Insight into the Assembly of Viruses with Vertical Single β-barrel Major Capsid Proteins

Structure
David Gil-CartonNicola G A Abrescia

Abstract

Archaeal viruses constitute the least explored niche within the virosphere. Structure-based approaches have revealed close relationships between viruses infecting organisms from different domains of life. Here, using biochemical and cryo-electron microscopy techniques, we solved the structure of euryarchaeal, halophilic, internal membrane-containing Haloarcula hispanica icosahedral virus 2 (HHIV-2). We show that the density of the two major capsid proteins (MCPs) recapitulates vertical single β-barrel proteins and that disulfide bridges stabilize the capsid. Below, ordered density is visible close to the membrane and at the five-fold vertices underneath the host-interacting vertex complex underpinning membrane-protein interactions. The HHIV-2 structure exemplifies the division of conserved architectural elements of a virion, such as the capsid, from those that evolve rapidly due to selective environmental pressure such as host-recognizing structures. We propose that in viruses with two vertical single β-barrel MCPs the vesicle is indispensable, and membrane-protein interactions serve as protein-railings for guiding the assembly.

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Citations

Oct 9, 2015·Structure·Rajeshwer S SankhalaGino Cingolani
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Mar 14, 2019·Nature Communications·Isaac Santos-PérezNicola G A Abrescia
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Nov 25, 2018·Virology Journal·Carmen San Martín, Mark J van Raaij
Jun 27, 2019·Current Opinion in Virology·Ross HartmanCharles Martin Lawrence

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