09.007","volume":"86","author":"X Wu","year":"2016","unstructured":"Wu X, Lu Y, Zhou S, Chen L, Xu B. Impact of climate change on human infectious diseases: empirical evidence and human adaptation. Environ Int. 2016;86:14\u201323.","journal-title":"Environ Int"},{"key":"6663_CR5","doi-asserted-by":"publisher","first-page":"1371","DOI":"10.1007\/s40121-022-00647-3","volume":"11","author":"JC Semenza","year":"2022","unstructured":"Semenza JC, Rockl\u00f6v J, Ebi KL. Climate change and cascading risks from infectious disease. Infect Dis Ther. 2022;11:1371\u201390.","journal-title":"Infect Dis Ther"},{"key":"6663_CR6","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s40249-019-0565-1","volume":"8","author":"F Fouque","year":"2019","unstructured":"Fouque F, Reeder JC. Impact of past and on-going changes on climate and weather on vector-borne diseases transmission: a look at the evidence. Infect Dis Poverty. 2019;8:1\u20139.","journal-title":"Infect Dis Poverty"},{"key":"6663_CR7","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1007\/978-981-15-9456-4_7","volume-title":"Molecular identification of mosquito vectors and their management","author":"I Baitharu","year":"2020","unstructured":"Baitharu I, Shroff S, Naik PP, Sahu JK. Environmental management and sustainable control of mosquito vector: challenges and opportunities. In: Molecular identification of mosquito vectors and their management. Springer Singapore: Singapore; 2020. p. 129\u201347."},{"key":"6663_CR8","doi-asserted-by":"publisher","first-page":"3274","DOI":"10.1073\/pnas.94.7.3274","volume":"94","author":"RV Durvasula","year":"1997","unstructured":"Durvasula RV, Gumbs A, Panackal A, Kruglov O, Aksoy S, Merrifield RB, et al. Prevention of insect-borne disease: an approach using transgenic symbiotic bacteria. Proc Natl Acad Sci USA. 1997;94:3274\u20138.","journal-title":"Proc Natl Acad Sci USA"},{"key":"6663_CR9","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s13071-015-0959-2","volume":"8","author":"ABB Wilke","year":"2015","unstructured":"Wilke ABB, Marrelli MT. Paratransgenesis: a promising new strategy for mosquito vector control. Parasit Vectors. 2015;8:1\u20139.","journal-title":"Parasit Vectors"},{"key":"6663_CR10","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s13071-021-05132-3","volume":"15","author":"NA Ratcliffe","year":"2022","unstructured":"Ratcliffe NA, Furtado Pacheco JP, Dyson P, Castro HC, Gonzalez MS, Azambuja P, et al. Overview of paratransgenesis as a strategy to control pathogen transmission by insect vectors. Parasit Vectors. 2022;15:1\u201331.","journal-title":"Parasit Vectors"},{"key":"6663_CR11","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1016\/j.tree.2012.10.020","volume":"28","author":"NR Casewell","year":"2013","unstructured":"Casewell NR, W\u00fcster W, Vonk FJ, Harrison RA, Fry BG. Complex cocktails: the evolutionary novelty of venoms. Trends Ecol Evol. 2013;28:219\u201329.","journal-title":"Trends Ecol Evol"},{"key":"6663_CR12","doi-asserted-by":"publisher","DOI":"10.1242\/jeb.227348","volume":"225","author":"SP Mackessy","year":"2022","unstructured":"Mackessy SP. Venom production and secretion in reptiles. J Exp Biol. 2022;225:227348.","journal-title":"J Exp Biol"},{"key":"6663_CR13","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxcx.2022.100119","volume":"14","author":"JC Guido-Pati\u00f1o","year":"2022","unstructured":"Guido-Pati\u00f1o JC, Plisson F. Profiling hymenopteran venom toxins: protein families, structural landscape, biological activities, and pharmacological benefits. Toxicon X. 2022;14:100119.","journal-title":"Toxicon X"},{"key":"6663_CR14","doi-asserted-by":"publisher","first-page":"893","DOI":"10.1016\/S0300-9084(00)01166-4","volume":"82","author":"P Escoubas","year":"2000","unstructured":"Escoubas P, Diochot S, Corzo G. Structure and pharmacology of spider venom neurotoxins. Biochimie. 