Title : Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor
ephrin-B2
Abstract :
- Nipah and Hendra viruses are emergent paramyxoviruses, causing disease characterized by rapid onset and high mortality rates, resulting in their classification as Biosafety Level 4 pathogens
- Their attachment glycoproteins are essential for the recognition of the cell-surface receptors ephrin-B2 ( EFNB2 ) and ephrin-B3 ( EFNB3 )
- Here we report crystal structures of both Nipah and Hendra attachment glycoproteins in complex with human EFNB2
- In contrast to previously solved paramyxovirus attachment complexes, which are mediated by sialic acid interactions, the Nipah and Hendra complexes are maintained by an extensive protein- protein interface, including a crucial phenylalanine side chain on EFNB2 that fits snugly into a hydrophobic pocket on the viral protein
- By analogy with the development of antivirals against sialic acid binding viruses, these results provide a structural template to target antiviral inhibition of protein- protein interactions