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Article: A tyrosine-based motif in the HIV-1 envelope glycoprotein tail mediates cell-type- and Rab11-FIP1C-dependent incorporation into virions

TitleA tyrosine-based motif in the HIV-1 envelope glycoprotein tail mediates cell-type- and Rab11-FIP1C-dependent incorporation into virions
Authors
KeywordsPseudotyping
Rab coupling protein
FIP1C
HIV assembly
HIV envelope
Issue Date2015
Citation
Proceedings of the National Academy of Sciences of the United States of America, 2015, v. 112, n. 24, p. 7575-7580 How to Cite?
Abstract© 2015, National Academy of Sciences. All rights reserved. Lentiviruses such as HIV-1 encode envelope glycoproteins (Env) with long cytoplasmic tails (CTs) that include motifs mediating interactions with host-cell-trafficking factors. We demonstrated recently that Rab11-family interacting protein 1C (FIP1C) is required for CT-dependent incorporation of Env into HIV-1 particles. Here, we used viruses bearing targeted substitutions within CT to map the FIP1C-dependent incorporation of Env. We identified YW795 as a critical motif mediating cell-type-dependent Env incorporation. Disruption of YW795 reproduced the cell-type-dependent particle incorporation of Env that had previously been observed with large truncations of CT. A revertant virus bearing a single amino acid change near the C terminus of CT restored wild-type levels of Env incorporation, Gag-Env colocalization on the plasma membrane, and viral replication. These findings highlight the importance of YW795 in the cell-type-dependent incorporation of Env and support a model of HIV assembly in which FIP1C/RCP mediates Env trafficking to the particle assembly site.
Persistent Identifierhttp://hdl.handle.net/10722/222689
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883

 

DC FieldValueLanguage
dc.contributor.authorQi, Mingli-
dc.contributor.authorChu, Hin-
dc.contributor.authorChen, Xuemin-
dc.contributor.authorChoi, Junghwa-
dc.contributor.authorWen, Xiaoyun-
dc.contributor.authorHammonds, Jason-
dc.contributor.authorDing, Lingmei-
dc.contributor.authorHunter, Eric-
dc.contributor.authorSpearman, Paul-
dc.date.accessioned2016-01-19T03:37:00Z-
dc.date.available2016-01-19T03:37:00Z-
dc.date.issued2015-
dc.identifier.citationProceedings of the National Academy of Sciences of the United States of America, 2015, v. 112, n. 24, p. 7575-7580-
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10722/222689-
dc.description.abstract© 2015, National Academy of Sciences. All rights reserved. Lentiviruses such as HIV-1 encode envelope glycoproteins (Env) with long cytoplasmic tails (CTs) that include motifs mediating interactions with host-cell-trafficking factors. We demonstrated recently that Rab11-family interacting protein 1C (FIP1C) is required for CT-dependent incorporation of Env into HIV-1 particles. Here, we used viruses bearing targeted substitutions within CT to map the FIP1C-dependent incorporation of Env. We identified YW<inf>795</inf> as a critical motif mediating cell-type-dependent Env incorporation. Disruption of YW<inf>795</inf> reproduced the cell-type-dependent particle incorporation of Env that had previously been observed with large truncations of CT. A revertant virus bearing a single amino acid change near the C terminus of CT restored wild-type levels of Env incorporation, Gag-Env colocalization on the plasma membrane, and viral replication. These findings highlight the importance of YW<inf>795</inf> in the cell-type-dependent incorporation of Env and support a model of HIV assembly in which FIP1C/RCP mediates Env trafficking to the particle assembly site.-
dc.languageeng-
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of America-
dc.subjectPseudotyping-
dc.subjectRab coupling protein-
dc.subjectFIP1C-
dc.subjectHIV assembly-
dc.subjectHIV envelope-
dc.titleA tyrosine-based motif in the HIV-1 envelope glycoprotein tail mediates cell-type- and Rab11-FIP1C-dependent incorporation into virions-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1073/pnas.1504174112-
dc.identifier.scopuseid_2-s2.0-84935826142-
dc.identifier.volume112-
dc.identifier.issue24-
dc.identifier.spage7575-
dc.identifier.epage7580-
dc.identifier.eissn1091-6490-

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