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AuthorNeyla Maria Pereira, Alves
Authorde Moura, Ronald Rodrigues
AuthorBernardo, Lucas Coêlho
AuthorAgrelli, Almerinda
Authorde Oliveira, Ana Sofia Lima Estevão
Authorda Silva, Natália Pereira
AuthorCrovella, Sergio
AuthorBrandão, Lucas André Cavalcanti
Available date2022-01-24T05:13:17Z
Publication Date2021-08-31
Publication NameInfection, Genetics and Evolution
Identifierhttp://dx.doi.org/10.1016/j.meegid.2021.104837
CitationAlves, N., de Moura, R. R., Bernardo, L. C., Agrelli, A., de Oliveira, A., da Silva, N. P., Crovella, S., & Brandão, L. (2021). In silico analysis of molecular interactions between HIV-1 glycoprotein gp120 and TNF receptors. Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases, 92, 104837. https://doi.org/10.1016/j.meegid.2021.104837
ISSN15671348
URIhttps://www.sciencedirect.com/science/article/pii/S1567134821001349
URIhttp://hdl.handle.net/10576/25800
AbstractProinflammatory microenvironmental is crucial for the Human Immunodeficiency Virus Type 1 (HIV-1) pathogenesis. The viral glycoprotein 120 (gp120) must interact with the CD4+ T cell chemokine receptor (CCR5) and a co-receptor C-X-C chemokine receptor type 4 (CXCR4) to let the virus entry into the host cells. However, the interaction of the viral particle with other cell surface receptors is mandatory for its attachment and subsequently entry. Tumor Necrosis Factor receptor type I (TNFR1), type II (TNFR2) and Fas are a superfamily of transmembrane proteins involved in canonical inflammatory pathway and cell death by apoptosis as responses against viral pathogens. In our study, we performed an in silico evaluation of the molecular interactions between viral protein gp120 and TNF receptors (TNFR1, TNFR2 and Fas). Protein structures were retrieved from Protein Databank (PDB), and Molecular Docking and dynamics were performed using ClusPro 2.0 server and GROMACS software, respectively. We observed that gp120 is able to bind TNFR1, TNFR2 and Fas receptors, although only the TNFR2-gp120 complex demonstrated to produce a stable and durable binding. Our findings suggest that gp120 may act as an agonist to TNF-α and also function as an attachment factor in HIV-1 entry process. These molecular interaction by gp120 may be the key to HIV-1 immunopathogenesis. In conclusion, gp120 may stimulate pro-inflammatory and apoptotic signaling transduction pathways mediated by TNFR2 and may act as an attachment factor retaining HIV-1 viral particles on the host cell surface.
SponsorWe acknowledge the financial support by the National Council for the Improvement of Higher Education – Brazil (CAPES) and the National Council for Scientific and Technological Development – Brazil (CNPq).
Languageen
PublisherElsevier
SubjectImmunological pathway
gp120 modulation
HIV-1 infection
Molecular dynamics
Molecular docking
TitleIn silico analysis of molecular interactions between HIV-1 glycoprotein gp120 and TNF receptors
TypeArticle
Volume Number92
dc.accessType Open Access


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