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  • Title: Insight into the Assembly of Viruses with Vertical Single β-barrel Major Capsid Proteins.
    Author: Gil-Carton D, Jaakkola ST, Charro D, Peralta B, Castaño-Díez D, Oksanen HM, Bamford DH, Abrescia NGA.
    Journal: Structure; 2015 Oct 06; 23(10):1866-1877. PubMed ID: 26320579.
    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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