{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,12]],"date-time":"2026-01-12T22:26:20Z","timestamp":1768256780243,"version":"3.49.0"},"reference-count":12,"publisher":"American Society of Tropical Medicine and Hygiene","issue":"4","license":[{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,10,1]]},"abstract":"<jats:title>ABSTRACT.<\/jats:title>\n<jats:p>Given the importance of eastern equine encephalitis virus (EEEV; complex lineage I) in veterinary and public health in North America, there is limited knowledge about lineages II, III, and IV, also known as Madariaga virus (MADV), which are prevalent in Central and South America. Because charge mutations in the envelope glycoproteins are critical to the emergence of Venezuelan equine encephalitis virus, we analyzed the structural polyproteins of Venezuelan MADV isolates and compared them with sequences of EEEV. Four substitutions involving positively charged residues were identified in the E3 (R44Q) and E2 (R205H\/Q, K260T\/A, and R310Q) proteins. Additionally, histidine residues were present in EEEV and absent in MADV: E2 (H82Y, H94Y, H114Q, and H181S) and E1 (H118Q). None of these amino acids were predicted to be under selective pressure or associated with a significant conformational change in the envelope proteins. However, some of these substitutions might still be associated with the virulence and pathogenicity of EEEV.<\/jats:p>","DOI":"10.4269\/ajtmh.24-0693","type":"journal-article","created":{"date-parts":[[2025,8,7]],"date-time":"2025-08-07T13:41:07Z","timestamp":1754574067000},"page":"879-882","source":"Crossref","is-referenced-by-count":1,"title":["Eastern Equine Encephalitis Virus Exhibits More Charged Amino Acids in Its Envelope Proteins, Compared to Madariaga Virus"],"prefix":"10.4269","volume":"113","author":[{"given":"Gladys","family":"Medina","sequence":"first","affiliation":[{"name":"Edificio de Sanidad Animal, Laboratorio de Arbovirus-CENIAP\/INIA, Aragua, Venezuela;"},{"name":"Laboratorio de Virolog\u00eda Molecular, CMBC, Instituto Venezolano de Investigaciones Cient\u00edficas (IVIC), Caracas, Venezuela;"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jose Luis","family":"Zambrano","sequence":"additional","affiliation":[{"name":"Laboratorio de Virolog\u00eda Celular, CMBC, Instituto Venezolano de Investigaciones Cient\u00edficas (IVIC), Caracas, Venezuela;"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carmen Luisa","family":"Loureiro","sequence":"additional","affiliation":[{"name":"Laboratorio de Virolog\u00eda Molecular, CMBC, Instituto Venezolano de Investigaciones Cient\u00edficas (IVIC), Caracas, Venezuela;"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Domingo J.","family":"Garzaro","sequence":"additional","affiliation":[{"name":"Laboratorio de Virolog\u00eda Molecular, CMBC, Instituto Venezolano de Investigaciones Cient\u00edficas (IVIC), Caracas, Venezuela;"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miguel","family":"Barrios","sequence":"additional","affiliation":[{"name":"Laboratorio de Virolog\u00eda Molecular, CMBC, Instituto Venezolano de Investigaciones Cient\u00edficas (IVIC), Caracas, Venezuela;"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rosa Alba","family":"Salas","sequence":"additional","affiliation":[{"name":"Residencias Thamara, Caracas, Venezuela;"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Scott C.","family":"Weaver","sequence":"additional","affiliation":[{"name":"World Reference Center for Emerging Viruses and Arboviruses, Institute for Human Infections and Immunity and Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Flor H.","family":"Pujol","sequence":"additional","affiliation":[{"name":"Laboratorio de Virolog\u00eda Molecular, CMBC, Instituto Venezolano de Investigaciones Cient\u00edficas (IVIC), Caracas, Venezuela;"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"2795","reference":[{"key":"b1","series-title":"Vector Borne Zoonotic Dis","first-page":"633","article-title":"Uncertainties surrounding Madariaga virus, a member of the eastern equine encephalitis virus 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evolutionary genetics analysis version 11","volume":"38","author":"Tamura","year":"2021"},{"key":"b7","series-title":"J Virol","first-page":"6302","article-title":"A single mutation in the E2 glycoprotein important for neurovirulence influences binding of Sindbis virus to neuroblastoma cells","volume":"76","author":"Lee","year":"2002"},{"key":"b8","series-title":"Nat Commun","first-page":"6866","article-title":"The receptor VLDLR binds eastern equine encephalitis virus through multiple distinct modes","volume":"15","author":"Cao","year":"2024"},{"key":"b9","series-title":"Mol Biol Evol","first-page":"773","article-title":"Datamonkey 2.0: A modern web application for characterizing selective and other evolutionary processes","volume":"35","author":"Weaver","year":"2018"},{"key":"b10","series-title":"Cell Rep","first-page":"3136","article-title":"Cryo-EM structures of eastern equine encephalitis virus reveal mechanisms of virus disassembly and antibody neutralization","volume":"25","author":"Hasan","year":"2018"},{"key":"b11","series-title":"Protein Sci","first-page":"e4792","article-title":"UCSF ChimeraX: Tools for structure building and analysis","volume":"32","author":"Meng","year":"2023"},{"key":"b12","series-title":"Nucleic Acids Res","first-page":"W296","article-title":"SWISS-MODEL: Homology modelling of protein structures and complexes","volume":"46","author":"Waterhouse","year":"2018"}],"container-title":["The American Journal of Tropical Medicine and 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