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.
Highlights
In 2012, cases of lethal pneumonia among Chinese miners prompted the isolation of a rat-borne henipavirus (HNV), Mojia%ng virus (MojV)
Immunoblotting revealed that MojV attachment glycoprotein (MojV-G) and MojV-F display expression profiles analogous to cognate Nipah virus (NiV), Hendra virus (HeV) and Kumasi virus (KV) glycoproteins: MojV-F undergoes proteolytic cleavage from an F0 glycoprotein precursor to a disulfide linked, mature F1/F2 complex (Fig. 1a) and MojV-G forms higher-order oligomers, constituting putative dimeric and tetrameric species, under non-reducing conditions (Fig. 1b)
We observed syncytia formation after co-expression of MojV-F and MojV-G, a strategy previously established for NiV-F/G and HeV-F/G31
Summary
In 2012, cases of lethal pneumonia among Chinese miners prompted the isolation of a rat-borne henipavirus (HNV), Mojia%ng virus (MojV). 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. Viruses belonging to additional 420 putative HNV clades have been detected in bat reservoirs in Africa and the near-complete genome of a Ghanaian bat HNV isolate has been sequenced. This isolate, previously termed as Ghana virus or Gh-M74a virus[4,5], is known as Kumasi virus (KV)[6]. Viral attachment is a primary determinant of host cell tropism and is initiated by a haemagglutinin-neuraminidase (HN)
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