4c53
Crystal Structure of Guanarito virus GP2 in the post-fusion conformation
Structural highlights
FunctionGLYC_GTOVV Interacts with the host receptor (By similarity). Mediates virus attachment to host TFRC. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (PubMed:17287727).[HAMAP-Rule:MF_04084][1] Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.[HAMAP-Rule:MF_04084] Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.[HAMAP-Rule:MF_04084] Publication Abstract from PubMedGuanarito virus (GTOV) is an emergent and deadly pathogen. We present the crystal structure of the glycosylated GTOV fusion glycoprotein to 4.1 A-resolution, in the post-fusion conformation. Our structure reveals a classical six-helix bundle and presents direct verification that New World arenaviruses exhibit class-I viral membrane fusion machinery. The structure provides visualization of an N-linked glycocalyx coat and consideration of glycan dynamics reveals extensive coverage of the underlying protein surface, following virus-host membrane fusion. Crystal structure of Venezuelan hemorrhagic fever virus fusion glycoprotein reveals a class 1 post-fusion architecture with extensive glycosylation.,Parsy ML, Harlos K, Huiskonen JT, Bowden TA J Virol. 2013 Sep 18. PMID:24049182[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||||
