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dc.contributor.authorRosa, Annachiara
dc.contributor.authorChande, Ajit
dc.contributor.authorZiglio, Serena
dc.contributor.authorDe Sanctis, Veronica
dc.contributor.authorBertorelli, Roberto
dc.contributor.authorGoh, Shih Lin
dc.contributor.authorMcCauley, Sean M.
dc.contributor.authorNowosielska, Anetta
dc.contributor.authorAntonarakis, Stylianos E.
dc.contributor.authorLuban, Jeremy
dc.contributor.authorSantoni, Federico Andrea
dc.contributor.authorPizzato, Massimo
dc.date2022-08-11T08:10:18.000
dc.date.accessioned2022-08-23T17:03:36Z
dc.date.available2022-08-23T17:03:36Z
dc.date.issued2015-10-08
dc.date.submitted2016-04-13
dc.identifier.citationNature. 2015 Oct 8;526(7572):212-7. doi: 10.1038/nature15399. Epub 2015 Sep 30. <a href="http://dx.doi.org/10.1038/nature15399">Link to article on publisher's site</a>
dc.identifier.issn0028-0836 (Linking)
dc.identifier.doi10.1038/nature15399
dc.identifier.pmid26416734
dc.identifier.urihttp://hdl.handle.net/20.500.14038/44462
dc.description.abstractHIV-1 Nef, a protein important for the development of AIDS, has well-characterized effects on host membrane trafficking and receptor downregulation. By an unidentified mechanism, Nef increases the intrinsic infectivity of HIV-1 virions in a host-cell-dependent manner. Here we identify the host transmembrane protein SERINC5, and to a lesser extent SERINC3, as a potent inhibitor of HIV-1 particle infectivity that is counteracted by Nef. SERINC5 localizes to the plasma membrane, where it is efficiently incorporated into budding HIV-1 virions and impairs subsequent virion penetration of susceptible target cells. Nef redirects SERINC5 to a Rab7-positive endosomal compartment and thereby excludes it from HIV-1 particles. The ability to counteract SERINC5 was conserved in Nef encoded by diverse primate immunodeficiency viruses, as well as in the structurally unrelated glycosylated Gag from murine leukaemia virus. These examples of functional conservation and convergent evolution emphasize the fundamental importance of SERINC5 as a potent anti-retroviral factor.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=26416734&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1038/nature15399
dc.subjectAnimals
dc.subjectCell Line
dc.subjectCell Membrane
dc.subjectEndosomes
dc.subjectEvolution, Molecular
dc.subjectGene Products, gag
dc.subjectGene Products, nef
dc.subjectHIV-1
dc.subjectHost Specificity
dc.subject*Host-Pathogen Interactions
dc.subjectHumans
dc.subjectLeukemia Virus, Murine
dc.subjectMembrane Proteins
dc.subjectNeoplasm Proteins
dc.subjectPrimates
dc.subjectReceptors, Cell Surface
dc.subjectVirion
dc.subjectnef Gene Products, Human Immunodeficiency Virus
dc.subjectrab GTP-Binding Proteins
dc.subjectBiochemistry
dc.subjectMolecular Biology
dc.titleHIV-1 Nef promotes infection by excluding SERINC5 from virion incorporation
dc.typeJournal Article
dc.source.journaltitleNature
dc.source.volume526
dc.source.issue7572
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/pmm_pp/56
dc.identifier.contextkey8471540
html.description.abstract<p>HIV-1 Nef, a protein important for the development of AIDS, has well-characterized effects on host membrane trafficking and receptor downregulation. By an unidentified mechanism, Nef increases the intrinsic infectivity of HIV-1 virions in a host-cell-dependent manner. Here we identify the host transmembrane protein SERINC5, and to a lesser extent SERINC3, as a potent inhibitor of HIV-1 particle infectivity that is counteracted by Nef. SERINC5 localizes to the plasma membrane, where it is efficiently incorporated into budding HIV-1 virions and impairs subsequent virion penetration of susceptible target cells. Nef redirects SERINC5 to a Rab7-positive endosomal compartment and thereby excludes it from HIV-1 particles. The ability to counteract SERINC5 was conserved in Nef encoded by diverse primate immunodeficiency viruses, as well as in the structurally unrelated glycosylated Gag from murine leukaemia virus. These examples of functional conservation and convergent evolution emphasize the fundamental importance of SERINC5 as a potent anti-retroviral factor.</p>
dc.identifier.submissionpathpmm_pp/56
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages212-7


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