Abstract:
:An 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.
journal_name
Proc Natl Acad Sci U S Aauthors
Halldorsson S,Behrens AJ,Harlos K,Huiskonen JT,Elliott RM,Crispin M,Brennan B,Bowden TAdoi
10.1073/pnas.1603827113subject
Has Abstractpub_date
2016-06-28 00:00:00pages
7154-9issue
26eissn
0027-8424issn
1091-6490pii
1603827113journal_volume
113pub_type
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