2000;82:893\u2013907.","journal-title":"Biochimie"},{"key":"6663_CR15","doi-asserted-by":"publisher","DOI":"10.1016\/j.phrs.2023.106978","volume":"197","author":"Z Xia","year":"2023","unstructured":"Xia Z, He D, Wu Y, Kwok HF, Cao Z. Scorpion venom peptides: molecular diversity, structural characteristics, and therapeutic use from channelopathies to viral infections and cancers. Pharmacol Res. 2023;197:106978.","journal-title":"Pharmacol Res"},{"key":"6663_CR16","first-page":"1","volume":"3","author":"JM Guti\u00e9rrez","year":"2017","unstructured":"Guti\u00e9rrez JM, Calvete JJ, Habib AG, Harrison RA, Williams DJ, Warrell DA. Snakebite envenoming. Nat Rev Dis Primers. 2017;3:1\u201321.","journal-title":"Nat Rev Dis Primers"},{"key":"6663_CR17","doi-asserted-by":"publisher","first-page":"2437","DOI":"10.1002\/ps.5452","volume":"75","author":"GF King","year":"2019","unstructured":"King GF. Tying pest insects in knots: the deployment of spider-venom-derived knottins as bioinsecticides. Pest Manag Sci. 2019;75:2437\u201345.","journal-title":"Pest Manag Sci"},{"key":"6663_CR18","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2023.124745","volume":"242","author":"JR Almeida","year":"2023","unstructured":"Almeida JR, Gomes A, Mendes B, Aguiar L, Ferreira M, Brioschi MBC, et al. Unlocking the potential of snake venom-based molecules against the malaria, chagas disease, and leishmaniasis triad. Int J Biol Macromol. 2023;242:124745.","journal-title":"Int J Biol Macromol"},{"key":"6663_CR19","doi-asserted-by":"publisher","first-page":"375","DOI":"10.3390\/toxins15060375","volume":"15","author":"ZM Salimo","year":"2023","unstructured":"Salimo ZM, Barros AL, Adri\u00e3o AAX, Rodrigues AM, Sartim MA, de Oliveira IS, et al. Toxins from animal venoms as a potential source of antimalarials: a comprehensive review. Toxins (Basel). 2023;15:375.","journal-title":"Toxins (Basel)"},{"key":"6663_CR20","doi-asserted-by":"publisher","first-page":"88","DOI":"10.2741\/s475","volume":"9","author":"RP Samy","year":"2017","unstructured":"Samy RP, Foo SL, Franco OL, Stiles BG, Kumar AP, Sethi G, et al. Identification of natural peptides as a new class of antimalarial drugs by in silico approaches. Front Biosci. 2017;9:88\u2013110.","journal-title":"Front Biosci"},{"key":"6663_CR21","first-page":"3634","volume":"23","author":"Y Utkin","year":"2022","unstructured":"Utkin Y, Siniavin A, Kasheverov I, Tsetlin V. Antiviral effects of animal toxins: is there a way to drugs? J Venom Anim Toxins Incl Trop Dis. 2022;23:3634.","journal-title":"J Venom Anim Toxins Incl Trop Dis"},{"key":"6663_CR22","first-page":"1","volume":"23","author":"\u00c9CG da Mata","year":"2017","unstructured":"da Mata \u00c9CG, Mour\u00e3o CBF, Rangel M, Schwartz EF. Antiviral activity of animal venom peptides and related compounds. J Venom Anim Toxins Includ Trop Dis. 2017;23:1\u201312.","journal-title":"J Venom Anim Toxins Includ Trop Dis"},{"key":"6663_CR23","doi-asserted-by":"publisher","first-page":"1763","DOI":"10.1007\/s00705-022-05494-8","volume":"167","author":"WG Lima","year":"2022","unstructured":"Lima WG, Maia CQ, de Carvalho TS, Leite GO, Brito JCM, God\u00f3i IPD, et al. Animal venoms as a source of antiviral peptides active against arboviruses: a systematic review. Arch Virol. 