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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography Krios I-Titan Krios I at Diamond	The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins Kamel El Omari , Sai Li , Abhay Kotecha , Thomas S. Walter , Eduardo A. Bignon , Karl Harlos , Pentti Somerharju , Felix De Haas , Daniel K. Clare , Mika Molin , Felipe Hurtado , Mengqiu Li , Jonathan Grimes , Dennis H. Bamford , Nicole D. Tischler , Juha T. Huiskonen , Dave I. Stuart , Elina Roine Nature Communications 10 DOI: 10.1038/s41467-019-08728-7 Diamond Proposal Number(s): [10627] Open Access Show Abstract ▼ 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.	Feb 2019
I04-Macromolecular Crystallography	Crystal structure of glycoprotein C from a hantavirus in the post-fusion conformation Shmuel Willensky , Hagit Bar-Rogovsky , Eduardo A. Bignon , Nicole D. Tischler , Yorgo Modis , Moshe Dessau Plos Pathogens 12 DOI: 10.1371/journal.ppat.1005948 Diamond Proposal Number(s): [15916] Open Access Show Abstract ▼ Abstract: 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	Oct 2016

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