Novel Escape Mutants Suggest an Extensive TRIM5α Binding Site Spanning the Entire Outer Surface of the Murine Leukemia Virus Capsid Protein - Wikidata - wikimedia - TriplyDB

Novel Escape Mutants Suggest an Extensive TRIM5α Binding Site Spanning the Entire Outer Surface of the Murine Leukemia Virus Capsid Protein

Novel Escape Mutants Suggest an Extensive TRIM5α Binding Site Spanning the Entire Outer Surface of the Murine Leukemia Virus Capsid Protein

http://www.wikidata.org/entity/Q27667494

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Impact of TRIM5α in vivo Structure of the rhesus monkey TRIM5 PRYSPRY domain, the HIV capsid recognition module Structural insight into HIV-1 capsid recognition by rhesus TRIM5 Gain-of-Sensitivity Mutations in a Trim5-Resistant Primary Isolate of Pathogenic SIV Identify Two Independent Conserved Determinants of Trim5α Specificity A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice Fates of retroviral core components during unrestricted and TRIM5-restricted infection Tracking interspecies transmission and long-term evolution of an ancient retrovirus using the genomes of modern mammals Rhesus monkey TRIM5α SPRY domain recognizes multiple epitopes that span several capsid monomers on the surface of the HIV-1 mature viral core Apparent effect of rabbit endogenous lentivirus type K acquisition on retrovirus restriction by lagomorph Trim5αs Pandemic influenza A viruses escape from restriction by human MxA through adaptive mutations in the nucleoprotein.Functional evidence for the involvement of microtubules and dynein motor complexes in TRIM5α-mediated restriction of retroviruses.Host and viral determinants of Mx2 antiretroviral activity Intracellular immunity: finding the enemy within--how cells recognize and respond to intracellular pathogens Assisted evolution enables HIV-1 to overcome a high TRIM5α-imposed genetic barrier to rhesus macaque tropism.Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.The fate of HIV-1 capsid: a biochemical assay for HIV-1 uncoating Potent restriction of HIV-1 and SIVmac239 replication by African green monkey TRIM5α.Crystal structure of TRIM20 C-terminal coiled-coil/B30.2 fragment: implications for the recognition of higher order oligomers RING domain mutations uncouple TRIM5α restriction of HIV-1 from inhibition of reverse transcription and acceleration of uncoating Evolutionary and Functional Analysis of Old World Primate TRIM5 Reveals the Ancient Emergence of Primate Lentiviruses and Convergent Evolution Targeting a Conserved Capsid Interface The Ty1 Retrotransposon Restriction Factor p22 Targets Gag.Role of Human TRIM5α in Intrinsic Immunity.Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid.The gammaretroviral p12 protein has multiple domains that function during the early stages of replication.Inhibition of reverse transcriptase activity increases stability of the HIV-1 core.Cyclophilin A-dependent restriction to capsid N121K mutant human immunodeficiency virus type 1 in a broad range of cell lines A comparison of murine leukemia viruses that escape from human and rhesus macaque TRIM5αs.Contributions of Charged Residues in Structurally Dynamic Capsid Surface Loops to Rous Sarcoma Virus Assembly.Virus-specific effects of TRIM5α(rh) RING domain functions on restriction of retroviruses.Generation of rhesus macaque-tropic HIV-1 clones that are resistant to major anti-HIV-1 restriction factors.Design of a novel integration-deficient lentivector technology that incorporates genetic and posttranslational elements to target human dendritic cells.N-linked glycosylation protects gammaretroviruses against deamination by APOBEC3 proteins.HIV-1 Capsid Stabilization Assay.Binding of the rhesus TRIM5α PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restriction.Human cytosolic extracts stabilize the HIV-1 core A general model for retroviral capsid pattern recognition by TRIM5 proteins.

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Novel Escape Mutants Suggest an Extensive TRIM5α Binding Site Spanning the Entire Outer Surface of the Murine Leukemia Virus Capsid Protein

http://www.wikidata.org/entity/Q27667494

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2011 nî lūn-bûn

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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JOURNAL.PPAT.1002011

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Ian A Taylor

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Kate Holden-Dye

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Melvyn W Yap

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Sadayuki Ohkura

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P2860

Genomic analysis of the TRIM family reveals two groups of genes with distinct evolutionary properties

The tripartite motif family identifies cell compartments.

TRIM family proteins: retroviral restriction and antiviral defence

Proteasome inhibitors uncouple rhesus TRIM5alpha restriction of HIV-1 reverse transcription and infection

Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5alpha restriction factor

Trim5alpha protein restricts both HIV-1 and murine leukemia virus

The human and African green monkey TRIM5alpha genes encode Ref1 and Lv1 retroviral restriction factor activities

Retrovirus resistance factors Ref1 and Lv1 are species-specific variants of TRIM5alpha

All three variable regions of the TRIM5alpha B30.2 domain can contribute to the specificity of retrovirus restriction

Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function

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Jonathan P. Stoye

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