2022;167:1763\u201372.","journal-title":"Arch Virol"},{"key":"6663_CR24","doi-asserted-by":"publisher","first-page":"616","DOI":"10.1016\/j.ijbiomac.2020.07.178","volume":"164","author":"SC Teixeira","year":"2020","unstructured":"Teixeira SC, Borges BC, Oliveira VQ, Carregosa LS, Bastos LA, Santos IA, et al. Insights into the antiviral activity of phospholipases A2 (PLA2s) from snake venoms. Int J Biol Macromol. 2020;164:616\u201325.","journal-title":"Int J Biol Macromol"},{"key":"6663_CR25","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1111\/j.1365-3024.2006.00804.x","volume":"28","author":"MMA Whitten","year":"2006","unstructured":"Whitten MMA, Shiao SH, Levashina EA. Mosquito midguts and malaria: cell biology, compartmentalization and immunology. Parasite Immunol. 2006;28:121\u201330.","journal-title":"Parasite Immunol"},{"key":"6663_CR26","doi-asserted-by":"publisher","first-page":"595","DOI":"10.1016\/j.ijpara.2006.12.002","volume":"37","author":"MA Riehle","year":"2007","unstructured":"Riehle MA, Moreira CK, Lampe D, Lauzon C, Jacobs-Lorena M. Using bacteria to express and display anti-Plasmodium molecules in the mosquito midgut. Int J Parasitol. 2007;37:595\u2013603.","journal-title":"Int J Parasitol"},{"key":"6663_CR27","first-page":"1399","volume":"2017","author":"S Wang","year":"1979","unstructured":"Wang S, Dos-Santos ALA, Huang W, Liu KC, Oshaghi MA, Wei G, et al. Driving mosquito refractoriness to Plasmodium falciparum with engineered symbiotic bacteria. Science. 1979;2017:1399\u2013402.","journal-title":"Science"},{"key":"6663_CR28","doi-asserted-by":"publisher","first-page":"12734","DOI":"10.1073\/pnas.1204158109","volume":"109","author":"S Wang","year":"2012","unstructured":"Wang S, Ghosh AK, Bongio N, Stebbings KA, Lampe DJ, Jacobs-Lorena M. Fighting malaria with engineered symbiotic bacteria from vector mosquitoes. Proc Natl Acad Sci USA. 2012;109:12734\u20139.","journal-title":"Proc Natl Acad Sci USA"},{"key":"6663_CR29","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0143541","volume":"10","author":"NJ Bongio","year":"2015","unstructured":"Bongio NJ, Lampe DJ. Inhibition of Plasmodium berghei development in mosquitoes by effector proteins secreted from Asaia sp. bacteria using a novel native secretion signal. PLoS ONE. 2015;10:e0143541.","journal-title":"PLoS ONE"},{"key":"6663_CR30","doi-asserted-by":"publisher","first-page":"438","DOI":"10.1111\/mve.12045","volume":"28","author":"C De Freece","year":"2014","unstructured":"De Freece C, Damiani C, Valzano M, D\u2019Amelio S, Cappelli A, Ricci I, et al. Detection and isolation of the \u03b1-proteobacterium Asaia in Culex mosquitoes. Med Vet Entomol. 