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The Sylvilagus TRIM5 alpha was 91% identical to the Oryctolagus protein.
Human TRIM5alpha G249D mutant, associated with higher susceptibility to HIV-1 infection, formed fewer assemblies than WT protein, in agreement with homology modeling predictions and molecular dynamics simulations of dimers and higher oligomers of TRIM5alpha, providing a mechanistic explanation of the reduced antiviral activity of the G249D polymorphism.
these data suggest that the specific hexagonal geometry of the TRIM5 lattice serves not only to enable virus binding but also to coordinate immune signaling with pathogen recognition.
Trim5alpha binds all mammalian ATG8s and that, unlike the typical LC3-interacting region (LIR) that binds to mammalian ATG8s through a beta-strand motif comprising approximately six residues, LC3B binds to Trim5alpha via the alpha-helical coiled-coil region.
TRIM5alpha haplotypes and the BST-2 i19 allele may significantly affect the modulation of HIV-1 acquisition and its progression. TRIM5alpha rs7127617 CC and BST-2 Delta19/i19 genotypes in alcohol-using HIV patients elevated the risk of HIV disease progression
HIV-1 vectors containing B27/B57+-specific CA had increased sensitivity to TRIM5alpha but not to Mx2. Following exposure to those vectors, cells showed increased resistance against both TRIM5alpha-sensitive and -insensitive HIV-1 strains.
study demonstrates the feasibility of editing the TRIM5 gene in human cells and identifies the main challenges to be addressed in order to use this approach to confer protection from HIV-1
genetic polymorphism is associated with susceptibility to HIV infections in Brazil
TRIM5 and TRIM22 single nucleotide polymorphisms are associated to increased odds of significant liver fibrosis and sustained virological response after pegIFNalpha/RBV therapy in human immunodeficiency virus/hepatitis C virus coinfected patients.
TRIM5alpha polymorphisms were associated with proviral loads, indicating that TRIM5alpha could be implicated in HTLV-1 replication.
TRIM5alpha potently restricts HIV-1 infection of Langerhans cells but not of subepithelial DC-SIGN+ dendritic cells
Collectively, these results are consistent with observations that the turnover of TRIM5alpha proteins is sensitive to autophagy inhibition; however, the data presented here do not support observations that the inhibition of autophagy abrogates retroviral restriction by TRIM5 proteins.
This meta-analysis indicates that TRIM5alpha H43Y polymorphism is associated with a decreased risk of HIV-1 infection in the homozygote comparison and recessive model.
These results support the relevance of R332G-R335G and other mutants of TRIM5alphahu as candidate effectors for HIV-1 gene therapy.
higher-order oligomerization of TRIM5alpha, which is promoted by the interaction with the retroviral capsid, enhances the E3 Ub ligase activity of TRIM5alpha and contributes to its antiretroviral function.
TRIM5alpha requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription.
co-immunoprecipitation experiments demonstrate that IE1CORE binds via the coiled-coil domain to PML and also interacts with TRIM5alpha
Data suggest that due to its lack of stability and inability to accumulate in pronounced cytoplasmic bodies likely due to its high self-ubiquitination activity, huTRIM5alpha was unable to block HIV-1 infection.
TRIM5alpha variations influence transduction efficiency with lentiviral vectors in both human and rhesus CD34(+) cells in vitro and in vivo.
TRIM5 acts as a selective autophagy receptor. Based on direct sequence-specific recognition, TRIM5 delivered its cognate cytosolic target, a viral capsid protein, for autophagic degradation. Thus, our study establishes that TRIMs can function both as regulators of autophagy and as autophagic cargo receptors, and reveals a basis for selective autophagy in mammalian cells.
Data suggest that SPRY domain of TRIM5a is essential in activation of AP-1 signaling but not NF-kappaB signaling in this species. (TRIM5a = tripartite motif-containing 5 alpha isoenzyme; AP-1 = activator 1 protein)
Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5alpha has been reported.
High resolution crystal structure of a Trim5Alpha dimeric Bbox domain.
L2 region of the TRIM5alpha dimer undergoes dynamic conformational changes, which results in the displacement of L2 regions by 25 angstroms relative to each other.
HIV-1 virus target the rhTRIM5alpha enhanced the susceptibility to HIV-1 infection.
Mutations in gag and pol are associated with escape of HIV-1 from rhTrim5alpha.
These studies provide direct evidence that ubiquitin conjugation to rhTRIM5alpha-containing complexes is required for inhibition of HIV-1 Reverse Transcription and Capsid Destabilization.
These results confirm that the SUMO machinery is involved in TRIM5alpha-mediated retroviral restriction, and demonstrate that TRIM5alpha is a SUMO 1 and SUMO 2 substrate.
These data show that there could be some distinct HIV-1 capsid patterns to confer significant resistance to rhesus TRIM5-alpha.
Authors found that TRIM5alpha restriction significantly delayed disease progression and improved the survival rate of simian immunodeficiency virus-infected macaques.
Analysis of TRIM genotype revealed a potential role for TRIM in disease development in the central nervous system. 5 of 5 animals with the permissive TRIM5alpha genotype (TRIMQ/Q) progressed to Simian Immunodeficiency Virus Encephalitis. In contrast, 2 animals with the restrictive TRIM5alpha genotype (TRIMTFP/TFP) did not show neurologic signs, nor did they develop SIVE.
Data show that rhTRIM5alpha is stable and able to accumulate in cytoplasmic bodies, as well as to potently block HIV-1 infection.
Rhesus TRIM5alpha acts as an autophagic receptor to restrict HIV-1 through autophagic degradation.
In conclusion, the TRIM5alpha sumoylation site appears to modulate the E3 ubiquitin ligase activities of the adjacent RING domain, promoting K63-linked ubiquitin chains at the expense of auto-ubiquitylation which is probably K48-linked.
The antiparallel organization of the NtD regions of Fv1 and Trim5alpha dimers correctly positions C-terminal specificity and N-terminal effector domains and facilitates stable binding to adjacent capsid hexamers in viral cores.
Taken together, it is likely that rhTRIM5alpha cytoplasmic bodies are involved in recruiting components of the ubiquitin-proteasome system to coordinate proteasomal destruction of a viral or cellular protein(s) during restriction of HIV-1.
Assisted evolution enables HIV-1 to overcome a high TRIM5alpha-imposed genetic barrier to rhesus macaque tropism.
direct evidence that TRIM5alpha exerts selective pressure on the cross-species transmission of SIV in primates.
PRYSPRY domain serves an unknown function, distinct from the binding of TRIM5alpharh to the HIV-1 core.
TRIM5alpha protein functionally resembled human TRIM5alpha, potently restricting infection by N-tropic murine leukemia virus (N-MLV) and moderately restricting human immunodeficiency virus type 1 (HIV-1) infection
SPRY domain of TRIM5alpha showed higher nonsynon/synonymous substitution ratios than the non-SPRY domain, indicating that the adaptive evolution of TRIM5alpha might be a strategy developed in defending retrovirus infection during primate evolution.
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein forms homo-oligomers via the coilel-coil region and localizes to cytoplasmic bodies. It appears to function as a E3 ubiquitin-ligase and ubiqutinates itself to regulate its subcellular localization. It may play a role in retroviral restriction. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene.
tripartite motif-containing 5
, tripartite motif-containing 5 alpha
, tripartite motif-containing protein 5
, tri-partite motif protein 5
, ring finger protein 88
, tripartite motif containing 5 transcript variant iota
, tripartite motif containing 5 transcript variant kappa
, tripartite motif protein TRIM5
, tripartite motif-containing protein 5 isoform alpha
, TRIM5 alpha