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Mutations in the G-H Loop Region of Ephrin-B2 can Enhance Nipah Virus Binding and Infection

Yuan, J., et al., 92(Pt 9), 2142-2152, J General Virology, 2011

Nipah Virus (NiV) first emerged in Asia in 1998-1999 as the causative agent of an outbreak of respiratory disease in pigs and severe encephalitic disease with high case fatality in humans. Ephrin-B2 and ephrin-B3 have been identified as functional receptors for NiV. This study revealed that some alanine-substitution mutations located within the G-H loop of ephrin-B2 were able to enhance virus entry and infection by infectious viruses. This study also potentially provides a new target host-cell platform for either virus isolation or virus entry inhibitor screening and discovery. The authors report binding kinetics data obtained on the Octet RED platform for an envelope glycoprotein called NiV-G binding to wildtype and mutated forms of ephrin-B2. For the Octet platform experiments, biotinylated sNiV-G was immobilized on Streptavidin biosensors. The data show that the mutated form has greater binding affinity and correlates with immunofluorescence staining results that show the mutated protein as having enhanced virus adsorption, entry and infection efficiency.

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