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

• DOI: 10.1073/pnas.1319245111
• Publication Date: 2014-02-25T02:44:15Z
• Authors: Bertram Daum; Tessa E. F. Quax; Martin Sachse; Deryck J. Mills; Julia Reimann; Özkan Yildiz; Sabine Häder; Cosmin Saveanu; Patrick Forterre; Sonja-Verena Albers; Werner Kühlbrandt; David Prangishvili
• Keywords: Models, Molecular; 0301 basic medicine; 570; 0303 health sciences; archaea; Protein Conformation; Cell Membrane; Cryoelectron Microscopy; archeovirus; Molecular; Saccharomyces cerevisiae; 630; Rudiviridae; Sulfolobus; 3. Good health; [SDV] Life Sciences [q-bio]; viral egress; Viral Proteins; 03 medical and health sciences; Models; Multiprotein Complexes; Escherichia coli; [SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology; Virus Release; Plasmids

Significance The Sulfolobus islandicus rod-shaped virus 2 (SIRV2) has developed unique mechanisms to penetrate the plasma membrane and S-layer of its host in order leave cell after replication. SIRV2 encodes 10-kDa protein PVAP, which assembles into sevenfold symmetric virus-associated pyramids (VAPs) membrane. Toward end viral replication cycle, these VAPs open form pores through S-layer, allowing egress. Here we show that PVAP inserts spontaneously forms any kind biological By electron cryotomography have obtained a 3D map VAP present model describing assembly VAPs. Our findings new avenues for large variety biotechnological applications.