About: Structural Characterization of the glycoprotein GP2 Core Domain from the CAS Virus, a Novel Arenavirus-like Species

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About: Structural Characterization of the glycoprotein GP2 Core Domain from the CAS Virus, a Novel Arenavirus-like Species Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Structural Characterization of the glycoprotein GP2 Core Domain from the CAS Virus, a Novel Arenavirus-like Species
Creator	Chandran, Kartik Dai, Zhou Liu, Yanyun Toro, Rafael Almo, Steven »more»
source	Elsevier; Medline; PMC
abstract	Fusion of the viral and host cell membranes is a necessary first step for infection by enveloped viruses, and is mediated by the envelope glycoprotein. The transmembrane subunits from the structurally defined “class I” glycoproteins adopt an α-helical “trimer- of-hairpins” conformation during the fusion pathway. Here we present our studies on the envelope glycoprotein transmembrane subunit, GP2, of the CAS virus (CASV). CASV was recently identified from annulated tree boas (Corallus annulatus) with inclusion body disease and is implicated in the disease etiology. We have generated and characterized two protein constructs consisting of the predicted CASV GP2 core domain. The crystal structure of the CASV GP2 post-fusion conformation indicates a trimeric α-helical bundle that is highly similar to those of Ebola Virus (EBOV) and Marburg Virus (MARV) GP2, despite CASV genome homology to arenaviruses. Denaturation studies demonstrate that the stability of CASV GP2 is pH-dependent with higher stability at lower pH; we propose that this behavior is due to a network of interactions among acidic residues that would destabilize the α-helical bundle under conditions where the side chains are deprotonated. The pH-dependent stability of the post-fusion structure has been observed in EBOV and MARV GP2, as well as other viruses that enter via the endosome. Infection experiments with CASV and the related Golden Gate Virus (GGV) support a mechanism of entry that requires endosomal acidification. Our results suggest that despite being primarily arenavirus-like, the transmembrane subunit of CASV is extremely similar to the filoviruses.
has issue date	2014-04-01(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2013.12.009
bibo:pmid	24333483
has license	green-oa
sha1sum (hex)	c7bed5de7f3b0420a20453a9393ce3b50fffef6e
schema:url	https://doi.org/10.1016/j.jmb.2013.12.009
resource representing a document's title	Structural Characterization of the glycoprotein GP2 Core Domain from the CAS Virus, a Novel Arenavirus-like Species
has PubMed Central identifier	PMC3951589
has PubMed identifier	24333483
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:c7bed5de7f3b0420a20453a9393ce3b50fffef6e#body_text
is schema:about of	named entity 'CAS' named entity 'defined' named entity 'studies' named entity 'structure' named entity 'transmembrane' »more»

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