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Related Experiment Video

Updated: Mar 20, 2026

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids.

Yen-Li Li¹, Viswanathan Chandrasekaran¹, Stephen D Carter²

¹Department of Biochemistry, University of Utah, Salt Lake City, United States.

|June 3, 2016

Summary

TRIM5 proteins form hexagonal nets to recognize retroviral capsids, blocking infection. This conserved assembly mechanism allows TRIM5 to adapt and bind diverse viral structures.

Keywords:

HIV-1 TRIM5 capsid hexagonal assembly human immunology infectious disease microbiology restriction virus

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Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

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Published on: September 14, 2014

Area of Science:

Virology
Structural Biology
Immunology

Background:

TRIM5 proteins act as restriction factors against retroviral infections.
Capsid recognition by TRIM5 is mediated by C-terminal SPRY or cyclophilin A domains and N-terminal TRIM motifs.
Efficient recognition relies on oligomerization and avidity effects.

Purpose of the Study:

To investigate the assembly and capsid recognition mechanisms of TRIM5 proteins.
To characterize the structural basis of TRIM5-capsid interactions.

Main Methods:

Isolation of native recombinant TRIM5 proteins.
Purification of stable HIV-1 capsids.
Biochemical and electron microscopy (EM) analyses.

Main Results:

TRIM5 proteins self-assemble into hexagonal nets.
These hexagonal nets bind to viral capsid surfaces.
TRIM5 assemblies form open hexameric rings with specific domain positioning (SPRY at edges, B-box/RING at vertices).

Conclusions:

Hexagonal TRIM5 assembly and capsid pattern recognition principles are conserved across primates.
This conserved mechanism provides conformational plasticity for recognizing diverse retroviral capsids.
TRIM5's hexagonal assembly is key to its broad antiviral activity.