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TRIM5alpha

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HIV Interactions with Host Cell Proteins

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 339))

Abstract

TRIM5α protein blocks retroviral replication at early postentry stage reducing the accumulation of reverse transcriptase products. TRIM5α proteins of Old World primates restrict HIV-1 infection whereas TRIM5α proteins of most New World monkeys restrict SIVmac infection. TRIM5α protein has a RING domain, B-box 2 domain, coiled-coil domain, and PRYSPRY domain. The PRYSPRY domain of TRIM5α determines viral specificity and restriction potency by mediating recognition of the retroviral capsid. The coiled-coil domain is essential for TRIM5α oligomerization, which contributes to binding avidity for the viral capsid. The RING domain and B-box 2 domain are required for efficient restriction activity of TRIM5α protein but the mechanisms remain to be defined.

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Authors and Affiliations

  1. Division of Pediatric Infectious Diseases, Emory University School of Medicine, 2015 Uppergate Drive, Atlanta, GA, 30322, USA

    Byeongwoon Song

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  1. Byeongwoon Song
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Correspondence to Byeongwoon Song .

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  1. School of Medicine, Dept. Pediatrics, Emory University, Uppergate Drive NE., 2015, Atlanta, 30322, Georgia, USA

    Paul Spearman

  2. HIV Drug Resistance Program, National Cancer Institute-Frederick, Frederick, Maryland, USA

    Eric O. Freed

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Song, B. (2009). TRIM5alpha. In: Spearman, P., Freed, E. (eds) HIV Interactions with Host Cell Proteins. Current Topics in Microbiology and Immunology, vol 339. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-02175-6_3

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