The Hantavirus Surface Glycoprotein Lattice and Its Fusion Control Mechanism

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http://hdl.handle.net/10138/322046

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Serris , A , Stass , R , Bignon , E A , Muena , N A , Manuguerra , J-C , Jangra , R K , Li , S , Chandran , K , Tischler , N D , Huiskonen , J T , Rey , F A & Guardado-Calvo , P 2020 , ' The Hantavirus Surface Glycoprotein Lattice and Its Fusion Control Mechanism ' , Cell , vol. 183 , no. 2 , pp. 442-456e16 . https://doi.org/10.1016/j.cell.2020.08.023

Title: The Hantavirus Surface Glycoprotein Lattice and Its Fusion Control Mechanism
Author: Serris, Alexandra; Stass, Robert; Bignon, Eduardo A.; Muena, Nicolas A.; Manuguerra, Jean-Claude; Jangra, Rohit K.; Li, Sai; Chandran, Kartik; Tischler, Nicole D.; Huiskonen, Juha T.; Rey, Felix A.; Guardado-Calvo, Pablo
Contributor organization: Institute of Biotechnology
Molecular and Integrative Biosciences Research Programme
Helsinki Institute of Life Science HiLIFE
Laboratory of Structural Biology
Date: 2020-10-15
Language: eng
Number of pages: 31
Belongs to series: Cell
ISSN: 0092-8674
DOI: https://doi.org/10.1016/j.cell.2020.08.023
URI: http://hdl.handle.net/10138/322046
Abstract: Hantaviruses are rodent-borne viruses causing serious zoonotic outbreaks worldwide for which no treatment is available. Hantavirus particles are pleomorphic and display a characteristic square surface lattice. The envelope glycoproteins Gn and Gc form heterodimers that further assemble into tetrameric spikes, the lattice building blocks. The glycoproteins, which are the sole targets of neutralizing antibodies, drive virus entry via receptor-mediated endocytosis and endosomal membrane fusion. Here we describe the high-resolution X-ray structures of the heterodimer of Gc and the Gn head and of the homotetrameric Gn base. Docking them into an 11.4-angstrom-resolution cryoelectron tomography map of the hantavirus surface accounted for the complete extramembrane portion of the viral glycoprotein shell and allowed a detailed description of the surface organization of these pleomorphic virions. Our results, which further revealed a built-in mechanism controlling Gc membrane insertion for fusion, pave the way for immunogen design to protect against pathogenic hantaviruses.
Subject: TO-PERSON TRANSMISSION
HANTAAN-VIRUS
ENVELOPE GLYCOPROTEIN
MEMBRANE-FUSION
CONFORMATIONAL-CHANGES
MONOCLONAL-ANTIBODIES
ENCEPHALITIS-VIRUS
CRYSTAL-STRUCTURE
STRUCTURAL BASIS
PROTEIN
1182 Biochemistry, cell and molecular biology
Peer reviewed: Yes
Usage restriction: closedAccess
Self-archived version: submittedVersion


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