2014;28:438\u201342.","journal-title":"Med Vet Entomol"},{"key":"6663_CR31","doi-asserted-by":"publisher","first-page":"9047","DOI":"10.1073\/pnas.0610451104","volume":"104","author":"G Favia","year":"2007","unstructured":"Favia G, Ricci I, Damiani C, Raddadi N, Crotti E, Marzorati M, et al. Bacteria of the genus Asaia stably associate with Anopheles stephensi, an Asian malarial mosquito vector. Proc Natl Acad Sci USA. 2007;104:9047\u201351.","journal-title":"Proc Natl Acad Sci USA"},{"key":"6663_CR32","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s13071-021-05044-2","volume":"14","author":"CGT Maffo","year":"2021","unstructured":"Maffo CGT, Sandeu MM, Fadel AN, Tchouakui M, Nguete DN, Menze B, et al. Molecular detection and maternal transmission of a bacterial symbiont Asaia species in field-caught Anopheles mosquitoes from Cameroon. Parasit Vectors. 2021;14:1\u201311.","journal-title":"Parasit Vectors"},{"key":"6663_CR33","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s13071-018-2955-9","volume":"11","author":"A Rami","year":"2018","unstructured":"Rami A, Raz A, Zakeri S, Dinparast Djadid N. Isolation and identification of Asaia sp. in Anopheles spp. mosquitoes collected from Iranian malaria settings: steps toward applying paratransgenic tools against malaria. Parasit Vectors. 2018;11:1\u20138.","journal-title":"Parasit Vectors"},{"key":"6663_CR34","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1111\/j.1574-6941.2010.01012.x","volume":"75","author":"K Zouache","year":"2011","unstructured":"Zouache K, Raharimalala FN, Raquin V, Tran-Van V, Raveloson LHR, Ravelonandro P, et al. Bacterial diversity of field-caught mosquitoes, Aedes albopictus and Aedes aegypti, from different geographic regions of Madagascar. FEMS Microbiol Ecol. 2011;75:377\u201389.","journal-title":"FEMS Microbiol Ecol"},{"key":"6663_CR35","doi-asserted-by":"publisher","first-page":"7444","DOI":"10.1128\/AEM.01747-10","volume":"76","author":"B Chouaia","year":"2010","unstructured":"Chouaia B, Rossi P, Montagna M, Ricci I, Crotti E, Damiani C, et al. Molecular evidence for multiple infections as revealed by typing of Asaia bacterial symbionts of four mosquito species. Appl Environ Microbiol. 2010;76:7444\u201350.","journal-title":"Appl Environ Microbiol"},{"key":"6663_CR36","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002742","volume":"8","author":"A Boissi\u00e8re","year":"2012","unstructured":"Boissi\u00e8re A, Tchioffo MT, Bachar D, Abate L, Marie A, Nsango SE, et al. Midgut microbiota of the Malaria mosquito vector Anopheles gambiae and interactions with Plasmodium falciparum infection. PLoS Pathog. 2012;8:e1002742.","journal-title":"PLoS Pathog"},{"key":"6663_CR37","doi-asserted-by":"publisher","first-page":"1074","DOI":"10.1126\/science.1199115","volume":"331","author":"W Fang","year":"2011","unstructured":"Fang W, Vega-Rodr\u00edguez J, Ghosh AK, Jacobs-Lorena M, Kang A, St. Leger RJ. Development of transgenic fungi that kill human malaria parasites in mosquitoes. Science. 1979;2011:1074\u20137.","journal-title":"Science"},{"key":"6663_CR38","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41467-018-06580-9","volume":"9","author":"JL Shane","year":"2018","unstructured":"Shane JL, Grogan CL, Cwalina C, Lampe DJ. Blood meal-induced inhibition of vector-borne disease by transgenic microbiota. Nat Commun. 2018;9:1\u201310.","journal-title":"Nat Commun"},{"key":"6663_CR39","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1003790","volume":"9","author":"V Carter","year":"2013","unstructured":"Carter V, Underhill A, Baber I, Sylla L, Baby M, Larget-Thiery I, et al. Killer bee molecules: antimicrobial peptides as effector molecules to target sporogonic stages of Plasmodium. PLoS Pathog. 2013;9:e1003790.","journal-title":"PLoS Pathog"},{"key":"6663_CR40","doi-asserted-by":"publisher","first-page":"872","DOI":"10.1016\/j.bbapap.2009.12.017","volume":"1804","author":"S Zhu","year":"2010","unstructured":"Zhu S, Gao B, Aumelas A, del Carmen RM, Lanz-Mendoza H, Peigneur S, et al. MeuTXK\u03b21, a scorpion venom-derived two-domain potassium channel toxin-like peptide with cytolytic activity. Biochim Biophys Acta. 2010;1804:872\u201383.","journal-title":"Biochim Biophys Acta"},{"key":"6663_CR41","doi-asserted-by":"publisher","DOI":"10.1002\/psc.3296","volume":"27","author":"C Pedron","year":"2021","unstructured":"Pedron C, Silva A, Torres M, de Oliveira C, Andrade G, Cerchiaro G, et al. Net charge tuning modulates the antiplasmodial and anticancer properties of peptides derived from scorpion venom. J Pept Sci. 2021;27:e3296.","journal-title":"J Pept Sci"},{"key":"6663_CR42","doi-asserted-by":"publisher","first-page":"3427","DOI":"10.1016\/j.bbagen.2013.01.028","volume":"1830","author":"L S\u00e1nchez-V\u00e1squez","year":"2013","unstructured":"S\u00e1nchez-V\u00e1squez L, Silva-Sanchez J, Jim\u00e9nez-Vargas JM, Rodr\u00edguez-Romero A, Mu\u00f1oz-Garay C, Rodr\u00edguez MC, et al. Enhanced antimicrobial activity of novel synthetic peptides derived from vejovine and hadrurin. Biochim Biophys Acta Gen Subj. 2013;1830:3427\u201336.","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"6663_CR43","doi-asserted-by":"publisher","first-page":"3081","DOI":"10.1007\/s00018-008-8250-8","volume":"65","author":"R Carballar-Lejaraz\u00fa","year":"2008","unstructured":"Carballar-Lejaraz\u00fa R, Rodr\u00edguez MH, De La Cruz H-H, Ramos-Casta\u00f1eda J, Possani LD, Zurita-Ortega M, et al. Recombinant scorpine: a multifunctional antimicrobial peptide with activity against different pathogens. Cell Mol Life Sci. 2008;65:3081\u201392.","journal-title":"Cell Mol Life Sci"},{"key":"6663_CR44","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1016\/S0014-5793(00)01384-3","volume":"471","author":"R Conde","year":"2000","unstructured":"Conde R, Zamudio FZ, Rodr\u00edguez MH, Possani LD. Scorpine, an anti-malaria and anti-bacterial agent purified from scorpion venom. FEBS Lett. 2000;471:165\u20138.","journal-title":"FEBS Lett"},{"key":"6663_CR45","doi-asserted-by":"publisher","first-page":"4157","DOI":"10.1242\/jeb.204.23.4157","volume":"204","author":"H Zieler","year":"2001","unstructured":"Zieler H, Keister DB, Dvorak JA. A snake venom phospholipase A2 blocks malaria parasite development in the mosquito midgut by inhibiting ookinete association with the midgut surface. J Exp Biol. 2001;204:4157\u201367.","journal-title":"J Exp Biol"},{"key":"6663_CR46","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1111\/j.1365-2583.2008.00791.x","volume":"17","author":"FG Rodrigues","year":"2008","unstructured":"Rodrigues FG, Santos MN, De Carvalho TXT, Rocha BC, Riehle MA, Pimenta PFP, et al. Expression of a mutated phospholipase A2 in transgenic Aedes fluviatilis mosquitoes impacts Plasmodium gallinaceum development. Insect Mol Biol. 2008;17:175\u201383.","journal-title":"Insect Mol Biol"},{"key":"6663_CR47","doi-asserted-by":"publisher","first-page":"644","DOI":"10.1590\/0074-0276130597","volume":"109","author":"RC Smith","year":"2014","unstructured":"Smith RC, Vega-Rodr\u00edguez J, Jacobs-Lorena M. The Plasmodium bottleneck: malaria parasite losses in the mosquito vector. Mem Inst Oswaldo Cruz. 2014;109:644\u201361.","journal-title":"Mem Inst Oswaldo Cruz"},{"key":"6663_CR48","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fmicb.2019.02134","volume":"10","author":"M Delves","year":"2019","unstructured":"Delves M, Lafuente-Monasterio MJ, Upton L, Ruecker A, Leroy D, Gamo FJ, et al. Fueling open innovation for malaria transmission-blocking drugs: hundreds of molecules targeting early parasite mosquito stages. Front Microbiol. 