Structural highlights
FunctionPublication Abstract from PubMedIn 2012, cases of lethal pneumonia among Chinese miners prompted the isolation of a rat-borne henipavirus (HNV), Mojiang 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 beta-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. Idiosyncratic Mojiang virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses.,Rissanen I, Ahmed AA, Azarm K, Beaty S, Hong P, Nambulli S, Duprex WP, Lee B, Bowden TA Nat Commun. 2017 Jul 12;8:16060. doi: 10.1038/ncomms16060. PMID:28699636[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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