{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T22:12:46Z","timestamp":1791065566063,"version":"4.1.0"},"reference-count":163,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T00:00:00Z","timestamp":1768953600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Science Foundation","award":["2146104"],"award-info":[{"award-number":["2146104"]}]},{"name":"National Science Foundation","award":["2127521"],"award-info":[{"award-number":["2127521"]}]},{"name":"Ohio State University"},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de pessoal de N\u00edvel Superior\u2014Brasil","doi-asserted-by":"crossref","award":["001"],"award-info":[{"award-number":["001"]}],"id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100005942","name":"Funda\u00e7\u00e3o Butantan","doi-asserted-by":"publisher","award":["001\/0708\/003.433\/2021"],"award-info":[{"award-number":["001\/0708\/003.433\/2021"]}],"id":[{"id":"10.13039\/501100005942","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Megalomyrmex ant species have a rich natural history that provides an interesting backdrop to understanding how venom has been shaped by evolution. However, like many other species in the tribe Solenopsidini, alkaloid investigations have dominated, limiting our understanding of the diversity of venom components. Here we use transcriptomics to qualify and quantify the proteins and peptides within Megalomyrmex milenae, a species of ant native to the Panamanian rainforest along the Panama Canal. RNA transcripts associated with and over-expressed in the venom gland allow the description of putative toxins and other significant protein components of the venom cocktail. Among other constituents, we find signatures for pore-forming toxins, neurotoxins, carbohydrate-digesting enzymes, proteins which potentially enhance trail pheromone efficacy, and peptides implicated in antimicrobial activity. This work greatly enhances our understanding of Megalomyrmex venoms, showing a multifaceted functional venom profile similar to other ant species. However, proteomic and functional assays are needed to clarify the venom functions hypothesized in this work.<\/jats:p>","DOI":"10.3390\/toxins18010055","type":"journal-article","created":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T15:31:46Z","timestamp":1769009506000},"page":"55","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Megalomyrmex milenae Transcriptome Reveals a Complex Venom Cocktail"],"prefix":"10.3390","volume":"18","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8313-8264","authenticated-orcid":false,"given":"Kyle S.","family":"Sozanski","sequence":"first","affiliation":[{"name":"Department of Evolution, Ecology, and Organismal Biology, The Ohio State University, Columbus, OH 43212, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9633-7219","authenticated-orcid":false,"given":"Guilherme R.","family":"Coelho","sequence":"additional","affiliation":[{"name":"Department of Evolution, Ecology, and Organismal Biology, The Ohio State University, Columbus, OH 43212, USA"},{"name":"Faculdade de Ci\u00eancias Farmac\u00eauticas de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5277-3046","authenticated-orcid":false,"given":"Marcela Akemi","family":"Ishihara","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Bioqu\u00edmica, Instituto Butantan, S\u00e3o Paulo 05585-000, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7874-0293","authenticated-orcid":false,"given":"Alonso","family":"Delgado","sequence":"additional","affiliation":[{"name":"Department of Evolution, Ecology, and Organismal Biology, The Ohio State University, Columbus, OH 43212, USA"},{"name":"Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, MA 02138, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0918-9861","authenticated-orcid":false,"given":"Rachelle M. M.","family":"Adams","sequence":"additional","affiliation":[{"name":"Department of Evolution, Ecology, and Organismal Biology, The Ohio State University, Columbus, OH 43212, USA"},{"name":"Smithsonian Tropical Research Institute, Smithsonian Institution, Anc\u00f3n, Panama City 0843-03092, Panama"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,1,21]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1042\/BCJ20160577","article-title":"Venomics: Integrative Venom Proteomics and Beyond","volume":"474","author":"Calvete","year":"2017","journal-title":"Biochem. J."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1736","DOI":"10.1016\/j.febslet.2009.03.029","article-title":"Venoms, Venomics, Antivenomics","volume":"583","author":"Calvete","year":"2009","journal-title":"FEBS Lett."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.jprot.2015.09.015","article-title":"Ecological Venomics: How Genomics, Transcriptomics and Proteomics Can Shed New Light on the Ecology and Evolution of Venom","volume":"135","author":"Sunagar","year":"2016","journal-title":"J. Proteom."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Bouzid, W., Verdenaud, M., Klopp, C., Ducancel, F., Noirot, C., and V\u00e9tillard, A. (2014). De Novo Sequencing and Transcriptome Analysis for Tetramorium bicarinatum: A Comprehensive Venom Gland Transcriptome Analysis from an Ant Species. BMC Genom., 15.","DOI":"10.1186\/1471-2164-15-987"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Delgado, A., Sozanski, K.S., and Daly, M. (2024). Towards the Exploration and Evolution of Insulin-like Venoms in Actiniaria (Sea Anemones). Mar. Drugs, 22.","DOI":"10.20944\/preprints202402.0590.v1"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"L\u00fcddecke, T., and Blank, S. (2024). Animal Toxins: Biodiscovery, Mechanistic Insights and Translational Potential. Toxins, 16.","DOI":"10.3390\/toxins16030130"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1964","DOI":"10.1093\/molbev\/msz125","article-title":"Many Options, Few Solutions: Over 60 My Snakes Converged on a Few Optimal Venom Formulations","volume":"36","author":"Barua","year":"2019","journal-title":"Mol. Biol. Evol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1146\/annurev.genom.9.081307.164356","article-title":"The Toxicogenomic Multiverse: Convergent Recruitment of Proteins into Animal Venoms","volume":"10","author":"Fry","year":"2009","journal-title":"Annu. Rev. Genom. Hum. Genet."