NDLI: Structure of the rhesus monkey TRIM5α PRYSPRY domain, the HIV capsid recognition module

Content Provider	PubMed Central
Author	Biris, Nikolaos Yang, Yang Taylor, Alexander B. Andrei, Tomashevski Guo, Miao Hart, P. John Felipe, Diaz-griffero Ivanov, Dmitri N.
Abstract	Tripartite motif protein TRIM5α blocks retroviral replication after cell entry, and species-specific differences in its activity are determined by sequence variations within the C-terminal B30.2/PRYSPRY domain. Here we report a high-resolution structure of a TRIM5α PRYSPRY domain, the PRYSPRY of the rhesus monkey TRIM5α that potently restricts HIV infection, and identify features involved in its interaction with the HIV capsid. The extensive capsid-binding interface maps on the structurally divergent face of the protein formed by hypervariable loop segments, confirming that TRIM5α evolution is largely determined by its binding specificity. Interactions with the capsid are mediated by flexible variable loops via a mechanism that parallels antigen recognition by IgM antibodies, a similarity that may help explain some of the unusual functional properties of TRIM5α. Distinctive features of this pathogen-recognition interface, such as structural plasticity conferred by the mobile v1 segment and interaction with multiple epitopes, may allow restriction of divergent retroviruses and increase resistance to capsid mutations.
Related Links	http://dx.doi.org/10.1073/pnas.1203536109
Ending Page	13283
Page Count	6
Starting Page	13278
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	33
Volume Number	109
Language	English
Publisher	National Academy of Sciences
Publisher Date	2012-08-14
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
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3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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Binding of the Rhesus TRIM5α PRYSPRY Domain to Capsid is Necessary but not Sufficient for HIV-1 Restriction

Structure of the rhesus monkey TRIM5 PRYSPRY domain, the HIV capsid recognition module.

Structural insight into HIV-1 capsid recognition by rhesus TRIM5α

Rhesus Monkey TRIM5α SPRY Domain Recognizes Multiple Epitopes That Span Several Capsid Monomers on the Surface of the HIV-1 Mature Viral Core

Recognition of the HIV Capsid by the TRIM5α Restriction Factor Is Mediated by a Subset of Pre-Existing Conformations of the TRIM5α SPRY Domain

Adaptation of HIV-1 to Cells Expressing Rhesus Monkey TRIM5α

An Invariant Surface Patch on the TRIM5α PRYSPRY Domain Is Required for Retroviral Restriction but Dispensable for Capsid Binding▿

Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection

Multiple sites in the N-terminal half of simian immunodeficiency virus capsid protein contribute to evasion from rhesus monkey TRIM5α-mediated restriction

Structure of the rhesus monkey TRIM5α PRYSPRY domain, the HIV capsid recognition module

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Binding of the Rhesus TRIM5α PRYSPRY Domain to Capsid is Necessary but not Sufficient for HIV-1 Restriction

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