Self-assembly of the general membrane-remodeling protein PVAP into sevenfold virus-associated pyramids.

ABSTRACT: Viruses have developed a wide range of strategies to escape from the host cells in which they replicate. For egress some archaeal viruses use a pyramidal structure with sevenfold rotational symmetry. Virus-associated pyramids (VAPs) assemble in the host cell membrane from the virus-encoded protein PVAP and open at the end of the infection cycle. We characterize this unusual supramolecular assembly using a combination of genetic, biochemical, and electron microscopic techniques. By whole-cell electron cryotomography, we monitored morphological changes in virus-infected host cells. Subtomogram averaging reveals the VAP structure. By heterologous expression of PVAP in cells from all three domains of life, we demonstrate that the protein integrates indiscriminately into virtually any biologica

SUBMITTER: Daum B 

PROVIDER: S-EPMC3956195 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature