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

DOI: 10.1038/s41467-019-08728-7 DOI Help

Authors: Kamel El Omari (University of Oxford) , Sai Li (Wellcome Centre for Human Genetics, University of Oxford) , Abhay Kotecha (Wellcome Centre for Human Genetics, University of Oxford) , Thomas S. Walter (Wellcome Centre for Human Genetics, University of Oxford) , Eduardo A. Bignon (Fundación Ciencia & Vida) , Karl Harlos (Wellcome Centre for Human Genetics, University of Oxford) , Pentti Somerharju (University of Helsinki) , Felix De Haas (Thermo Fisher Scientific) , Daniel K. Clare (Diamond Light Source) , Mika Molin (University of Helsinki) , Felipe Hurtado (Fundación Ciencia & Vida) , Mengqiu Li (Wellcome Centre for Human Genetics, University of Oxford) , Jonathan Grimes (Wellcome Centre for Human Genetics,University of Oxford) , Dennis H. Bamford (University of Helsinki) , Nicole D. Tischler (Fundación Ciencia & Vida) , Juha T. Huiskonen (Wellcome Centre for Human Genetics, University of Oxford; University of Helsinki) , Dave I. Stuart (Wellcome Centre for Human Genetics, University of Oxford; Diamond Light Source) , Elina Roine (University of Helsinki)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 10

State: Published (Approved)
Published: February 2019
Diamond Proposal Number(s): 10627

Open Access Open Access

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.

Journal Keywords: Cryoelectron tomography; Microbiology; Molecular biology; X-ray crystallography

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: I02-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography , Krios I-Titan Krios I at Diamond

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s41467-019-08728-7.pdf