2019;10:1\u201310.","journal-title":"Front Microbiol"},{"key":"6663_CR49","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1128\/CMR.15.3.355-364.2002","volume":"15","author":"FL Schuster","year":"2002","unstructured":"Schuster FL. Cultivation of Plasmodium spp. Clin Microbiol Rev. 2002;15:355\u201364.","journal-title":"Clin Microbiol Rev"},{"key":"6663_CR50","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1186\/s13071-021-05044-2","volume":"14","author":"CGT Maffo","year":"2021","unstructured":"Maffo CGT, Sandeu MM, Fadel AN, Tchouakui M, Nguete DN, Menze B, et al. Molecular detection and maternal transmission of a bacterial symbiont Asaia species in field-caught Anopheles mosquitoes from Cameroon. Parasit Vectors. 2021;14:539.","journal-title":"Parasit Vectors"},{"key":"6663_CR51","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1186\/s13071-018-2955-9","volume":"11","author":"A Rami","year":"2018","unstructured":"Rami A, Raz A, Zakeri S, Dinparast Djadid N. Isolation and identification of Asaia sp. in Anopheles spp. mosquitoes collected from Iranian malaria settings: Steps toward applying paratransgenic tools against malaria. Parasit Vectors. 2018;11:367.","journal-title":"Parasit Vectors"},{"key":"6663_CR52","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/v15030705","volume":"15","author":"MF Lee","year":"2023","unstructured":"Lee MF, Wu YS, Poh CL. Molecular mechanisms of antiviral agents against dengue virus. Viruses. 2023;15:1\u201337.","journal-title":"Viruses"},{"key":"6663_CR53","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/0169-4758(93)90142-3","volume":"9","author":"CB Beard","year":"1993","unstructured":"Beard CB, O\u2019Neill SL, Tesh RB, Richards FF, Aksoy S. Modification of arthropod vector competence via symbiotic bacteria. Parasitol Today. 1993;9:179\u201383.","journal-title":"Parasitol Today"},{"key":"6663_CR54","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.tiv.2023.105562","volume":"88","author":"EHV Dias","year":"2023","unstructured":"Dias EHV, de Sousa Simamoto BB, da Cunha Pereira DF, Ribeiro MSM, Santiago FM, de Oliveira F, et al. Effect of BaltPLA2, a phospholipase A2 from Bothrops alternatus snake venom, on the viability of cells infected with dengue virus. Toxicol In Vitro. 2023;88:1\u20136.","journal-title":"Toxicol In Vitro"},{"key":"6663_CR55","doi-asserted-by":"publisher","first-page":"1780","DOI":"10.3390\/toxins5101780","volume":"5","author":"AB Cecilio","year":"2013","unstructured":"Cecilio AB, Caldas S, De Oliveira RA, Santos ASB, Richardson M, Naumann GB, et al. Molecular characterization of Lys49 and Asp49 phospholipases A2 from snake venom and their antiviral activities against Dengue virus. Toxins (Basel). 2013;5:1780\u201398.","journal-title":"Toxins (Basel)"},{"key":"6663_CR56","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1016\/j.biologicals.2019.12.002","volume":"63","author":"H Brenes","year":"2020","unstructured":"Brenes H, Lor\u00eda GD, Lomonte B. Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper. Biologicals. 