ArticlePLoS pathogens2011
Novel escape mutants suggest an extensive TRIM5α binding site spanning the entire outer surface of the murine leukemia virus capsid protein.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 51 citations in OpenAlex.
- An ancient alpharetrovirus lineage in bats: Evolutionary insights and possible roles in reproduction.PLoS genetics · 2026Article
- Characterization of Megabat-Favored, CA-Dependent Susceptibility to Retrovirus Infection.Journal of virology · 2023Article
- Mapping of molecular interactions between human E3 ligase TRIM69 and Dengue virus NS3 protease using hydrogen-deuterium exchange mass spectrometry.Cellular and molecular life sciences : CMLS · 2022Article
- HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules.Retrovirology · 2021Review
- Hierarchical assembly governs TRIM5α recognition of HIV-1 and retroviral capsids.Science advances · 2019Article
- Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019Review
- Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5α identified by magic-angle spinning NMR and molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- General Model for Retroviral Capsid Pattern Recognition by TRIM5 Proteins.Journal of virology · 2018Article
- Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid.PLoS pathogens · 2016Article
- Contributions of Charged Residues in Structurally Dynamic Capsid Surface Loops to Rous Sarcoma Virus Assembly.Journal of virology · 2016Article
- Article
- HIV-1 Capsid Stabilization Assay.Methods in molecular biology (Clifton, N.J.) · 2016Article
- The Ty1 Retrotransposon Restriction Factor p22 Targets Gag.PLoS genetics · 2015Article
- Impact of TRIM5α in vivo.AIDS (London, England) · 2015Review
- Evolutionary and Functional Analysis of Old World Primate TRIM5 Reveals the Ancient Emergence of Primate Lentiviruses and Convergent Evolution Targeting a Conserved Capsid Interface.PLoS pathogens · 2015Article
- Crystal structure of TRIM20 C-terminal coiled-coil/B30.2 fragment: implications for the recognition of higher order oligomers.Scientific reports · 2015Article
- Potent restriction of HIV-1 and SIVmac239 replication by African green monkey TRIM5α.Retrovirology · 2015Article
- N-linked glycosylation protects gammaretroviruses against deamination by APOBEC3 proteins.Journal of virology · 2015Article
- Intracellular immunity: finding the enemy within--how cells recognize and respond to intracellular pathogens.Journal of leukocyte biology · 2014Article
- Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
After entry into target cells, retroviruses encounter the host restriction factors such as Fv1 and TRIM5α. While it is clear that these factors target retrovirus capsid proteins (CA), recognition remains poorly defined in the absence of structural information. To better understand the binding interaction between TRIM5α and CA, we selected a panel of novel N-tropic murine leukaemia virus (N-MLV) escape mutants by a serial passage of replication competent N-MLV in rhesus macaque TRIM5α (rhTRIM5α)-positive cells using a small percentage of unrestricted cells to allow multiple rounds of virus replication. The newly identified mutations, many of which involve changes in charge, are distributed over the outer 'top' surface of N-MLV CA, including the N-terminal β-hairpin, and map up to 29 A(o) apart. Biological characterisation with a number of restriction factors revealed that only one of the new mutations affects restriction by human TRIM5α, indicating significant differences in the binding interaction between N-MLV and the two TRIM5αs, whereas three of the mutations result in dual sensitivity to Fv1(n) and Fv1(b). Structural studies of two mutants show that no major changes in the overall CA conformation are associated with escape from restriction. We conclude that interactions involving much, if not all, of the surface of CA are vital for TRIM5α binding.
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