The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins

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El Omari , K , Li , S , Kotecha , A , Walter , T S , Bignon , E , Harlos , K , Somerharju , P , Haas , F D , Clare , D , Molin , M , Hurtado , F , Li , M , Grimes , J M , Bamford , D H , Tischler , N D , Huiskonen , J T , Stuart , D I & Roine , E 2019 , ' The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins ' , Nature Communications , vol. 10 , 846 . https://doi.org/10.1038/s41467-019-08728-7

Title: The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins
Author: El Omari, Kamel; Li, Sai; Kotecha, Abhay; Walter, Thomas S.; Bignon, Eduardo; Harlos, Karl; Somerharju, Pentti; Haas, Felix de; Clare, Daniel; Molin, Mika; Hurtado, Felipe; Li, Mengqiu; Grimes, Jonathan M.; Bamford, Dennis Henry; Tischler, Nicole D.; Huiskonen, Juha T.; Stuart, David I.; Roine, Elina
Contributor: University of Helsinki, Pentti Somerharju / Principal Investigator
University of Helsinki, Institute of Biotechnology
University of Helsinki, Biosciences
University of Helsinki, Helsinki Institute of Life Science HiLIFE
University of Helsinki, Helsinki Institute of Life Science HiLIFE, Joint Activities
Date: 2019-02-19
Language: eng
Number of pages: 11
Belongs to series: Nature Communications
ISSN: 2041-1723
URI: http://hdl.handle.net/10138/300221
Abstract: Lipid membrane fusion is an essential function in many biological processes. Detailed mechanisms of membrane fusion and the protein structures involved have been mainly studied in eukaryotic systems, whereas very little is known about membrane fusion in prokaryotes. Haloarchaeal pleomorphic viruses (HRPVs) have a membrane envelope decorated with spikes that are presumed to be responsible for host attachment and membrane fusion. Here we determine atomic structures of the ectodomains of the 57-kDa spike protein VP5 from two related HRPVs revealing a previously unreported V-shaped fold. By Volta phase plate cryo-electron tomography we show that VP5 is monomeric on the viral surface, and we establish the orientation of the molecules with respect to the viral membrane. We also show that the viral membrane fuses with the host cytoplasmic membrane in a process mediated by VP5. This sheds light on protein structures involved in prokaryotic membrane fusion.
Subject: 1183 Plant biology, microbiology, virology
Archaea
Virus
Prokaryote
1182 Biochemistry, cell and molecular biology
Cryo-ET
X-ray crystal structure
Membrane fusion
Fusion proteins
NANOLITRE CRYSTALLIZATION EXPERIMENTS
INFLUENZA-VIRUS
SYSTEM
VISUALIZATION
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