SignificanceThe main structural component of HIV-1 is the Gag polyprotein. During virus release, Gag is cleaved by the viral protease at five sites, triggering a major change in the structure and morphology of the virus. This transition, called maturation, is required to make an infectious virion. We used cryoelectron tomography to obtain high-resolution structures of Gag inside virus particles carrying mutations that block specific combinations of cleavage sites. Analysis of these structures suggests that different combinations of cleavages can destabilize a bundle of alpha-helices at the C terminus of CA. This destabilization, rather than formation of a beta-hairpin at the N terminus of CA as previously suggested, acts as the structural switch for maturation of the virus into its infectious form.
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