Caging the beast

TRIM5α binding to the HIV-1 core

Research output: Contribution to journalArticle

12 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)423-428
Number of pages6
JournalViruses
Volume3
Issue number5
DOIs
StatePublished - May 2011

Fingerprint

HIV-1
Transport Vesicles
Clathrin
Capsid
Clathrin-Coated Vesicles
Protein Array Analysis
Infection
HIV Infections

Keywords

  • Binding
  • Capsid
  • Core
  • HIV-1
  • TRIM5α

ASJC Scopus subject areas

  • Infectious Diseases
  • Virology

Cite this

Caging the beast : TRIM5α binding to the HIV-1 core. / Diaz-Griffero, Felipe.

In: Viruses, Vol. 3, No. 5, 05.2011, p. 423-428.

Research output: Contribution to journalArticle

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