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Caging the Beast: TRIM5α Binding to the HIV-1 Core
The potent HIV-1 inhibitor TRIM5α blocks HIV-1 infection by accelerating the uncoating of HIV-1. TRIM5α is known to form higher-order self-association complexes that contribute to the avidity of TRIM5α for the HIV-1 capsid, and are essential to inhibit infection; these higher-order self-association...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Molecular Diversity Preservation International (MDPI)
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3186010/ https://www.ncbi.nlm.nih.gov/pubmed/21994740 http://dx.doi.org/10.3390/v3050423 |
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author | Diaz-Griffero, Felipe |
author_facet | Diaz-Griffero, Felipe |
author_sort | Diaz-Griffero, Felipe |
collection | PubMed |
description | The potent HIV-1 inhibitor TRIM5α blocks HIV-1 infection by accelerating the uncoating of HIV-1. TRIM5α is known to form higher-order self-association complexes that contribute to the avidity of TRIM5α for the HIV-1 capsid, and are essential to inhibit infection; these higher-order self-association complexes are dependent upon an intact B-box 2 domain. Even though the ability to form higher-order self-association complexes resembles the clathrin triskelion that forms a protein array, or cage, around the endocytic vesicle, evidence for the ability of TRIM5α to assemble a similar type of structure surrounding the HIV-1 core has been lacking. Recent work by Ganser-Pornillos, Chandrasekaran and colleagues has now demonstrated the ability of the restriction factor TRIM5α to “cage” or “net” the HIV-1 core by forming an hexagonal array on the surface of the viral capsid [1]. This hexagonal array is strikingly similar in design to the array formed by the clathrin triskelion on the surface of the clathrin-coated endocytic vesicle. This remarkable finding represents an important advance on our understanding of the restriction factor TRIM5α, and suggests that TRIM5α cages the HIV-1 core in order to terminate infection. The present note discusses the implications of this discovery. |
format | Online Article Text |
id | pubmed-3186010 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-31860102011-10-12 Caging the Beast: TRIM5α Binding to the HIV-1 Core Diaz-Griffero, Felipe Viruses Commentary The potent HIV-1 inhibitor TRIM5α blocks HIV-1 infection by accelerating the uncoating of HIV-1. TRIM5α is known to form higher-order self-association complexes that contribute to the avidity of TRIM5α for the HIV-1 capsid, and are essential to inhibit infection; these higher-order self-association complexes are dependent upon an intact B-box 2 domain. Even though the ability to form higher-order self-association complexes resembles the clathrin triskelion that forms a protein array, or cage, around the endocytic vesicle, evidence for the ability of TRIM5α to assemble a similar type of structure surrounding the HIV-1 core has been lacking. Recent work by Ganser-Pornillos, Chandrasekaran and colleagues has now demonstrated the ability of the restriction factor TRIM5α to “cage” or “net” the HIV-1 core by forming an hexagonal array on the surface of the viral capsid [1]. This hexagonal array is strikingly similar in design to the array formed by the clathrin triskelion on the surface of the clathrin-coated endocytic vesicle. This remarkable finding represents an important advance on our understanding of the restriction factor TRIM5α, and suggests that TRIM5α cages the HIV-1 core in order to terminate infection. The present note discusses the implications of this discovery. Molecular Diversity Preservation International (MDPI) 2011-04-27 /pmc/articles/PMC3186010/ /pubmed/21994740 http://dx.doi.org/10.3390/v3050423 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Commentary Diaz-Griffero, Felipe Caging the Beast: TRIM5α Binding to the HIV-1 Core |
title | Caging the Beast: TRIM5α Binding to the HIV-1 Core |
title_full | Caging the Beast: TRIM5α Binding to the HIV-1 Core |
title_fullStr | Caging the Beast: TRIM5α Binding to the HIV-1 Core |
title_full_unstemmed | Caging the Beast: TRIM5α Binding to the HIV-1 Core |
title_short | Caging the Beast: TRIM5α Binding to the HIV-1 Core |
title_sort | caging the beast: trim5α binding to the hiv-1 core |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3186010/ https://www.ncbi.nlm.nih.gov/pubmed/21994740 http://dx.doi.org/10.3390/v3050423 |
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