Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly

摘要: The assembly of HIV-1 is mediated by oligomerization the major structural polyprotein, Gag, into a hexameric protein lattice at plasma membrane infected cell. This leads to budding and release progeny immature virus particles. Subsequent proteolytic cleavage Gag triggers rearrangement particles form mature infectious virions. Obtaining model assembled within necessary understand interactions that mediate in cell, describe substrate subsequently cleaved viral protease. An 8-A resolution structure an virus-like tubular array from Gag-derived related retrovirus Mason–Pfizer monkey (M-PMV) has previously been reported, for arrangement capsid (CA) domains generated based on homology this structure. Here we have arrays with immature-like C-terminal CA solved their using hybrid cryo-EM tomography analysis. reveals domain lattice, provides, our knowledge, first high-resolution view region immediately downstream CA, which essential assembly, significantly different respective M-PMV. Our results reveal hollow column density compatible presence six-helix bundle position.