Structural characterization of the glycoprotein GP2 core domain from the CAS virus, a novel arenavirus-like species.

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 simila

SUBMITTER: Koellhoffer JF 

PROVIDER: S-EPMC3951589 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature