Hendra virus (HeV) and Nipah virus (NiV) are closely related paramyxoviruses that infect and cause disease in a wide range of mammalian hosts. To determine whether host receptor molecules play a role in species-specific and/or virus-specific infection we have cloned and characterized ephrin-B2 and ephrin-B3 ligands from a range of species, including human, horse, pig, cat, dog, bats (Pteropus alecto and Pteropus vampyrus) and mouse. HeV and NiV were both able to infect cells expressing any of the ephrin-B2 and ephrin-B3 molecules. There did not appear to be significant differences in receptor function from different species or receptor usage by HeV and NiV. Soluble ephrin ligands, their receptors and G-specific human monoclonal antibodies differentially blocked henipavirus infections suggesting different receptor affinities, overlapping receptor binding domains of the henipavirus attachment glycoprotein (G) and that the functional domains of the ephrin ligands may be important for henipavirus binding.
Hendra virus (HeV) and Nipah virus (NiV) were both able to infect cells expressing any of the ephrin-B2 and ephrin-B3 molecules. There did not appear to be significant differences in receptor function from different species or receptor usage by HeV and NiV.
Method
functional infection assay
Receptors
ephrin-B2
Receptor UsageExtraction confidence 0.98
Key finding
Hendra virus and Nipah virus both use ephrin-B2 and ephrin-B3 as receptors to mediate infection in cells from various mammalian species.
Hendra virus (HeV) and Nipah virus (NiV) were both able to infect cells expressing any of the ephrin-B2 and ephrin-B3 molecules. There did not appear to be significant differences in receptor function from different species or receptor usage by HeV and NiV.
Method
functional infection assay
Receptors
ephrin-B3
Receptor UsageExtraction confidence 0.98
Key finding
Hendra virus and Nipah virus both use ephrin-B2 and ephrin-B3 as receptors to mediate infection in cells from various mammalian species.
Hendra virus (HeV) and Nipah virus (NiV) were both able to infect cells expressing any of the ephrin-B2 and ephrin-B3 molecules. There did not appear to be significant differences in receptor function from different species or receptor usage by HeV and NiV.
Method
functional infection assay
Receptors
ephrin-B2
Receptor UsageExtraction confidence 0.98
Key finding
Hendra virus and Nipah virus both use ephrin-B2 and ephrin-B3 as receptors to mediate infection in cells from various mammalian species.
Hendra virus (HeV) and Nipah virus (NiV) were both able to infect cells expressing any of the ephrin-B2 and ephrin-B3 molecules. There did not appear to be significant differences in receptor function from different species or receptor usage by HeV and NiV.
Method
functional infection assay
Receptors
ephrin-B3
Molecular Adaptation1 records
Molecular AdaptationExtraction confidence 0.80
Key finding
Hendra and Nipah viruses can utilize ephrin-B2 and ephrin-B3 from multiple species, and variation in ephrin functional domains and receptor affinity influences henipavirus G glycoprotein binding.
HeV and NiV were both able to infect cells expressing any of the ephrin-B2 and ephrin-B3 molecules. Soluble ephrin ligands, their receptors and G-specific human monoclonal antibodies differentially blocked henipavirus infections suggesting different receptor affinities, overlapping receptor binding domains of the henipavirus attachment glycoprotein (G) and that the functional domains of the ephrin ligands may be important for henipavirus binding.