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"e20210047","DOI":"10.1590\/1678-9199-jvatitd-2021-0047","article-title":"Overview of Protein Posttranslational Modifications in Arthropoda Venoms","volume":"28","author":"Moreira","year":"2022","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Xie, B., Dashevsky, D., Rokyta, D., Ghezellou, P., Fathinia, B., Shi, Q., Richardson, M.K., and Fry, B.G. (2022). Dynamic Genetic Differentiation Drives the Widespread Structural and Functional Convergent Evolution of Snake Venom Proteinaceous Toxins. BMC Biol., 20.","DOI":"10.1186\/s12915-021-01208-9"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Jackson, T.N.W., Jouanne, H., and Vidal, N. (2019). Snake Venom in Context: Neglected Clades and Concepts. Front. Ecol. Evol., 7.","DOI":"10.3389\/fevo.2019.00332"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3488","DOI":"10.3390\/toxins6123488","article-title":"Quo Vadis Venomics? A Roadmap to Neglected Venomous Invertebrates","volume":"6","author":"Campbell","year":"2014","journal-title":"Toxins"},{"key":"ref_13","unstructured":"Bolton, B. (2024, January 12). AntCat. Available online: https:\/\/antcat.org\/."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"107006","DOI":"10.1016\/j.toxicon.2022.107006","article-title":"Transcriptomic and Biochemical Analysis from the Venom Gland of the Neotropical Ant Odontomachus chelifer","volume":"223","author":"Ferro","year":"2023","journal-title":"Toxicon"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Kazuma, K., Masuko, K., Konno, K., and Inagaki, H. (2017). Combined Venom Gland Transcriptomic and Venom Peptidomic Analysis of the Predatory Ant Odontomachus monticola. Toxins, 9.","DOI":"10.3390\/toxins9100323"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Aili, S.R., Touchard, A., Hayward, R., Robinson, S.D., Pineda, S.S., Lalag\u00fce, H., Vetter, I., Undheim, E.A.B., and Kini, R.M. (2020). An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant Paraponera clavata. Toxins, 12.","DOI":"10.3390\/toxins12050324"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Torres, A.F.C., Huang, C., Chong, C.-M., Leung, S.W., Prieto-da-Silva, \u00c1.R.B., Havt, A., Quinet, Y.P., Martins, A.M.C., Lee, S.M.Y., and R\u00e1dis-Baptista, G. (2014). Transcriptome Analysis in Venom Gland of the Predatory Giant Ant Dinoponera quadriceps: Insights into the Polypeptide Toxin Arsenal of Hymenopterans. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0087556"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1186\/s12953-022-00197-z","article-title":"A Combined Protein Toxin Screening Based on the Transcriptome and Proteome of Solenopsis invicta","volume":"20","author":"Cai","year":"2022","journal-title":"Proteome Sci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"4643","DOI":"10.1021\/pr300451g","article-title":"Proteomic View of the Venom from the Fire Ant Solenopsis invicta Buren","volume":"11","author":"Fox","year":"2012","journal-title":"J. Proteome Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1","DOI":"10.11646\/zootaxa.3732.1.1","article-title":"Central American Ants of the Genus Megalomyrmex Forel (Hymenoptera: Formicidae): Six New Species and Keys to Workers and Males","volume":"3732","author":"Boudinot","year":"2013","journal-title":"Zootaxa"},{"key":"ref_21","first-page":"1","article-title":"Systematic Revision of the Neotropical Ant Genus Megalomyrmex Forel (Hymenoptera: Formicidae: Myrmicinae), with the Description of Thirteen New Species","volume":"31","year":"1990","journal-title":"Arq. Zool"},{"key":"ref_22","first-page":"145","article-title":"Further Revisionary Studies on the Ant Genus Megalomyrmex Forel (Hymenoptera: Formicidae: Myrmicinae: Solenopsidini)","volume":"43","year":"2003","journal-title":"Pap\u00e9is Avulsos Zool"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"35","DOI":"10.11646\/zootaxa.2720.1.3","article-title":"A Taxonomic Review of the Ant Genus Megalomyrmex Forel (Hymenoptera: Formicidae) in Central America","volume":"2720","author":"Longino","year":"2010","journal-title":"Zootaxa"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Sozanski, K., Prado, L.P.d., Mularo, A.J., Sadowski, V.A., Jones, T.H., and Adams, R.M.M. (2020). Venom Function of a New Species of Megalomyrmex Forel, 1885 (Hymenoptera: Formicidae). Toxins, 12.","DOI":"10.3390\/toxins12110679"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Fox, E.G.P. (2014). Venom Toxins of Fire Ants, Springer. Toxinology.","DOI":"10.1007\/978-94-007-6649-5_38-1"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1146\/annurev-ento-072821-063525","article-title":"On the Biological Diversity of Ant Alkaloids","volume":"67","author":"Fox","year":"2022","journal-title":"Annu. Rev. Entomol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"3061","DOI":"10.1016\/0040-4039(88)85085-8","article-title":"Ant Venom Alkaloids from Monomorium Species: Natural Insecticides","volume":"29","author":"Bacos","year":"1988","journal-title":"Tetrahedron Lett."