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Viruses 2011, 3(5), 423-428; doi:10.3390/v3050423
Commentary

Caging the Beast: TRIM5α Binding to the HIV-1 Core

Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
Received: 16 March 2011 / Revised: 21 April 2011 / Accepted: 21 April 2011 / Published: 27 April 2011
(This article belongs to the Section Editorial)
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Abstract

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.
Keywords: HIV-1; TRIM5α; capsid; binding; core HIV-1; TRIM5α; capsid; binding; core
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Diaz-Griffero, F. Caging the Beast: TRIM5α Binding to the HIV-1 Core. Viruses 2011, 3, 423-428.

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