Structure and assembly mechanism of virus-associated pyramids
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Viruses have developed intricate molecular machines to infect, replicate within and escape from their host cells. Perhaps one of the most intriguing of these mechanisms is the pyramidal egress structure that has evolved in archaeal viruses, such as SIRV2 or STIV1. The structure and mechanism of these virus-associated pyramids (VAPs) has been studied by cryo-electron tomography and complementary biochemical techniques, revealing that VAPs are formed by multiple copies of a virus-encoded 10-kDa protein (PVAP) that integrate into the cell membrane and assemble into hollow, sevenfold symmetric pyramids. In this process, growing VAPs puncture the protective surface layer and ultimately open to release newly replicated viral particles into the surrounding medium. PVAP has the striking capability to spontaneously integrate and self-assemble into VAPs in biological membranes of the archaea, bacteria and eukaryotes. This renders the VAP a universal membrane remodelling system. In this review, we provide an overview of the VAP structure and assembly mechanism and discuss the possible use of VAPs in nano-biotechnology.
KeywordsArchaeal virus Nanostructure Archaea Sulfolobus Cryo-electron tomography Virion egress
This work was supported by a Marie-Curie Intra-European fellowship, a Post-doctoral grant from the Carl-Zeiss-Stiftung to T.E.F. Quax and a Research Fellow’s Start-up Grant by the University of Exeter to B. Daum.
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Conflict of interest
Tessa E.F. Quax declares that she has no conflicts of interest. Bertram Daum declares that he has no conflicts of interest.
This article does not contain any studies with human participants or animals performed by any of the authors.
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