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1126\/science.128.3319.306.b","article-title":"Chemical, Insecticidal and Antibiotic Properties of Fire Ant Venom","volume":"128","author":"Blum","year":"1958","journal-title":"Science"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/S0099-9598(08)60261-8","article-title":"Alkaloids from Ants and Other Insects","volume":"31","author":"Numata","year":"1987","journal-title":"Alkaloids Chem. Pharmacol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1897","DOI":"10.1007\/BF00993736","article-title":"Chemistry of Venom Alkaloids in the Ant Genus Megalomyrmex","volume":"17","author":"Jones","year":"1991","journal-title":"J. Chem. Ecol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/0041-0101(79)90267-8","article-title":"Protein Components of Fire Ant Venom (Solenopsis invicta)","volume":"17","author":"Baer","year":"1979","journal-title":"Toxicon"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"4468","DOI":"10.3390\/toxins7114468","article-title":"Honeybee Venom Proteome Profile of Queens and Winter Bees as Determined by a Mass Spectrometric Approach","volume":"7","author":"Danneels","year":"2015","journal-title":"Toxins"},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Dashevsky, D., Baumann, K., Undheim, E.A.B., Nouwens, A., Ikonomopoulou, M.P., Schmidt, J.O., Ge, L., Kwok, H.F., Rodriguez, J., and Fry, B.G. (2023). Functional and Proteomic Insights into Aculeata Venoms. Toxins, 15.","DOI":"10.3390\/toxins15030224"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"21645","DOI":"10.1038\/s41598-020-78740-1","article-title":"Identification and Quantification of Honeybee Venom Constituents by Multiplatform Metabolomics","volume":"10","author":"Klupczynska","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_35","unstructured":"Meier, J. (2008). Biology and Distribution of Hymenopterans of Medical Importance, Their Venom Apparatus and Venom Composition. Handbook of Clinical Toxicology of Animal Venoms and Poisons, CRC Press."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"100117","DOI":"10.1016\/j.toxcx.2022.100117","article-title":"Venom Profile of the European Carpenter Bee Xylocopa violacea: Evolutionary and Applied Considerations on Its Toxin Components","volume":"14","author":"Dutertre","year":"2022","journal-title":"Toxicon X"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"21179","DOI":"10.1038\/s41598-024-72014-w","article-title":"Revealing the pH-Dependent Conformational Changes in Sol g 2.1 Protein and Potential Ligands Binding","volume":"14","author":"Nonkhwao","year":"2024","journal-title":"Sci. Rep."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1111\/j.1365-2311.2012.01384.x","article-title":"Fitness Consequences of Nest Infiltration by the Mutualist-Exploiter Megalomyrmex adamsae","volume":"37","author":"Adams","year":"2012","journal-title":"Ecol. Entomol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"15752","DOI":"10.1073\/pnas.1311654110","article-title":"Chemically Armed Mercenary Ants Protect Fungus-Farming Societies","volume":"110","author":"Adams","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1007\/s10886-015-0565-y","article-title":"Alkaloid Venom Weaponry of Three Megalomyrmex Thief Ants and the Behavioral Response of Cyphomyrmex costatus Host Ants","volume":"41","author":"Adams","year":"2015","journal-title":"J. Chem. Ecol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2507","DOI":"10.1007\/BF00994598","article-title":"Chemistry of Venom Alkaloids in the Ant Megalomyrmex foreli (Myrmicinae) from Costa Rica","volume":"17","author":"Jones","year":"1991","journal-title":"J. Chem. Ecol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1093\/jisesa\/iew068","article-title":"Uncoupling Flight and Reproduction in Ants: Evolution of Ergatoid Queens in Two Lineages of Megalomyrmex (Hymenoptera: Formicidae)","volume":"16","author":"Peeters","year":"2016","journal-title":"J. Insect Sci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/BF01242708","article-title":"Ergatoid Queens and Intercastes in Ants: Two Distinct Adult Forms Which Look Morphologically Intermediate between Workers and Winged Queens","volume":"38","author":"Peeters","year":"1991","journal-title":"Insectes Sociaux"},{"key":"ref_44","unstructured":"Leever, G., Murray, S.K., Prado, L.P., and Adams, R.M.M. (2021). Worker-queen Dimorphism and Queen Winglessness in Megalomyrmex Forel, 1885. [Doctoral Dissertation, The Ohio State University]."},{"key":"ref_45","unstructured":"Roberts, J.M., Carter, G.G., Murray, N.K., and Adams, R.M.M. (2019, January 26). Intraspecific Aggression in a Recently Described Panamanian Ant, Megalomyrmex milenae. Presented at the OSU Fall Undergraduate Research Symposium, Columbus, OH, USA."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.1007\/BF01012125","article-title":"Gaster Flagging by Fire Ants (Solenopsis spp.): Functional Significance of Venom Dispersal Behavior","volume":"11","author":"Obin","year":"1985","journal-title":"J. Chem. Ecol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1603\/0013-8746(2002)095[0487:BOFIRI]2.0.CO;2","article-title":"Biodiversity of Fungi in Red Imported Fire Ant (Hymenoptera: Formicidae) Mounds","volume":"95","author":"Zettler","year":"2002","journal-title":"Ann. Entomol. Soc. Am."},{"key":"ref_48","first-page":"61","article-title":"The Global Ant Genomics Alliance (GAGA)","volume":"25","author":"Boomsma","year":"2017","journal-title":"Myrmecol. News"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1016\/0091-6749(88)90084-X","article-title":"Allergens in Hymenoptera Venom","volume":"82","author":"Hoffman","year":"1988","journal-title":"J. Allergy Clin. Immunol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1385\/CRIAI:30:2:109","article-title":"Hymenoptera venom allergens","volume":"30","author":"Hoffman","year":"2006","journal-title":"Clin. Rev. Allerg Immunol"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Spillner, E., Blank, S., and Jakob, T. (2014). Hymenoptera Allergens: From Venom to \u201cVenome\u201d. Front. Immunol., 5.","DOI":"10.3389\/fimmu.2014.00077"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"103876","DOI":"10.1016\/j.ibmb.2022.103876","article-title":"Venomics Survey of Six Myrmicine Ants Provides Insights into the Molecular and Structural Diversity of Their Peptide Toxins","volume":"151","author":"Klopp","year":"2022","journal-title":"Insect Biochem. Mol. