Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding

Hassan Javanbakht; Wen Yuan; Darwin F. Yeung; Byeongwoon Song; Felipe Diaz-Griffero; Yuan Li; Xing Li; Matthew Stremlau; Joseph Sodroski

doi:10.1016/j.virol.2006.05.017

Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding

Hassan Javanbakht, Wen Yuan, Darwin F. Yeung, Byeongwoon Song, Felipe Diaz-Griffero, Yuan Li, Xing Li, Matthew Stremlau, Joseph Sodroski

Research output: Contribution to journal › Article › peer-review

107 Scopus citations

Abstract

The coiled-coil domain of the tripartite motif (TRIM) family protein TRIM5α is required for trimerization and function as an antiretroviral restriction factor. Unlike the coiled-coil regions of other related TRIM proteins, the coiled coil of TRIM5α is not sufficient for multimerization. The linker region between the coiled-coil and B30.2 domains is necessary for efficient TRIM5α trimerization. Most of the hydrophilic residues predicted to be located on the surface-exposed face of the coiled coil can be altered without compromising TRIM5α antiviral activity against human immunodeficiency virus (HIV-1). However, changes that disrupt TRIM5α trimerization proportionately affect the ability of TRIM5α to bind HIV-1 capsid complexes. Therefore, TRIM5α trimerization makes a major contribution to its avidity for the retroviral capsid, and to the ability to restrict virus infection.

Original language	English (US)
Pages (from-to)	234-246
Number of pages	13
Journal	Virology
Volume	353
Issue number	1
DOIs	https://doi.org/10.1016/j.virol.2006.05.017
State	Published - Sep 15 2006
Externally published	Yes

Keywords

Coiled-coil domain
HIV-1
Retroviral capsid
TRIM5α
Trimerization

ASJC Scopus subject areas

Virology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.virol.2006.05.017

Cite this

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title = "Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding",

abstract = "The coiled-coil domain of the tripartite motif (TRIM) family protein TRIM5α is required for trimerization and function as an antiretroviral restriction factor. Unlike the coiled-coil regions of other related TRIM proteins, the coiled coil of TRIM5α is not sufficient for multimerization. The linker region between the coiled-coil and B30.2 domains is necessary for efficient TRIM5α trimerization. Most of the hydrophilic residues predicted to be located on the surface-exposed face of the coiled coil can be altered without compromising TRIM5α antiviral activity against human immunodeficiency virus (HIV-1). However, changes that disrupt TRIM5α trimerization proportionately affect the ability of TRIM5α to bind HIV-1 capsid complexes. Therefore, TRIM5α trimerization makes a major contribution to its avidity for the retroviral capsid, and to the ability to restrict virus infection.",

keywords = "Coiled-coil domain, HIV-1, Retroviral capsid, TRIM5α, Trimerization",

author = "Hassan Javanbakht and Wen Yuan and Yeung, {Darwin F.} and Byeongwoon Song and Felipe Diaz-Griffero and Yuan Li and Xing Li and Matthew Stremlau and Joseph Sodroski",

note = "Funding Information: We thank Ms. Yvette McLaughlin and Ms. Lisa Bradbury for manuscript preparation, and the National Institutes of Health (AI063987, HL54785, AI45405, and a Center for AIDS Research Award [AI28691]), the International AIDS Vaccine Initiative, the Bristol-Myers Squibb Foundation, and the late William F. McCarty-Cooper. H.J. was supported by a fellowship from the Canadian Institutes of Health Research and by the William A. Haseltine Foundation for the Arts and Sciences. M.S. was supported by a National Defense Science and Engineering Fellowship and is a Fellow of the Ryan Foundation.",

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T1 - Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding

AU - Javanbakht, Hassan

AU - Yuan, Wen

AU - Yeung, Darwin F.

AU - Song, Byeongwoon

AU - Diaz-Griffero, Felipe

AU - Li, Yuan

AU - Li, Xing

AU - Stremlau, Matthew

AU - Sodroski, Joseph

N1 - Funding Information: We thank Ms. Yvette McLaughlin and Ms. Lisa Bradbury for manuscript preparation, and the National Institutes of Health (AI063987, HL54785, AI45405, and a Center for AIDS Research Award [AI28691]), the International AIDS Vaccine Initiative, the Bristol-Myers Squibb Foundation, and the late William F. McCarty-Cooper. H.J. was supported by a fellowship from the Canadian Institutes of Health Research and by the William A. Haseltine Foundation for the Arts and Sciences. M.S. was supported by a National Defense Science and Engineering Fellowship and is a Fellow of the Ryan Foundation.

PY - 2006/9/15

Y1 - 2006/9/15

N2 - The coiled-coil domain of the tripartite motif (TRIM) family protein TRIM5α is required for trimerization and function as an antiretroviral restriction factor. Unlike the coiled-coil regions of other related TRIM proteins, the coiled coil of TRIM5α is not sufficient for multimerization. The linker region between the coiled-coil and B30.2 domains is necessary for efficient TRIM5α trimerization. Most of the hydrophilic residues predicted to be located on the surface-exposed face of the coiled coil can be altered without compromising TRIM5α antiviral activity against human immunodeficiency virus (HIV-1). However, changes that disrupt TRIM5α trimerization proportionately affect the ability of TRIM5α to bind HIV-1 capsid complexes. Therefore, TRIM5α trimerization makes a major contribution to its avidity for the retroviral capsid, and to the ability to restrict virus infection.

AB - The coiled-coil domain of the tripartite motif (TRIM) family protein TRIM5α is required for trimerization and function as an antiretroviral restriction factor. Unlike the coiled-coil regions of other related TRIM proteins, the coiled coil of TRIM5α is not sufficient for multimerization. The linker region between the coiled-coil and B30.2 domains is necessary for efficient TRIM5α trimerization. Most of the hydrophilic residues predicted to be located on the surface-exposed face of the coiled coil can be altered without compromising TRIM5α antiviral activity against human immunodeficiency virus (HIV-1). However, changes that disrupt TRIM5α trimerization proportionately affect the ability of TRIM5α to bind HIV-1 capsid complexes. Therefore, TRIM5α trimerization makes a major contribution to its avidity for the retroviral capsid, and to the ability to restrict virus infection.

KW - Coiled-coil domain

KW - HIV-1

KW - Retroviral capsid

KW - TRIM5α

KW - Trimerization

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Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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