Using accelerated molecular dynamics simulation to elucidate the effects of the T198F mutation on the molecular flexibility of the West Nile virus envelope protein
The envelope (E) protein is an important target for antibodies in favivirus. Literature reports that the mutation T198F, located at the domain I-II hinge of the E protein, regulates viral breathing and increases the accessibility of a distal cryptic epitope located on the fusion loop, having a dir...
| Autor principal: | Valente, Renan Patrick de Penha |
|---|---|
| Outros Autores: | Souza, Rafael Concei??o de, Muniz, Gabriela de Medeiros, Ferreira, Jo?o Elias Vidueira, Miranda, Ricardo Morais de, Lima, Anderson Henrique Lima e, Vianez J?nior, Jo?o L?dio da Silva Gon?alves |
| Grau: | Artigo |
| Idioma: | eng |
| Publicado em: |
Nature Research
2020
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| Assuntos: | |
| Acesso em linha: |
http://patua.iec.gov.br//handle/iec/4110 |
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ir-iec-4110 |
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dspace |
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ir-iec-41102020-06-30T18:53:28Z Using accelerated molecular dynamics simulation to elucidate the effects of the T198F mutation on the molecular flexibility of the West Nile virus envelope protein Valente, Renan Patrick de Penha Souza, Rafael Concei??o de Muniz, Gabriela de Medeiros Ferreira, Jo?o Elias Vidueira Miranda, Ricardo Morais de Lima, Anderson Henrique Lima e Vianez J?nior, Jo?o L?dio da Silva Gon?alves V?rus do Nilo Ocidental / isolamento & purifica??o Prote?nas do Envelope Viral Muta??o Mapeamento de Epitopos Simula??o de Din?mica Molecular The envelope (E) protein is an important target for antibodies in favivirus. Literature reports that the mutation T198F, located at the domain I-II hinge of the E protein, regulates viral breathing and increases the accessibility of a distal cryptic epitope located on the fusion loop, having a direct impact in the neutralization of West Nile virus (WNV). Our study aimed to describe, using accelerated molecular dynamics simulations, the efects of the T198F mutation in the fexibility of the E protein of WNV and to elucidate the mechanism that regulates epitope accessibility. The simulation results revealed that the mutation favors the formation of alternative hydrogen bonds, hampering the bending movement between domains I and II. We hypothesized that this is the mechanism by which the T198F mutation, located at the middle of the protein, locks the distal cryptc epitope near a single preferred conformation, rendering it more prone to recognition by antibodies. Evandro Chagas Institute, Federal University of Par?, Federal Institute of Education, Science and Technology of Par?, FAPESPA and CNPq. 2020-06-30T18:29:27Z 2020-06-30T18:29:27Z 2020 Artigo VALENTE, Renan Patrick de Penha et al. Using accelerated molecular dynamics simulation to elucidate the effects of the T198F mutation on the molecular flexibility of the West Nile virus envelope protein. Scientific Reports, v. 10, n. 9625, 2020. 2045-2322 http://patua.iec.gov.br//handle/iec/4110 10.1038/s41598-020-66344-8 eng Acesso Aberto application/pdf Nature Research |
| institution |
Instituto Evandro Chagas (IEC) |
| collection |
PATUA |
| language |
eng |
| topic |
V?rus do Nilo Ocidental / isolamento & purifica??o Prote?nas do Envelope Viral Muta??o Mapeamento de Epitopos Simula??o de Din?mica Molecular |
| spellingShingle |
V?rus do Nilo Ocidental / isolamento & purifica??o Prote?nas do Envelope Viral Muta??o Mapeamento de Epitopos Simula??o de Din?mica Molecular Valente, Renan Patrick de Penha Using accelerated molecular dynamics simulation to elucidate the effects of the T198F mutation on the molecular flexibility of the West Nile virus envelope protein |
| topic_facet |
V?rus do Nilo Ocidental / isolamento & purifica??o Prote?nas do Envelope Viral Muta??o Mapeamento de Epitopos Simula??o de Din?mica Molecular |
| description |
The envelope (E) protein is an important target for antibodies in favivirus. Literature reports that
the mutation T198F, located at the domain I-II hinge of the E protein, regulates viral breathing and
increases the accessibility of a distal cryptic epitope located on the fusion loop, having a direct impact in
the neutralization of West Nile virus (WNV). Our study aimed to describe, using accelerated molecular
dynamics simulations, the efects of the T198F mutation in the fexibility of the E protein of WNV
and to elucidate the mechanism that regulates epitope accessibility. The simulation results revealed
that the mutation favors the formation of alternative hydrogen bonds, hampering the bending
movement between domains I and II. We hypothesized that this is the mechanism by which the T198F
mutation, located at the middle of the protein, locks the distal cryptc epitope near a single preferred
conformation, rendering it more prone to recognition by antibodies. |
| format |
Artigo |
| author |
Valente, Renan Patrick de Penha |
| author2 |
Souza, Rafael Concei??o de Muniz, Gabriela de Medeiros Ferreira, Jo?o Elias Vidueira Miranda, Ricardo Morais de Lima, Anderson Henrique Lima e Vianez J?nior, Jo?o L?dio da Silva Gon?alves |
| author2Str |
Souza, Rafael Concei??o de Muniz, Gabriela de Medeiros Ferreira, Jo?o Elias Vidueira Miranda, Ricardo Morais de Lima, Anderson Henrique Lima e Vianez J?nior, Jo?o L?dio da Silva Gon?alves |
| title |
Using accelerated molecular dynamics simulation to elucidate the effects of the T198F mutation on the molecular flexibility of the West Nile virus envelope protein |
| title_short |
Using accelerated molecular dynamics simulation to elucidate the effects of the T198F mutation on the molecular flexibility of the West Nile virus envelope protein |
| title_full |
Using accelerated molecular dynamics simulation to elucidate the effects of the T198F mutation on the molecular flexibility of the West Nile virus envelope protein |
| title_fullStr |
Using accelerated molecular dynamics simulation to elucidate the effects of the T198F mutation on the molecular flexibility of the West Nile virus envelope protein |
| title_full_unstemmed |
Using accelerated molecular dynamics simulation to elucidate the effects of the T198F mutation on the molecular flexibility of the West Nile virus envelope protein |
| title_sort |
using accelerated molecular dynamics simulation to elucidate the effects of the t198f mutation on the molecular flexibility of the west nile virus envelope protein |
| publisher |
Nature Research |
| publishDate |
2020 |
| url |
http://patua.iec.gov.br//handle/iec/4110 |
| _version_ |
1717584515419865088 |
| score |
11.755432 |