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Instruments / Technical Area	Publication Details	Published	Actions
I24-Microfocus Macromolecular Crystallography	Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses Ilona Rissanen , Asim A. Ahmed , Kristopher Azarm , Shannon Beaty , Patrick Hong , Sham Nambulli , W. Paul Duprex , Benhur Lee , Thomas a. Bowden Nature Communications 8 DOI: 10.1038/ncomms16060 Diamond Proposal Number(s): [8423] Open Access Show Abstract ▼ 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 attachment glycoproteins, in particular at host receptor-binding surfaces. We confirm the inability of MojV-G to interact with known paramyxoviral receptors in vitro, indicating an independence from well-characterized ephrinB2/B3, sialic acid and CD150-mediated entry pathways. Furthermore, we find that MojV-G is antigenically distinct, indicating that MojV would less likely be detected in existing large-scale serological screening studies focused on well-established HNVs. Altogether, these data indicate a unique host-cell entry pathway for this emerging and potentially pathogenic HNV.	Jul 2017

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I24-Microfocus Macromolecular Crystallography

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

Ilona Rissanen , Asim A. Ahmed , Kristopher Azarm , Shannon Beaty , Patrick Hong , Sham Nambulli , W. Paul Duprex , Benhur Lee , Thomas a. Bowden

Nature Communications 8

DOI: 10.1038/ncomms16060

Diamond Proposal Number(s): [8423]