The human immunodeficiency virus (HIV) uses enclosing capsid (CA) proteins to package and release its genetic information into newly infected host cells. CA forms fullerene cones that compartmentalize viral RNA. TRIM5 is an important antiretroviral restriction factor found in rhesus macaques that blocks HIV infection. Recent cryo-electron tomography analysis demonstrate cytoplasmic TRIM5 self-assembles into hexagonally patterned nets that encage mature capsids, with a symmetry and spacing that matches the underlying CA lattice. In this work, we use coarse-grained and atomistic simulations to probe the structural and thermodynamic properties TRIM5 assembly and the molecular mechanisms of how TRIM5 recognizes and restricts viral capsid.