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.anai.2022.02.018","article-title":"Dipeptidyl Peptidase IV of the Vespa velutina Nigrithorax Venom Is Recognized as a Relevant Allergen","volume":"129","author":"Pretre","year":"2022","journal-title":"Ann. Allergy Asthma Immunol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1318","DOI":"10.1038\/s41598-018-19666-7","article-title":"The High Molecular Weight Dipeptidyl Peptidase IV Pol d 3 Is a Major Allergen of Polistes dominula Venom","volume":"8","author":"Schiener","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2371","DOI":"10.1271\/bbb.110571","article-title":"Functional Expression and Characterization of Dipeptidyl Peptidase IV from the Black-Bellied Hornet Vespa basalis in Sf21 Insect Cells","volume":"75","author":"Hshieh","year":"2011","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/j.jaci.2004.11.020","article-title":"Sol i 1, the Phospholipase Allergen of Imported Fire Ant Venom","volume":"115","author":"Hoffman","year":"2005","journal-title":"J. Allergy Clin. Immunol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2090","DOI":"10.1093\/molbev\/msi203","article-title":"Molecular Evolutionary Analyses of the Odorant-Binding Protein Gene Gp-9 in Fire Ants and Other Solenopsis Species","volume":"22","author":"Krieger","year":"2005","journal-title":"Mol. Biol. Evol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1800","DOI":"10.1021\/acs.jproteome.0c00048","article-title":"Venom Peptide Repertoire of the European Myrmicine Ant Manica rubida: Identification of Insecticidal Toxins","volume":"19","author":"Touchard","year":"2020","journal-title":"J. Proteome Res."},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Heep, J., Skaljac, M., Grotmann, J., Kessel, T., Seip, M., Schmidtberg, H., and Vilcinskas, A. (2019). Identification and Functional Characterization of a Novel Insecticidal Decapeptide from the Myrmicine Ant Manica rubida. Toxins, 11.","DOI":"10.3390\/toxins11100562"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"eaau4640","DOI":"10.1126\/sciadv.aau4640","article-title":"A Comprehensive Portrait of the Venom of the Giant Red Bull Ant, Myrmecia gulosa, Reveals a Hyperdiverse Hymenopteran Toxin Gene Family","volume":"4","author":"Robinson","year":"2018","journal-title":"Sci. Adv."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.toxicon.2013.03.010","article-title":"Profiling the Venom Gland Transcriptome of Tetramorium bicarinatum (Hymenoptera: Formicidae): The First Transcriptome Analysis of an Ant Species","volume":"70","author":"Bouzid","year":"2013","journal-title":"Toxicon"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1016\/0091-6749(90)90042-3","article-title":"Allergens in Hymenoptera Venom. XXII. Comparison of Venoms from Two Species of Imported Fire Ants, Solenopsis invicta and richteri","volume":"85","author":"Hoffman","year":"1990","journal-title":"J. Allergy Clin. Immunol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1111\/j.1432-1033.1971.tb01414.x","article-title":"Phospholipase A from Bee Venom","volume":"20","author":"Shipolini","year":"1971","journal-title":"Eur. J. Biochem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1007\/s11882-020-00943-3","article-title":"The Honeybee Venom Major Allergen Api m 10 (Icarapin) and Its Role in Diagnostics and Treatment of Hymenoptera Venom Allergy","volume":"20","author":"Jakob","year":"2020","journal-title":"Curr. Allergy Asthma Rep."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.dci.2016.05.011","article-title":"Secapin, a Bee Venom Peptide, Exhibits Anti-Fibrinolytic, Anti-Elastolytic, and Anti-Microbial Activities","volume":"63","author":"Lee","year":"2016","journal-title":"Dev. Comp. Immunol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"2358","DOI":"10.1093\/gbe\/evw155","article-title":"Tissue-Specific Venom Composition and Differential Gene Expression in Sea Anemones","volume":"8","author":"Macrander","year":"2016","journal-title":"Genome Biol. Evol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1093\/molbev\/msu294","article-title":"Expression of Venom Gene Homologs in Diverse Python Tissues Suggests a New Model for the Evolution of Snake Venom","volume":"32","author":"Card","year":"2015","journal-title":"Mol. Biol. Evol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1093\/molbev\/msu337","article-title":"Venom-Related Transcripts from Bothrops Jararaca Tissues Provide Novel Molecular Insights into the Production and Evolution of Snake Venom","volume":"32","author":"Bastos","year":"2015","journal-title":"Mol. Biol. Evol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1111\/j.1558-5646.1979.tb04668.x","article-title":"Evolution of the Sting Apparatus in the Myrmicine Ants","volume":"33","author":"Kugler","year":"1979","journal-title":"Evolution"},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Drukewitz, S.H., Fuhrmann, N., Undheim, E.A.B., Blanke, A., Giribaldi, J., Mary, R., Laconde, G., Dutertre, S., and von Reumont, B.M. (2018). A Dipteran\u2019s Novel Sucker Punch: Evolution of Arthropod Atypical Venom with a Neurotoxic Component in Robber Flies (Asilidae, Diptera). Toxins, 10.","DOI":"10.3390\/toxins10010029"},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Reumont, V., and Marcus, B. (2018). Studying Smaller and Neglected Organisms in Modern Evolutionary Venomics Implementing RNASeq (Transcriptomics)\u2014A Critical Guide. Toxins, 10.","DOI":"10.3390\/toxins10070292"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Smith, J.J., and Undheim, E.A.B. (2018). True Lies: Using Proteomics to Assess the Accuracy of Transcriptome-Based Venomics in Centipedes Uncovers False Positives and Reveals Startling Intraspecific Variation in Scolopendra subspinipes. Toxins, 10.","DOI":"10.3390\/toxins10030096"},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Lynch, V.J. (2007). Inventing an Arsenal: Adaptive Evolution and Neofunctionalization of Snake Venom Phospholipase A2 Genes. BMC Evol. Biol., 7.","DOI":"10.1186\/1471-2148-7-2"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2007","DOI":"10.1016\/j.cub.2017.05.032","article-title":"The Evolution of Venom by Co-Option of Single-Copy Genes","volume":"27","author":"Martinson","year":"2017","journal-title":"Curr. Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"2001","DOI":"10.1093\/molbev\/msz132","article-title":"The Birth and Death of Toxins with Distinct Functions: A Case Study in the Sea Anemone Nematostella","volume":"36","author":"Sachkova","year":"2019","journal-title":"Mol. Biol. Evol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1353","DOI":"10.1042\/BST20190820","article-title":"The Evolutionary Dynamics of Venom Toxins Made by Insects and Other Animals","volume":"48","author":"Walker","year":"2020","journal-title":"Biochem. Soc. Trans."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/S0091-6749(97)70173-8","article-title":"Reactions to Less Common Species of Fire Ants","volume":"100","author":"Hoffman","year":"1997","journal-title":"J. Allergy Clin. Immunol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1111\/j.1398-9995.2005.00963.x","article-title":"EAACI Interest Group on Insect Venom Hypersensitivity. Diagnosis of Hymenoptera Venom Allergy","volume":"60","author":"Rueff","year":"2005","journal-title":"Allergy"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1590\/S1678-91992012000300010","article-title":"Characterization of the Allergen Sol Gem 2 from the Fire Ant Venom, Solenopsis geminata","volume":"18","author":"Sukprasert","year":"2012","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Nonkhwao, S., Rungsa, P., Buraphaka, H., Klaynongsruang, S., Daduang, J., Kornthong, N., and Daduang, S. (2023). Characterization and Localization of Sol g 2.1 Protein from Solenopsis geminata Fire Ant Venom in the Central Nervous System of Injected Crickets (Acheta domestica). Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241914814"},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Nonkhwao, S., Plettner, E., and Daduang, S. (2024). Protein\u2013Ligand Binding and Structural Modelling Studies of Pheromone-Binding Protein-like Sol g 2.1 from Solenopsis geminata Fire Ant Venom. Molecules, 29.","DOI":"10.3390\/molecules29051033"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1","DOI":"10.22159\/ijpps.2021v13i11.42227","article-title":"Toxic and Immune Allergic Responses of Ant Venom Toxins: A Review","volume":"13","author":"Sharma","year":"2021","journal-title":"Int. J. Pharm. Pharm. Sci."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1016\/j.jaci.2004.07.043","article-title":"Hymenoptera Venom Protease Allergens","volume":"114","author":"Winningham","year":"2004","journal-title":"J. Allergy Clin. Immunol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1949","DOI":"10.1016\/0040-4020(82)80044-6","article-title":"Ant Venom Alkaloids from Solenopsis and Monomorium Species: Recent Developments","volume":"38","author":"Jones","year":"1982","journal-title":"Tetrahedron"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1016\/j.toxicon.2012.05.011","article-title":"Identification, Expression, and Immuno-Reactivity of Sol i 2 & Sol i 4 Venom Proteins of Queen Red Imported Fire Ants, Solenopsis invicta Buren (Hymenoptera: Formicidae)","volume":"60","author":"Lockwood","year":"2012","journal-title":"Toxicon"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1111\/imb.12388","article-title":"Major Venom Proteins of the Fire Ant Solenopsis invicta: Insights into Possible Pheromone-Binding Function from Mass Spectrometric Analysis","volume":"27","author":"Das","year":"2018","journal-title":"Insect Mol. Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"5403","DOI":"10.4049\/jimmunol.0803709","article-title":"Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3","volume":"184","author":"Blank","year":"2010","journal-title":"J. Immunol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1111\/j.1432-1033.1980.tb06073.x","article-title":"Stepwise Cleavage of the pro Part of Promelittin by Dipeptidylpeptidase IV","volume":"111","author":"Kreil","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Wu, C., Yang, C., Wang, Y., Wang, J., and Zhu, J. (2023). Molecular Characterization and Functional Analysis of the Dipeptidyl Peptidase IV from Venom of the Ectoparasitoid Scleroderma guani. Toxins, 15.","DOI":"10.3390\/toxins15050311"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.cbpb.2008.03.005","article-title":"Snake Venom Dipeptidyl Peptidase IV: Taxonomic Distribution and Quantitative Variation","volume":"150","author":"Aird","year":"2008","journal-title":"Comp. Biochem. Physiol. Part B Biochem. Mol. Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/j.toxicon.2003.11.005","article-title":"Skeletal Muscle Degeneration Induced by Venom Phospholipases A2: Insights into the Mechanisms of Local and Systemic Myotoxicity","volume":"42","author":"Ownby","year":"2003","journal-title":"Toxicon"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/0041-0101(65)90024-3","article-title":"Venom Phospholipase A: A Review","volume":"2","author":"Condrea","year":"1965","journal-title":"Toxicon"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1454","DOI":"10.1007\/s43440-023-00543-8","article-title":"Unraveling Snake Venom Phospholipase A2: An Overview of Its Structure, Pharmacology, and Inhibitors","volume":"75","author":"Sampat","year":"2023","journal-title":"Pharmacol. Rep."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1016\/0041-0101(94)90313-1","article-title":"Some Enzymic Activities of Two Australian Ant Venoms: A Jumper Ant Myrmecia pilosula and a Bulldog Ant Myrmecia pyriformis","volume":"32","author":"Matuszek","year":"1994","journal-title":"Toxicon"},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Wang, B., Xiao, Q., Li, X., Wang, J., and Zhu, J. (2023). Proteinaceous Venom Expression of the Yellow Meadow Ant, Lasius flavus (Hymenoptera: Formicidae). Toxins, 15.","DOI":"10.3390\/toxins15020106"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1124\/molpharm.123.000709","article-title":"A Brief Overview of the Toxic Sphingomyelinase Ds of Brown Recluse Spider Venom and Other Organisms and Simple Methods to Detect Production of Its Signature Cyclic Ceramide Phosphate","volume":"105","author":"Lachmayr","year":"2024","journal-title":"Mol. Pharmacol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1016\/j.tcb.2014.07.008","article-title":"Damage Control: Cellular Mechanisms of Plasma Membrane Repair","volume":"24","author":"Andrews","year":"2014","journal-title":"Trends Cell Biol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.toxicon.2018.11.428","article-title":"Queen Venom Isosolenopsin A Delivers Rapid Incapacitation of Fire Ant Competitors","volume":"158","author":"Fox","year":"2019","journal-title":"Toxicon"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1016\/S1081-1206(10)60991-X","article-title":"Cardiodepressant and Neurologic Actions of Solenopsis invicta (Imported Fire Ant) Venom Alkaloids","volume":"94","author":"Howell","year":"2005","journal-title":"Ann. Allergy Asthma Immunol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/j.jprot.2009.01.015","article-title":"Timeline of Key Events in Snake Venom Metalloproteinase Research","volume":"72","author":"Fox","year":"2009","journal-title":"J. Proteom."