Correlated cryogenic fluorescence microscopy and electron cryo-tomography shows that exogenous TRIM5alpha can form hexagonal lattices or autophagy aggregates in vivo.
Categories
Family & Domains, Interaction, Subcellular Location
Variations in Trim5alpha and Cyclophilin A genes among HIV-1 elite controllers and non controllers in Uganda: a laboratory-based cross-sectional study.
apply cryo-electron tomography and subtomogram averaging to determine structures of TRIM5alpha bound to recombinant HIV-1 capsid assemblies. Our data support a mechanism of hierarchical assembly in which a limited number of basal interaction modes are successively organized in increasingly higher-order structures that culminate in a TRIM5alpha cage surrounding a retroviral capsid.
disruption of the capsid protein-CypA interaction renders HIV-1 susceptible to potent restriction by human TRIM5alpha with the block occurring before reverse transcription
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.
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