2020;63:48\u201352.","journal-title":"Biologicals"},{"key":"6663_CR57","doi-asserted-by":"publisher","first-page":"630","DOI":"10.1016\/j.ijbiomac.2022.12.102","volume":"227","author":"NM Cassani","year":"2023","unstructured":"Cassani NM, Santos IA, Grosche VR, Ferreira GM, Guevara-Vega M, Rosa RB, et al. Roles of Bothrops jararacussu toxins I and II: antiviral findings against Zika virus. Int J Biol Macromol. 2023;227:630\u201340.","journal-title":"Int J Biol Macromol"},{"key":"6663_CR58","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/v15051168","volume":"15","author":"GM Ayusso","year":"2023","unstructured":"Ayusso GM, Lima MLD, da Silva Sanches PR, Santos IA, Martins DOS, da Concei\u00e7\u00e3o PJP, et al. The dimeric peptide (KKYRYHLKPF)2K shows broad-spectrum antiviral activity by inhibiting different steps of chikungunya and zika virus infection. Viruses. 2023;15:1\u201317.","journal-title":"Viruses"},{"key":"6663_CR59","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0112351","volume":"9","author":"VD Muller","year":"2014","unstructured":"Muller VD, Soares RO, Dos S-J, Trabuco AC, Cintra AC, Figueiredo LT, et al. Phospholipase A2 isolated from the venom of Crotalus durissus terrificus inactivates dengue virus and other enveloped viruses by disrupting the viral envelope. PLoS ONE. 2014;9:e112351.","journal-title":"PLoS ONE"},{"key":"6663_CR60","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1016\/j.toxicon.2011.05.021","volume":"59","author":"VDM Muller","year":"2012","unstructured":"Muller VDM, Russo RR, Oliveira Cintra AC, Sartim MA, De Melo A-P, Figueiredo LTM, et al. Crotoxin and phospholipases A 2 from Crotalus durissus terrificus showed antiviral activity against dengue and yellow fever viruses. Toxicon. 2012;59:507\u201315.","journal-title":"Toxicon"},{"key":"6663_CR61","doi-asserted-by":"publisher","first-page":"1159","DOI":"10.1007\/s00705-019-04172-6","volume":"164","author":"RR Russo","year":"2019","unstructured":"Russo RR, dos Santos J\u00fanior NN, Cintra ACO, Figueiredo LTM, Sampaio SV, Aquino VH. Expression, purification and virucidal activity of two recombinant isoforms of phospholipase A 2 from Crotalus durissus terrificus venom. Arch Virol. 2019;164:1159\u201371.","journal-title":"Arch Virol"},{"key":"6663_CR62","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41598-021-88039-4","volume":"11","author":"IA Santos","year":"2021","unstructured":"Santos IA, Shimizu JF, de Oliveira DM, Martins DOS, Cardoso-Sousa L, Cintra ACO, et al. Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus. Sci Rep. 2021;11:1\u201312.","journal-title":"Sci Rep"},{"key":"6663_CR63","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-016-0028-x","volume":"7","author":"M Chen","year":"2017","unstructured":"Chen M, Aoki-Utsubo C, Kameoka M, Deng L, Terada Y, Kamitani W, et al. Broad-spectrum antiviral agents: secreted phospholipase A2 targets viral envelope lipid bilayers derived from the endoplasmic reticulum membrane. Sci Rep. 2017;7:1\u20138.","journal-title":"Sci Rep"},{"key":"6663_CR64","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1016\/j.toxicon.2020.12.007","volume":"191","author":"M Miyashita","year":"2021","unstructured":"Miyashita M, Mitani N, Kitanaka A, Yakio M, Chen M, Nishimoto S, et al. Identification of an antiviral component from the venom of the scorpion Liocheles australasiae using transcriptomic and mass spectrometric analyses. Toxicon. 