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Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses.

Abstract:

In 2012, cases of lethal pneumonia among Chinese miners prompted the isolation of a rat-borne henipavirus (HNV), Mòjiāng virus (MojV). Although MojV is genetically related to highly pathogenic bat-borne henipaviruses, the absence of a conserved ephrin receptor-binding motif in the MojV attachment glycoprotein (MojV-G) indicates a differing host-cell recognition mechanism. Here we find that MojV-G displays a six-bladed β-propeller fold bearing limited similarity to known paramyxoviral attachme...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/ncomms16060

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
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Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Communications Journal website
Volume:
8
Pages:
16060
Publication date:
2017-07-01
Acceptance date:
2017-05-25
DOI:
EISSN:
2041-1723
Source identifiers:
707887
Language:
English
Keywords:
Pubs id:
pubs:707887
UUID:
uuid:f9e491ef-4905-4ce9-9951-bea998f617a1
Local pid:
pubs:707887
Deposit date:
2017-07-13

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