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"3458","DOI":"10.1002\/eji.200324475","article-title":"Inflammatory Pathogenesis of Snake Venom Metalloproteinase-Induced Skin Necrosis","volume":"33","author":"Laing","year":"2003","journal-title":"Eur. J. Immunol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1002\/arch.20316","article-title":"Differential Gene Expression Profiles in the Venom Gland\/Sac of Orancistrocerus drewseni (Hymenoptera: Eumenidae)","volume":"71","author":"Baek","year":"2009","journal-title":"Arch. Insect Biochem. Physiol."},{"key":"ref_103","first-page":"18","article-title":"Proteolytic Activity of Elapid and Viperid Snake Venoms and Its Implication to Digestion","volume":"1","author":"Bottrall","year":"2010","journal-title":"J. Venom. Res."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1093\/icb\/23.2.427","article-title":"Venom Toxins: Plausible Evolution from Digestive Enzymes","volume":"23","author":"Kochva","year":"1983","journal-title":"Am. Zool"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1163\/1570754043492135","article-title":"Enzyme Activities and Biological Functions of Snake Venoms","volume":"2","author":"McCue","year":"2005","journal-title":"Appl. Herpetol."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Fernandes-Pedrosa, M.F., Junqueira-de-Azevedo, I.d.L., Gon\u00e7alves-de-Andrade, R.M., Kobashi, L.S., Almeida, D.D., Ho, P.L., and Tambourgi, D.V. (2008). Transcriptome Analysis of Loxosceles laeta (Araneae, Sicariidae) Spider Venomous Gland Using Expressed Sequence Tags. BMC Genom., 9.","DOI":"10.1186\/1471-2164-9-279"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1002\/ps.5206","article-title":"Molecular Basis and Mechanism Underlying the Insecticidal Activity of Venoms and Toxins from Latrodectus Spiders","volume":"75","author":"Wang","year":"2019","journal-title":"Pest Manag. Sci."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Diniz, M.R.V., Paiva, A.L.B., Guerra-Duarte, C., Nishiyama, M.Y., Mudadu, M.A., Oliveira, U., Borges, M.H., Yates, J.R., and Junqueira-de-Azevedo, I.d.L. (2018). An Overview of Phoneutria nigriventer Spider Venom Using Combined Transcriptomic and Proteomic Approaches. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0200628"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"20971","DOI":"10.1016\/S0021-9258(17)31916-6","article-title":"Isolation, Cloning, and Characterization of New Chitinase Stored in Active Form in Chitin-Lined Venom Reservoir","volume":"269","author":"Krishnan","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1111\/j.1365-2583.2009.00985.x","article-title":"Chitinase-like Proteins Encoded in the Genome of the Pea Aphid, Acyrthosiphon pisum","volume":"19","author":"Nakabachi","year":"2010","journal-title":"Insect Mol. Biol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"7915464","DOI":"10.1155\/2018\/7915464","article-title":"Assessing the Proteomic Activity of the Venom of the Ant Ectatomma tuberculatum (Hymenoptera: Formicidae: Ectatomminae)","volume":"2018","author":"Silva","year":"2018","journal-title":"Psyche A J. Entomol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1080\/10408690390826455","article-title":"Chitin\u2014The Undisputed Biomolecule of Great Potential","volume":"43","author":"Tharanathan","year":"2003","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"El-Beltagi, H.S., El-Mahdy, O.M., Mohamed, H.I., and El-Ansary, A.E. (2022). Antioxidants, Antimicrobial, and Anticancer Activities of Purified Chitinase of Talaromyces funiculosus Strain CBS 129594 Biosynthesized Using Crustacean Bio-Wastes. Agronomy, 12.","DOI":"10.3390\/agronomy12112818"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1099\/00221287-134-1-169","article-title":"Plant and Bacterial Chitinases Differ in Antifungal Activity","volume":"134","author":"Roberts","year":"1988","journal-title":"Microbiology"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1046\/j.1444-2906.2002.00404.x","article-title":"Antimicrobial Activity of Shrimp Chitin and Chitosan from Different Treatments","volume":"68","author":"Tsai","year":"2002","journal-title":"Fish. Sci."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1006\/bbrc.1996.0071","article-title":"A Novel Antimicrobial Peptide from Bufo bufo gargarizans","volume":"218","author":"Park","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/S1570-9639(03)00018-9","article-title":"Hipposin, a Histone-Derived Antimicrobial Peptide in Atlantic Halibut (Hippoglossus hippoglossus L.)","volume":"1646","author":"Birkemo","year":"2003","journal-title":"Biochim. Biophys. Acta-Proteins Proteom."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1016\/j.biochi.2008.07.003","article-title":"Antimicrobial Action of Histone H2B in Escherichia Coli: Evidence for Membrane Translocation and DNA-Binding of a Histone H2B Fragment after Proteolytic Cleavage by Outer Membrane Proteinase T","volume":"90","author":"Kawasaki","year":"2008","journal-title":"Biochimie"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"2489","DOI":"10.1038\/jid.2009.106","article-title":"Histone H4 Is a Major Component of the Antimicrobial Action of Human Sebocytes","volume":"129","author":"Lee","year":"2009","journal-title":"J. Investig. Dermatol."