2021;191:25\u201337.","journal-title":"Toxicon"},{"key":"6663_CR65","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fmicb.2020.01871","volume":"11","author":"M Xing","year":"2020","unstructured":"Xing M, Ji M, Hu J, Zhu T, Chen Y, Bai X, et al. Snake cathelicidin derived peptide inhibits zika virus infection. Front Microbiol. 2020;11:1\u201311.","journal-title":"Front Microbiol"},{"key":"6663_CR66","doi-asserted-by":"publisher","first-page":"811","DOI":"10.1007\/s10989-019-09888-2","volume":"26","author":"AMH El-Bitar","year":"2020","unstructured":"El-Bitar AMH, Sarhan M, Abdel-Rahman MA, Quintero-Hernandez V, Aoki-Utsubo C, Moustafa MA, et al. Smp76, a scorpine-Like peptide isolated from the venom of the scorpion Scorpio maurus palmatus, with a potent antiviral activity against hepatitis c virus and dengue virus. Int J Pept Res Ther. 2020;26:811\u201321.","journal-title":"Int J Pept Res Ther"},{"key":"6663_CR67","doi-asserted-by":"publisher","first-page":"545","DOI":"10.1007\/s12250-018-0068-4","volume":"33","author":"Z Ji","year":"2018","unstructured":"Ji Z, Li F, Xia Z, Guo X, Gao M, Sun F, et al. The scorpion venom peptide Smp76 inhibits viral infection by regulating Type-I interferon response. Virol Sin. 2018;33:545\u201356.","journal-title":"Virol Sin"},{"key":"6663_CR68","doi-asserted-by":"publisher","first-page":"182","DOI":"10.1074\/jbc.RA118.005015","volume":"294","author":"F Li","year":"2019","unstructured":"Li F, Lang Y, Ji Z, Xia Z, Han Y, Cheng Y, et al. A scorpion venom peptide Ev37 restricts viral late entry by alkalizing acidic organelles. J Biol Chem. 2019;294:182\u201394.","journal-title":"J Biol Chem"},{"key":"6663_CR69","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1111\/tra.12012","volume":"14","author":"J Flipse","year":"2013","unstructured":"Flipse J, Wilschut J, Smit JM. Molecular mechanisms involved in antibody-dependent enhancement of dengue virus infection in humans. Traffic. 2013;14:25\u201335.","journal-title":"Traffic"},{"key":"6663_CR70","doi-asserted-by":"publisher","first-page":"1112","DOI":"10.1038\/s41564-022-01190-0","volume":"7","author":"JM Fox","year":"2022","unstructured":"Fox JM, Pierson TC. Chikungunya virus assembly and egress. Nat Microbiol. 2022;7:1112\u20133.","journal-title":"Nat Microbiol"}],"container-title":["Parasites &amp; Vectors"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s13071-025-06663-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s13071-025-06663-9\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s13071-025-06663-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,1,29]],"date-time":"2025-01-29T09:13:15Z","timestamp":1738141995000},"score":1,"resource":{"primary":{"URL":"https:\/\/parasitesandvectors.biomedcentral.com\/articles\/10.1186\/s13071-025-06663-9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1,29]]},"references-count":70,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["6663"],"URL":"https:\/\/doi.org\/10.1186\/s13071-025-06663-9","relation":{},"ISSN":["1756-3305"],"issn-type":[{"value":"1756-3305","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,1,29]]},"assertion":[{"value":"25 September 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"7 January 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 January 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"The authors declare no competing interests.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"32"}}