5g47
From Proteopedia
Structure of Gc glycoprotein from severe fever with thrombocytopenia syndrome virus in the trimeric postfusion conformation
Structural highlights
FunctionGP_SFTS Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (PubMed:23388721). Plays a role in the packaging of ribonucleoproteins during virus assembly (By similarity).[UniProtKB:P09613][UniProtKB:P21401][1] Structural component of the virion that interacts with glycoprotein N (By similarity). Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (PubMed:23388721).[UniProtKB:P09613][UniProtKB:P21401][2] Publication Abstract from PubMedAn emergent viral pathogen termed severe fever with thrombocytopenia syndrome virus (SFTSV) is responsible for thousands of clinical cases and associated fatalities in China, Japan, and South Korea. Akin to other phleboviruses, SFTSV relies on a viral glycoprotein, Gc, to catalyze the merger of endosomal host and viral membranes during cell entry. Here, we describe the postfusion structure of SFTSV Gc, revealing that the molecular transformations the phleboviral Gc undergoes upon host cell entry are conserved with otherwise unrelated alpha- and flaviviruses. By comparison of SFTSV Gc with that of the prefusion structure of the related Rift Valley fever virus, we show that these changes involve refolding of the protein into a trimeric state. Reverse genetics and rescue of site-directed histidine mutants enabled localization of histidines likely to be important for triggering this pH-dependent process. These data provide structural and functional evidence that the mechanism of phlebovirus-host cell fusion is conserved among genetically and patho-physiologically distinct viral pathogens. Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion.,Halldorsson S, Behrens AJ, Harlos K, Huiskonen JT, Elliott RM, Crispin M, Brennan B, Bowden TA Proc Natl Acad Sci U S A. 2016 Jun 28;113(26):7154-9. doi:, 10.1073/pnas.1603827113. Epub 2016 Jun 20. PMID:27325770[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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