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

Bertram Daum, Tessa Quax, Martin Sachse, Deryck J. Mills, Ozkan Yildiz, Sabine Haeder, Cosmin Saveanu, Patrick Forterre, Sonja Albers, Werner Kuehlbrandt*, David Prangishvili*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

41 Citations (Scopus)

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 biological membrane, where it forms sevenfold pyramids. We identify the protein domains essential for VAP formation in PVAP truncation mutants by their ability to remodel the cell membrane. Self-assembly of PVAP into pyramids requires at least two different, in-plane and out-of-plane, protein interactions. Our findings allow us to propose a model describing how PVAP arranges to form sevenfold pyramids and suggest how this small, robust protein may be used as a general membrane-remodeling system.
Original languageEnglish
Article number1319245111
Pages (from-to)3829-3834
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume111
Issue number10
DOIs
Publication statusPublished - Mar-2014
Externally publishedYes

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