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Evaluation of potential MHC-I allele-specific epitopes in Zika virus proteins and the effects of mutations on peptide-MHC-I interaction studied using in silico approaches.
da Costa, Aline Silva; Fernandes, Tácio Vinício Amorim; Bello, Murilo Lamim; de Souza, Theo Luiz Ferraz.
Afiliación
  • da Costa AS; Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, 21941-902, Brazil; Instituto Nacional de Ciência e Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
  • Fernandes TVA; Laboratório de Macromoléculas, Diretoria de Metrologia Aplicada às Ciências da Vida, Instituto Nacional de Metrologia, Qualidade e Tecnologia - INMETRO, Duque de Caxias, RJ, 25250-020, Brazil.
  • Bello ML; Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, 21941-902, Brazil.
  • de Souza TLF; Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, 21941-902, Brazil; Instituto Nacional de Ciência e Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil. Electronic address: theo@pharma.ufrj.br.
Comput Biol Chem ; 92: 107459, 2021 Jun.
Article en En | MEDLINE | ID: mdl-33636637
Zika virus (ZIKV) infection is a global health concern due to its association with microcephaly and neurological complications. The development of a T-cell vaccine is important to combat this disease. In this study, we propose ZIKV major histocompatibility complex I (MHC-I) epitopes based on in silico screening consensus followed by molecular docking, PRODIGY, and molecular dynamics (MD) simulation analyses. The effects of the reported mutations on peptide-MHC-I (pMHC-I) complexes were also evaluated. In general, our data indicate an allele-specific peptide-binding human leukocyte antigen (HLA) and potential epitopes. For HLA-B44, we showed that the absence of acidic residue Glu at P2, due to the loss of the electrostatic interaction with Lys45, has a negative impact on the pMHC-I complex stability and explains the low free energy estimated for the immunodominant peptide E-4 (IGVSNRDFV). Our MD data also suggest the deleterious effects of acidic residue Asp at P1 on the pMHC-I stability of HLA-B8 due to destabilization of the α-helix and ß-strand. Free energy estimation further indicated that the mutation from Val to Ala at P9 of peptide E-247 (DAHAKRQTV), which was found exclusively in microcephaly samples, did not reduce HLA-B8 affinity. In contrast, the mutation from Thr to Pro at P2 of the peptide NS5-832 (VTKWTDIPY) decreased the interaction energy, number of intermolecular interactions, and adversely affected its binding mode with HLA-A1. Overall, our findings are important with regard to the design of T-cell peptide vaccines and for understanding how ZIKV escapes recognition by CD8 + T-cells.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Proteínas Virales / Simulación de Dinámica Molecular / Virus Zika / Complejo Mayor de Histocompatibilidad / Epítopos Tipo de estudio: Prognostic_studies Idioma: En Revista: Comput Biol Chem Asunto de la revista: BIOLOGIA / INFORMATICA MEDICA / QUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Proteínas Virales / Simulación de Dinámica Molecular / Virus Zika / Complejo Mayor de Histocompatibilidad / Epítopos Tipo de estudio: Prognostic_studies Idioma: En Revista: Comput Biol Chem Asunto de la revista: BIOLOGIA / INFORMATICA MEDICA / QUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido