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Related Experiment Video

Updated: Jun 17, 2026

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

TRIM5alpha.

Byeongwoon Song1

  • 1Division of Pediatric Infectious Diseases, Emory University School of Medicine, 2015 Uppergate Drive, Atlanta, GA 30322, USA. bsong4@emory.edu

Current Topics in Microbiology and Immunology
|December 17, 2009
PubMed
Summary
This summary is machine-generated.

TRIM5alpha protein restricts retroviral replication by recognizing viral capsid. Its PRYSPRY domain dictates viral specificity, while other domains are crucial for its function.

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Last Updated: Jun 17, 2026

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

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Published on: June 14, 2017

Vasodilation of Isolated Vessels and the Isolation of the Extracellular Matrix of Tight-skin Mice
08:09

Vasodilation of Isolated Vessels and the Isolation of the Extracellular Matrix of Tight-skin Mice

Published on: March 24, 2017

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • TRIM5alpha protein is a key innate immune sensor that restricts retroviral infection.
  • Primate TRIM5alpha exhibits distinct specificities, restricting HIV-1 in Old World monkeys and SIVmac in New World monkeys.

Purpose of the Study:

  • To elucidate the structural and functional domains of TRIM5alpha protein involved in retroviral restriction.
  • To understand the molecular mechanisms underlying TRIM5alpha-mediated viral specificity and restriction potency.

Main Methods:

  • Analysis of TRIM5alpha protein domains (RING, B-box 2, coiled-coil, PRYSPRY).
  • Investigating the role of these domains in viral capsid recognition and binding avidity.
  • Assessing the contribution of TRIM5alpha domains to restriction activity.

Main Results:

  • The PRYSPRY domain mediates recognition of the retroviral capsid, determining viral specificity and restriction.
  • The coiled-coil domain is essential for TRIM5alpha oligomerization, enhancing capsid binding.
  • The RING and B-box 2 domains are necessary for efficient restriction, though their precise mechanisms require further study.

Conclusions:

  • TRIM5alpha utilizes distinct domains for viral recognition, oligomerization, and restriction.
  • Understanding TRIM5alpha's structure-function relationship is critical for developing antiviral strategies.