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PDBsum entry 5evm
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Viral protein
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PDB id
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5evm
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the pre-Fusion nipah virus fusion glycoprotein reveals a novel hexamer-Of-Trimers assembly.
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Authors
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K.Xu,
Y.P.Chan,
B.Bradel-Tretheway,
Z.Akyol-Ataman,
Y.Zhu,
S.Dutta,
L.Yan,
Y.Feng,
L.F.Wang,
G.Skiniotis,
B.Lee,
Z.H.Zhou,
C.C.Broder,
H.C.Aguilar,
D.B.Nikolov.
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Ref.
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Plos Pathog, 2015,
11,
e1005322.
[DOI no: ]
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PubMed id
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Abstract
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Nipah virus (NiV) is a paramyxovirus that infects host cells through the
coordinated efforts of two envelope glycoproteins. The G glycoprotein attaches
to cell receptors, triggering the fusion (F) glycoprotein to execute membrane
fusion. Here we report the first crystal structure of the pre-fusion form of the
NiV-F glycoprotein ectodomain. Interestingly this structure also revealed a
hexamer-of-trimers encircling a central axis. Electron tomography of Nipah
virus-like particles supported the hexameric pre-fusion model, and biochemical
analyses supported the hexamer-of-trimers F assembly in solution. Importantly,
structure-assisted site-directed mutagenesis of the interfaces between F trimers
highlighted the functional relevance of the hexameric assembly. Shown here, in
both cell-cell fusion and virus-cell fusion systems, our results suggested that
this hexamer-of-trimers assembly was important during fusion pore formation. We
propose that this assembly would stabilize the pre-fusion F conformation prior
to cell attachment and facilitate the coordinated transition to a post-fusion
conformation of all six F trimers upon triggering of a single trimer. Together,
our data reveal a novel and functional pre-fusion architecture of a
paramyxoviral fusion glycoprotein.
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