6y9m
From Proteopedia
Crystal structure of TSWV glycoprotein N ectodomain (sGn)
Structural highlights
Function[A0A3G1GK10_TSWV] Together with Glycoprotein C are present at the surface of the virion. They are able to attach the virion to a cell receptor and to promote fusion of membranes after endocytosis of the virion.[ARBA:ARBA00002373] Together with Glycoprotein N are present at the surface of the virion. They are able to attach the virion to a cell receptor and to promote fusion of membranes after endocytosis of the virion.[ARBA:ARBA00004076] Publication Abstract from PubMedTospoviridae is a family of enveloped RNA plant viruses that infect many field crops, inflicting a heavy global economic burden. These tripartite, single-stranded, negative-sense RNA viruses are transmitted from plant to plant by thrips as the insect vector. The medium (M) segment of the viral genome encodes two envelope glycoproteins, GN and GC, which together form the envelope spikes. GC is considered the virus fusogen, while the accompanying GN protein serves as an attachment protein that binds to a yet unknown receptor, mediating the virus acquisition by the thrips carrier. Here we present the crystal structure of glycoprotein N (GN) from the tomato spotted wilt virus (TSWV), a representative member of the Tospoviridae family. The structure suggests that GN is organized as dimers on TSWV's outer shell. Our structural data also suggest that this dimerization is required for maintaining GN structural integrity. Although the structure of the TSWV GN is different from other bunyavirus GN proteins, they all share similar domain connectivity that resembles glycoproteins from unrelated animal-infecting viruses, suggesting a common ancestor for these accompanying proteins. Crystal structure of tomato spotted wilt virus GN reveals a dimer complex formation and evolutionary link to animal-infecting viruses.,Bahat Y, Alter J, Dessau M Proc Natl Acad Sci U S A. 2020 Oct 5. pii: 2004657117. doi:, 10.1073/pnas.2004657117. PMID:33020295[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|