Journal
SCIENTIFIC REPORTS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep40037
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Funding
- Europrise Network of Excellence, Life Sciences Programme, European Commission Grant
- Italian Ministry of Health [ISS40H92]
- FUR
- University of Verona
- European Regional Development Fund (ERDF) [SAF2015-64118-R, UNLL10-3E-783]
- Fundacion CajaCanarias
- Plan Nacional I + D + i [RD12/0017/0034]
- ISCIII-Subdireccion General de Evaluacion
- ERDF (RIS-RETIC)
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HLA-C has been demonstrated to associate with HIV-1 envelope glycoprotein (Env). Virions lacking HLA-C have reduced infectivity and increased susceptibility to neutralizing antibodies. Like all others MHC-I molecules, HLA-C requires beta(2)-microglobulin (beta(2)m) for appropriate folding and expression on the cell membrane but this association is weaker, thus generating HLA-C free-chains on the cell surface. In this study, we deepen the understanding of HLA-C and Env association by showing that HIV-1 specifically increases the amount of HLA-C free chains, not bound to beta(2)m, on the membrane of infected cells. The association between Env and HLA-C takes place at the cell membrane requiring beta(2)m to occur. We report that the enhanced infectivity conferred to HIV-1 by HLA-C specifically involves HLA-C free chain molecules that have been correctly assembled with beta(2)m. HIV-1 Env-pseudotyped viruses produced in the absence of beta(2)m are less infectious than those produced in the presence of beta(2)m. We hypothesize that the conformation and surface expression of HLA-C molecules could be a discriminant for the association with Env. Binding stability to beta(2)m may confer to HLA-C the ability to preferentially act either as a conventional immune-competent molecule or as an accessory molecule involved in HIV-1 infectivity.
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