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

DOI: 10.1038/ncomms16060 DOI Help

Authors: Ilona Rissanen (Wellcome Trust Centre for Human Genetics, University of Oxford) , 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 (Trust Centre for Human Genetics, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 8

State: Published (Approved)
Published: July 2017
Diamond Proposal Number(s): 8423

Open Access Open Access

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.

Journal Keywords: Pathogens; Viral proteins; Virus–host interactions; X-ray crystallography

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I24-Microfocus Macromolecular Crystallography

Documents:
ncomms16060.pdf