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 () and Thomas A. Bowden ()
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Ilona Rissanen: Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, Oxfordshire OX3 7BN, UK
Asim A. Ahmed: Boston Children’s Hospital
Kristopher Azarm: Icahn School of Medicine at Mount Sinai
Shannon Beaty: Icahn School of Medicine at Mount Sinai
Patrick Hong: Icahn School of Medicine at Mount Sinai
Sham Nambulli: Boston University School of Medicine
W. Paul Duprex: Boston University School of Medicine
Benhur Lee: Icahn School of Medicine at Mount Sinai
Thomas A. Bowden: Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, Oxfordshire OX3 7BN, UK

Nature Communications, 2017, vol. 8, issue 1, 1-11

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.

Date: 2017
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DOI: 10.1038/ncomms16060

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