},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Wang, R., Li, F., Zhang, W., Zhang, X., Qu, C., Tetreau, G., Sun, L., Luo, C., and Zhou, J. (2017). Identification and Expression Profile Analysis of Odorant Binding Protein and Chemosensory Protein Genes in Bemisia tabaci MED by Head Transcriptome. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0171739"},{"key":"ref_121","unstructured":"Aniszewski, T. (2007). Alkaloids\u2014Secrets of Life, Elsevier."},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Aniszewski, T. (2015). Alkaloids: Chemistry, Biology, Ecology, and Applications, Elsevier.","DOI":"10.1016\/B978-0-444-59433-4.00002-X"},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Leal, W.S., and Ishida, Y. (2008). GP-9s Are Ubiquitous Proteins Unlikely Involved in Olfactory Mediation of Social Organization in the Red Imported Fire Ant, Solenopsis invicta. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0003762"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"e21634","DOI":"10.1002\/arch.21634","article-title":"Genomic and Transcriptomic Analyses of Glutathione S-Transferases in an Endoparasitoid Wasp, Pteromalus puparum","volume":"103","author":"Xu","year":"2019","journal-title":"Arch. Insect Biochem. Physiol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1111\/j.1365-2583.2009.00961.x","article-title":"Metabolic Enzymes Associated with Xenobiotic and Chemosensory Responses in Nasonia vitripennis","volume":"19","author":"Oakeshott","year":"2010","journal-title":"Insect Mol. Biol."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Xia, D., Zheng, R., Huang, J., Lu, S., and Tang, Q. (2022). Identification and Functional Analysis of Glutathione S-Transferases from Sitophilus zeamais in Olfactory Organ. Insects, 13.","DOI":"10.3390\/insects13030259"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"128514","DOI":"10.1016\/j.ijbiomac.2023.128514","article-title":"Molecular and Functional Characterization of an Antenna-Enriched Glutathione S-Transferase BminGSTd3 Involved in Undecanol Degradation in the Citrus Fruit Fly, Bactrocera Minax (Enderlein) (Diptera: Tephritidae)","volume":"256","author":"Liu","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Liu, H., Tang, Y., Wang, Q., Shi, H., Yin, J., and Li, C. (2021). Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth. Front. Physiol., 12.","DOI":"10.3389\/fphys.2021.727619"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1242\/jeb.202.12.1625","article-title":"An Olfactory-Specific Glutathione-S-Transferase in the Sphinx Moth Manduca sexta","volume":"202","author":"Rogers","year":"1999","journal-title":"J. Exp. Biol."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Hurka, S., L\u00fcddecke, T., Paas, A., Dersch, L., Schulte, L., Eichberg, J., Hardes, K., Brinkrolf, K., and Vilcinskas, A. (2022). Bioactivity Profiling of in Silico Predicted Linear Toxins from the Ants Myrmica rubra and Myrmica ruginodis. Toxins, 14.","DOI":"10.3390\/toxins14120846"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"3503","DOI":"10.1021\/acs.jproteome.8b00452","article-title":"Deciphering the Molecular Diversity of an Ant Venom Peptidome through a Venomics Approach","volume":"17","author":"Touchard","year":"2018","journal-title":"J. Proteome Res."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"2977","DOI":"10.1038\/s41467-023-38839-1","article-title":"Ant Venoms Contain Vertebrate-Selective Pain-Causing Sodium Channel Toxins","volume":"14","author":"Robinson","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"819.1","DOI":"10.1096\/fasebj.30.1_supplement.819.1","article-title":"Bioinformatic and Functional Analysis of Venom from the Jewel Wasp Ampulex compressa","volume":"30","author":"Arvidson","year":"2016","journal-title":"FASEB J."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"4895","DOI":"10.1016\/j.febslet.2006.08.005","article-title":"Molecular Cloning and Expression of Icarapin, a Novel IgE-Binding Bee Venom Protein","volume":"580","author":"Peiren","year":"2006","journal-title":"FEBS Lett."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.aspen.2016.12.009","article-title":"Synthetic Secapin Bee Venom Peptide Exerts an Anti-Microbial Effect but Not a Cytotoxic or Inflammatory Response","volume":"20","author":"Kim","year":"2017","journal-title":"J. Asia-Pac. Entomol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.peptides.2014.07.004","article-title":"Hyperalgesic and Edematogenic Effects of Secapin-2, a Peptide Isolated from Africanized Honeybee (Apis mellifera) Venom","volume":"59","author":"Mourelle","year":"2014","journal-title":"Peptides"},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Choo, Y.M., Lee, K.S., Yoon, H.J., Qiu, Y., Wan, H., Sohn, M.R., Sohn, H.D., and Jin, B.R. (2012). Antifibrinolytic Role of a Bee Venom Serine Protease Inhibitor That Acts as a Plasmin Inhibitor. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0032269"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/j.peptides.2007.11.013","article-title":"A Novel Serine Protease Inhibitor from Bungarus fasciatus Venom","volume":"29","author":"Lu","year":"2008","journal-title":"Peptides"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"2069","DOI":"10.3390\/md11062069","article-title":"Protease Inhibitors from Marine Venomous Animals and Their Counterparts in Terrestrial Venomous Animals","volume":"11","author":"Schwartz","year":"2013","journal-title":"Mar. Drugs"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.cbpb.2013.10.002","article-title":"A Bumblebee (Bombus ignitus) Venom Serine Protease Inhibitor That Acts as a Microbial Serine Protease Inhibitor","volume":"167","author":"Wan","year":"2014","journal-title":"Comp. Biochem. Physiol. Part B Biochem. Mol. Biol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.cbpb.2009.02.010","article-title":"A Novel Serine Protease Inhibitor from the Venom of Vespa bicolor Fabricius","volume":"153","author":"Yang","year":"2009","journal-title":"Comp. Biochem. Physiol. Part B