2026-11-062026-11-062026LIMA, André Miller Cortêz. Análise comparativa da ocorrência de epítopos lineares na glicoproteína de lissavírus dos filogrupos I e II. Orientador: Carlos Alberto Marques de Carvalho. 2026. 45 f. Dissertação ( Mestrado em Biologia Parasitária na Amazônia) - Centro de Ciências Biológicas e da Saúde, Universidade do Estado do Pará, Belém, 2026.https://portaldaposgraduacao.uepa.br/handle/riuepa/432AbertoLissavírusEpítoposBiologia computacionalProteínas viraisLyssavirusEpitopesComputational biologyViral proteinsAnálise comparativa da ocorrência de epítopos lineares na glicoproteína de lissavírus dos filogrupos I e IIComparative analysis of the occurrence of linear epitopes in the glycoprotein of lyssaviruses from phylogroups I and IIDissertaçãoCiências BiológicasCiências Biológicas::MicrobiologiaCiências Biológicas::Microbiologia::Biologia e Fisiologia dos MicroorganismosLyssaviruses comprise a group of neurotropic viruses responsible for lethal encephalitis, most notably the rabies virus. The G protein of these viruses plays a central role in infection, being the main target of humoral and cell-mediated adaptive immunity. In this context, the present study aimed to comparatively analyze the occurrence of linear B and CD4+ T cell epitopes in the ectodomain of the G protein of lyssaviruses belonging to phylogroups I (RABV, EBLV-1, EBLV-2, DUVV, and ABLV) and II (LBV and MOKV), using bioinformatics approaches. The amino acid sequences of the G protein were retrieved by conceptual translation from the reference viral genome available in GenBank, processed in SignalP and TMHMM for ectodomain isolation, aligned in Clustal Omega for percentage identity determination, and submitted to EMBOSS Cons for consensus sequence generation. Prediction of CD4+ T cell epitopes was performed based on analysis of binding affinity to HLA-II alleles using NetMHCIIpan with the aid of Epitope-Evaluator, while B cell epitopes were identified from the combination of hydrophilicity, accessibility, and flexibility parameters in NPS@ PCProf, also evaluating the potential masking by N-glycans in NetNGlyc. The results showed amino acid identity of 76.71% to 83.79% in phylogroup I and 82.72% in phylogroup II. A higher density of HLA-II epitopes was observed in phylogroup I (0.22) compared to phylogroup II (0.18). Although the average antigenicity was higher in distinct halves of the G protein ectodomain in each lyssavirus phylogroup, linear B cell epitopes contained in equivalent positions of phylogroups I and II (FKRKHF and TFKRKHFK, respectively) overlapped to peptides commonly bound by the HLA-II DRB1*15:01 allele (TYTNFVGYVTTTFKR, YTNFVGYVTTTFKRK, and TNFVGYVTTTFKRKH) and not masked by N-glycans, suggesting functional relevance in CD4+ T cell-dependent antibody responses. Taken together, these findings contribute to the understanding of antigenic determinants of the G protein and provide support for the development of more comprehensive vaccine and immunoprophylactic strategies against lyssaviruses.PPG-BPA - Morfofisiologia e genética dos agentes infecciosos, parasitários e vetores de endemias na Amazônia