Surface glycoproteins of the recently identified African Henipavirus promote viral entry and cell fusion in a range of human, simian and bat cell lines.
Philip Lawrence1
Beatriz Escudero Pérez1
Jan Felix Drexler2
Victor Max Corman2
Marcel A Müller2
Christian Drosten2
Viktor Volchkov3
Affiliations3 institutions
International Centre for Research in Infectiology (CIRI), INSERM U1111 - CNRS UMR5308, Université Lyon 1, ENS de Lyon, Lyon, France.
Institute of Virology, University of Bonn Medical Centre, Bonn, Germany.
International Centre for Research in Infectiology (CIRI), INSERM U1111 - CNRS UMR5308, Université Lyon 1, ENS de Lyon, Lyon, France. Electronic address: [email protected].
The recent discovery of a wide range of henipavirus-like viruses circulating in Megabats in Africa raises the question as to the zoonotic potential of these pathogens given the high human mortality rates seen with their pathogenic relatives Nipah virus and Hendra virus. In the absence of cultured infectious African Henipavirus we have performed experiments with recombinant F and G glycoproteins from the representative African Henipavirus strain M74a aimed at estimating its cellular tropism and capacity to use similar receptors to its highly pathogenic counterparts. The ability of the M74a virus G surface protein to use the ubiquitous Ephrin B2 host cell receptor and its heterologous cross-compatibility with Nipah virus could be expected to impart upon this virus a reasonable potential for species spillover, although differences in fusion efficiency seen with the M74a virus F protein in certain cell lines could present a barrier for zoonotic transmission.
African Henipavirus M74a glycoproteins mediated entry and fusion in human, simian, and bat cell lines, indicating potential cross-species cellular susceptibility.
Experiments with recombinant F and G glycoproteins from the representative African Henipavirus strain M74a estimated its cellular tropism and capacity to use similar receptors to its highly pathogenic counterparts, promoting viral entry and cell fusion in human, simian and bat cell lines.
African Henipavirus M74a G protein can use the Ephrin B2 receptor similarly to Nipah virus, while F protein shows variable fusion efficiency across host cell lines, indicating molecular adaptations influencing host range and spillover potential.
The ability of the M74a virus G surface protein to use the ubiquitous Ephrin B2 host cell receptor and its heterologous cross-compatibility with Nipah virus could be expected to impart upon this virus a reasonable potential for species spillover, although differences in fusion efficiency seen with the M74a virus F protein in certain cell lines could present a barrier for zoonotic transmission.
The ability of the M74a virus G surface protein to use the ubiquitous Ephrin B2 host cell receptor and its heterologous cross-compatibility with Nipah virus could be expected to impart upon this virus a reasonable potential for species spillover.
