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The HIV-1 capsid core is an opportunistic nuclear import receptor
The movement of viruses and other large macromolecular cargo through nuclear pore complexes (NPCs) is poorly understood. The human immunodeficiency virus type 1 (HIV-1) provides an attractive model to interrogate this process. HIV-1 capsid (CA), the chief structural component of the viral core, is a...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10290713/ https://www.ncbi.nlm.nih.gov/pubmed/37355754 http://dx.doi.org/10.1038/s41467-023-39146-5 |
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author | Xue, Guangai Yu, Hyun Jae Buffone, Cindy Huang, Szu-Wei Lee, KyeongEun Goh, Shih Lin Gres, Anna T. Guney, Mehmet Hakan Sarafianos, Stefan G. Luban, Jeremy Diaz-Griffero, Felipe KewalRamani, Vineet N. |
author_facet | Xue, Guangai Yu, Hyun Jae Buffone, Cindy Huang, Szu-Wei Lee, KyeongEun Goh, Shih Lin Gres, Anna T. Guney, Mehmet Hakan Sarafianos, Stefan G. Luban, Jeremy Diaz-Griffero, Felipe KewalRamani, Vineet N. |
author_sort | Xue, Guangai |
collection | PubMed |
description | The movement of viruses and other large macromolecular cargo through nuclear pore complexes (NPCs) is poorly understood. The human immunodeficiency virus type 1 (HIV-1) provides an attractive model to interrogate this process. HIV-1 capsid (CA), the chief structural component of the viral core, is a critical determinant in nuclear transport of the virus. HIV-1 interactions with NPCs are dependent on CA, which makes direct contact with nucleoporins (Nups). Here we identify Nup35, Nup153, and POM121 to coordinately support HIV-1 nuclear entry. For Nup35 and POM121, this dependence was dependent cyclophilin A (CypA) interaction with CA. Mutation of CA or removal of soluble host factors changed the interaction with the NPC. Nup35 and POM121 make direct interactions with HIV-1 CA via regions containing phenylalanine glycine motifs (FG-motifs). Collectively, these findings provide additional evidence that the HIV-1 CA core functions as a macromolecular nuclear transport receptor (NTR) that exploits soluble host factors to modulate NPC requirements during nuclear invasion. |
format | Online Article Text |
id | pubmed-10290713 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-102907132023-06-26 The HIV-1 capsid core is an opportunistic nuclear import receptor Xue, Guangai Yu, Hyun Jae Buffone, Cindy Huang, Szu-Wei Lee, KyeongEun Goh, Shih Lin Gres, Anna T. Guney, Mehmet Hakan Sarafianos, Stefan G. Luban, Jeremy Diaz-Griffero, Felipe KewalRamani, Vineet N. Nat Commun Article The movement of viruses and other large macromolecular cargo through nuclear pore complexes (NPCs) is poorly understood. The human immunodeficiency virus type 1 (HIV-1) provides an attractive model to interrogate this process. HIV-1 capsid (CA), the chief structural component of the viral core, is a critical determinant in nuclear transport of the virus. HIV-1 interactions with NPCs are dependent on CA, which makes direct contact with nucleoporins (Nups). Here we identify Nup35, Nup153, and POM121 to coordinately support HIV-1 nuclear entry. For Nup35 and POM121, this dependence was dependent cyclophilin A (CypA) interaction with CA. Mutation of CA or removal of soluble host factors changed the interaction with the NPC. Nup35 and POM121 make direct interactions with HIV-1 CA via regions containing phenylalanine glycine motifs (FG-motifs). Collectively, these findings provide additional evidence that the HIV-1 CA core functions as a macromolecular nuclear transport receptor (NTR) that exploits soluble host factors to modulate NPC requirements during nuclear invasion. Nature Publishing Group UK 2023-06-24 /pmc/articles/PMC10290713/ /pubmed/37355754 http://dx.doi.org/10.1038/s41467-023-39146-5 Text en © This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Xue, Guangai Yu, Hyun Jae Buffone, Cindy Huang, Szu-Wei Lee, KyeongEun Goh, Shih Lin Gres, Anna T. Guney, Mehmet Hakan Sarafianos, Stefan G. Luban, Jeremy Diaz-Griffero, Felipe KewalRamani, Vineet N. The HIV-1 capsid core is an opportunistic nuclear import receptor |
title | The HIV-1 capsid core is an opportunistic nuclear import receptor |
title_full | The HIV-1 capsid core is an opportunistic nuclear import receptor |
title_fullStr | The HIV-1 capsid core is an opportunistic nuclear import receptor |
title_full_unstemmed | The HIV-1 capsid core is an opportunistic nuclear import receptor |
title_short | The HIV-1 capsid core is an opportunistic nuclear import receptor |
title_sort | hiv-1 capsid core is an opportunistic nuclear import receptor |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10290713/ https://www.ncbi.nlm.nih.gov/pubmed/37355754 http://dx.doi.org/10.1038/s41467-023-39146-5 |
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