HIV restriction factors and mechanisms of evasion

MH Malim, PD Bieniasz - Cold Spring …, 2012 - perspectivesinmedicine.cshlp.org
Retroviruses have long been a fertile model for discovering host–pathogen interactions and
their associated biological principles and processes. These advances have not only …

Restriction of HIV-1 and other retroviruses by TRIM5

BK Ganser-Pornillos, O Pornillos - Nature Reviews Microbiology, 2019 - nature.com
Mammalian cells express a variety of innate immune proteins—known as restriction factors—
which defend against invading retroviruses such as HIV-1. Two members of the tripartite …

[HTML][HTML] Coarse-grained simulation reveals key features of HIV-1 capsid self-assembly

JMA Grime, JF Dama, BK Ganser-Pornillos… - Nature …, 2016 - nature.com
The maturation of HIV-1 viral particles is essential for viral infectivity. During maturation,
many copies of the capsid protein (CA) self-assemble into a capsid shell to enclose the viral …

[PDF][PDF] Trivalent RING assembly on retroviral capsids activates TRIM5 ubiquitination and innate immune signaling

AJ Fletcher, M Vaysburd, S Maslen, J Zeng… - Cell host & …, 2018 - cell.com
TRIM5 is a RING domain E3 ubiquitin ligase with potent antiretroviral function. TRIM5
assembles into a hexagonal lattice on retroviral capsids, causing envelopment of the …

A B-box 2 surface patch important for TRIM5α self-association, capsid binding avidity, and retrovirus restriction

F Diaz-Griffero, X Qin, F Hayashi, T Kigawa… - Journal of …, 2009 - Am Soc Microbiol
ABSTRACT TRIM5α is a tripartite motif (TRIM) protein that consists of RING, B-box 2, coiled-
coil, and B30. 2 (SPRY) domains. The TRIM5αrh protein from rhesus monkeys recognizes …

[HTML][HTML] Discordant Evolution of the Adjacent Antiretroviral Genes TRIM22 and TRIM5 in Mammals

SL Sawyer, M Emerman, HS Malik - PLoS pathogens, 2007 - journals.plos.org
TRIM5α provides a cytoplasmic block to retroviral infection, and orthologs encoded by some
primates are active against HIV. Here, we present an evolutionary comparison of the TRIM5 …

[HTML][HTML] Interferon-stimulated TRIM69 interrupts dengue virus replication by ubiquitinating viral nonstructural protein 3

K Wang, C Zou, X Wang, C Huang, T Feng… - PLoS …, 2018 - journals.plos.org
In order to eliminate viral infections, hundreds of interferon-stimulated genes (ISGs) are
induced via type I interferons (IFNs). However, the functions and mechanisms of most ISGs …

Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5α

JM Wagner, MD Roganowicz, K Skorupka, SL Alam… - Elife, 2016 - elifesciences.org
Restriction factors and pattern recognition receptors are important components of intrinsic
cellular defenses against viral infection. Mammalian TRIM5α proteins are restriction factors …

The TRIM5α B-box 2 domain promotes cooperative binding to the retroviral capsid by mediating higher-order self-association

X Li, J Sodroski - Journal of virology, 2008 - Am Soc Microbiol
The retroviral restriction factor, TRIM5α, blocks infection of a spectrum of retroviruses soon
after virus entry into the cell. TRIM5α consists of RING, B-box 2, coiled-coil, and B30. 2 …

[HTML][HTML] Proteasomal degradation of TRIM5α during retrovirus restriction

CJ Rold, C Aiken - PLoS pathogens, 2008 - journals.plos.org
The host protein TRIM5α inhibits retroviral infection at an early post-penetration stage by
targeting the incoming viral capsid. While the detailed mechanism of restriction remains …