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Crystal Structure of Glycoprotein C from a Hantavirus in the Post-fusion Conformation.

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Title: Crystal Structure of Glycoprotein C from a Hantavirus in the Post-fusion Conformation.
Authors: Shmuel Willensky, Hagit Bar-Rogovsky, Eduardo A Bignon, Nicole D Tischler, Yorgo Modis, Moshe Dessau
Source: PLoS Pathogens, Vol 12, Iss 10, p e1005948 (2016)
Publisher Information: Public Library of Science (PLoS), 2016.
Publication Year: 2016
Collection: LCC:Immunologic diseases. Allergy
LCC:Biology (General)
Subject Terms: Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5
More Details: Hantaviruses are important emerging human pathogens and are the causative agents of serious diseases in humans with high mortality rates. Like other members in the Bunyaviridae family their M segment encodes two glycoproteins, GN and GC, which are responsible for the early events of infection. Hantaviruses deliver their tripartite genome into the cytoplasm by fusion of the viral and endosomal membranes in response to the reduced pH of the endosome. Unlike phleboviruses (e.g. Rift valley fever virus), that have an icosahedral glycoprotein envelope, hantaviruses display a pleomorphic virion morphology as GN and GC assemble into spikes with apparent four-fold symmetry organized in a grid-like pattern on the viral membrane. Here we present the crystal structure of glycoprotein C (GC) from Puumala virus (PUUV), a representative member of the Hantavirus genus. The crystal structure shows GC as the membrane fusion effector of PUUV and it presents a class II membrane fusion protein fold. Furthermore, GC was crystallized in its post-fusion trimeric conformation that until now had been observed only in Flavi- and Togaviridae family members. The PUUV GC structure together with our functional data provides intriguing evolutionary and mechanistic insights into class II membrane fusion proteins and reveals new targets for membrane fusion inhibitors against these important pathogens.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1553-7366
1553-7374
Relation: https://doaj.org/toc/1553-7366; https://doaj.org/toc/1553-7374
DOI: 10.1371/journal.ppat.1005948
Access URL: https://doaj.org/article/ff692250127c4c2ea71392dc08afc5a2
Accession Number: edsdoj.ff692250127c4c2ea71392dc08afc5a2
Database: Directory of Open Access Journals
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  Data: Hantaviruses are important emerging human pathogens and are the causative agents of serious diseases in humans with high mortality rates. Like other members in the Bunyaviridae family their M segment encodes two glycoproteins, GN and GC, which are responsible for the early events of infection. Hantaviruses deliver their tripartite genome into the cytoplasm by fusion of the viral and endosomal membranes in response to the reduced pH of the endosome. Unlike phleboviruses (e.g. Rift valley fever virus), that have an icosahedral glycoprotein envelope, hantaviruses display a pleomorphic virion morphology as GN and GC assemble into spikes with apparent four-fold symmetry organized in a grid-like pattern on the viral membrane. Here we present the crystal structure of glycoprotein C (GC) from Puumala virus (PUUV), a representative member of the Hantavirus genus. The crystal structure shows GC as the membrane fusion effector of PUUV and it presents a class II membrane fusion protein fold. Furthermore, GC was crystallized in its post-fusion trimeric conformation that until now had been observed only in Flavi- and Togaviridae family members. The PUUV GC structure together with our functional data provides intriguing evolutionary and mechanistic insights into class II membrane fusion proteins and reveals new targets for membrane fusion inhibitors against these important pathogens.
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