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We sought to determine whether published Moj V-F and -G sequences give rise to functional proteins.Full-length Moj V-F and Moj V-G open reading frames were cloned into mammalian expression vectors with an AU1 or HA epitope tag at the C terminus, respectively, as previously described(a) Expression of Moj V-F, Ni V-F, He V-F and KV-F in BSR-T7 cells in the presence or absence of the cognate G glycoprotein.This isolate, previously termed as Ghana virus or Gh-M74a virus.However, there is serological evidence of HNV spillover events into humans in Africa and it has been proposed that these viruses may contribute to the prevalence of undiagnosed or misdiagnosed encephalitis.

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These data indicate an idiosyncratic host cell entry mechanism for this emergent paramyxovirus.Syncytia formed by expression of vesicular stomatitis virus-G and co-expression of Ni V-F and -G are positive controls.(d) A quantitative heterologous fusion assay shows that Moj V-F and -G-mediated fusion occurs with a variety of target cells of diverse species and tissue origins.Here we find that Moj V-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 Moj V-G to interact with known paramyxoviral receptors in vitro, indicating an independence from well-characterized ephrin B2/B3, sialic acid and CD150-mediated entry pathways.

The H glycoprotein from the prototypic morbillivirus, measles virus (MV), targets CD150 (also known as signalling lymphocytic activation molecule F.

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