Biochem. Mol. Biol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1159\/000092424","article-title":"Serine Proteases Affecting Blood Coagulation and Fibrinolysis from Snake Venoms","volume":"34","author":"Kini","year":"2006","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.toxicon.2013.09.017","article-title":"Antimicrobial Activity of a Honeybee (Apis cerana) Venom Kazal-Type Serine Protease Inhibitor","volume":"76","author":"Kim","year":"2013","journal-title":"Toxicon"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.cbpc.2017.09.001","article-title":"Anti-Fibrinolytic and Anti-Microbial Activities of a Serine Protease Inhibitor from Honeybee (Apis cerana) Venom","volume":"201","author":"Yang","year":"2017","journal-title":"Comp. Biochem. Physiol. Part C Toxicol. Pharmacol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1128\/AAC.2.4.291","article-title":"Antibacterial Activity of Venom Alkaloids from the Imported Fire Ant, Solenopsis invicta Buren","volume":"2","author":"Jouvenaz","year":"1972","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.jip.2003.12.005","article-title":"Diversity of Entomopathogenic Fungi near Leaf-Cutting Ant Nests in a Neotropical Forest, with Particular Reference to Metarhizium anisopliae Var. Anisopliae","volume":"85","author":"Hughes","year":"2004","journal-title":"J. Invertebr. Pathol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/j.funbio.2015.06.010","article-title":"Five New Species of Entomopathogenic Fungi from the Amazon and Evolution of Neotropical Ophiocordyceps","volume":"119","author":"Sanjuan","year":"2015","journal-title":"Fungal Biol."},{"key":"ref_148","unstructured":"Adu-Oppong, B., Boomsma, J.J., and Adams, R.M.M. (2013, January 3). Novel alkaloids in the venom of Megalomyrmex milenae have antibacterial properties. Proceedings of the Alan Templeton Symposium at Washington University, Saint Louis, IL, USA."},{"key":"ref_149","unstructured":"Sozanski, K.S. (2025). Biochemical Swiss Army Knives: The Ecology and Evolution of Megalomyrmex Venoms Recapitulate Natural History. [Ph.D. Thesis, The Ohio State University]."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1046\/j.1432-1327.1999.00624.x","article-title":"Post-Translationally Modified Neuropeptides from Conus Venoms","volume":"264","author":"Craig","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.cca.2004.04.004","article-title":"The Effect of Post-Translational Modifications on the Hemorrhagic Activity of Snake Venom Metalloproteinases","volume":"138","author":"Ramos","year":"2004","journal-title":"Comp. Biochem. Physiol. Part C Toxicol. Pharmacol."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Evans, E.R.J., Northfield, T.D., Daly, N.L., and Wilson, D.T. (2019). Venom Costs and Optimization in Scorpions. Front. Ecol. Evol., 7.","DOI":"10.3389\/fevo.2019.00196"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.toxicon.2012.11.022","article-title":"The Venom Optimization Hypothesis Revisited","volume":"63","author":"Morgenstern","year":"2013","journal-title":"Toxicon"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"229","DOI":"10.2307\/3493193","article-title":"Artificial Diet for Rearing Various Species of Ants","volume":"53","author":"Bhatkar","year":"1970","journal-title":"Fla. Entomol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"i884","DOI":"10.1093\/bioinformatics\/bty560","article-title":"Fastp: An Ultra-Fast All-in-One FASTQ Preprocessor","volume":"34","author":"Chen","year":"2018","journal-title":"Bioinformatics"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1038\/nprot.2013.084","article-title":"De Novo Transcript Sequence Reconstruction from RNA-Seq Using the Trinity Platform for Reference Generation and Analysis","volume":"8","author":"Haas","year":"2013","journal-title":"Nat. Protoc."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"2114","DOI":"10.1093\/bioinformatics\/btu170","article-title":"Trimmomatic: A Flexible Trimmer for Illumina Sequence Data","volume":"30","author":"Bolger","year":"2014","journal-title":"Bioinformatics"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"3210","DOI":"10.1093\/bioinformatics\/btv351","article-title":"BUSCO: Assessing Genome Assembly and Annotation Completeness with Single-Copy Orthologs","volume":"31","author":"Waterhouse","year":"2015","journal-title":"Bioinformatics"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/nmeth.3176","article-title":"Fast and Sensitive Protein Alignment Using DIAMOND","volume":"12","author":"Buchfink","year":"2015","journal-title":"Nat. Methods"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"D444","DOI":"10.1093\/nar\/gkae1082","article-title":"InterPro: The Protein Sequence Classification Resource in 2025","volume":"53","author":"Blum","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1038\/nbt.3519","article-title":"Near-Optimal Probabilistic RNA-Seq Quantification","volume":"34","author":"Bray","year":"2016","journal-title":"Nat. Biotechnol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"gkaf018","DOI":"10.1093\/nar\/gkaf018","article-title":"edgeR v4: Powerful Differential Analysis of Sequencing Data with Expanded Functionality and Improved Support for Small Counts and Larger Datasets","volume":"53","author":"Chen","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1093\/bioinformatics\/btp616","article-title":"edgeR: A Bioconductor Package for Differential Expression Analysis of Digital Gene Expression Data","volume":"26","author":"Robinson","year":"2010","journal-title":"Bioinformatics"}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/18\/1\/55\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,1,24]],"date-time":"2026-01-24T05:26:33Z","timestamp":1769232393000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/18\/1\/55"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1,21]]},"references-count":163,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,1]]}},"alternative-id":["toxins18010055"],"URL":"https:\/\/doi.org\/10.3390\/toxins18010055","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,1,21]]}}}