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TitleThe structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 846, Year 2019
Publish dateFeb 19, 2019
AuthorsKamel 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 M Grimes / Dennis H Bamford / Nicole D Tischler / Juha T Huiskonen / David I Stuart / Elina Roine /
PubMed AbstractLipid 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, ...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.
External linksNat Commun / PubMed:30783086 / PubMed Central
MethodsEM (subtomogram averaging) / X-ray diffraction
Resolution2.46 - 16.0 Å
Structure data

9779

6j7v

EMDB-9779: Reconstruction of HRPV6 VP5 spike
PDB-6j7v: Structure of HRPV6 VP5 fitted in the cryoEM density of the spike
Method: EM (subtomogram averaging) / Resolution: 16.0 Å

PDB-6qgi:
Crystal structure of VP5 from Haloarchaeal pleomorphic virus 2
Method: X-RAY DIFFRACTION / Resolution: 2.46 Å

PDB-6qgl:
Crystal structure of VP5 from Haloarchaeal pleomorphic virus 6
Method: X-RAY DIFFRACTION / Resolution: 2.69 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-CL:
Unknown entry / Chloride

ChemComp-HOH:
WATER / Water

ChemComp-BR:
BROMIDE ION / Bromide

Source
  • halorubrum pleomorphic virus 6
  • halorubrum pleomorphic virus 2
KeywordsVIRAL PROTEIN / HRPV6 / spike / envelope protein / fusion protein / archaea / haloarchaea / prokaryotic / viral / membrane fusion

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