Disease relevance of G

• Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus [1].
• In this study, the extra-cellular domain of NiV G protein was fused with hexahistidine residues at its N-terminal end and expressed in Escherichia coli [2].
• Feline model of acute nipah virus infection and protection with a soluble glycoprotein-based subunit vaccine [3].
• Using a recombinant vaccinia virus system and a quantitative assay for fusion, we demonstrate NiV glycoprotein function and the same pattern of cellular tropism recently reported for HeV-mediated fusion, suggesting that NiV likely uses the same cellular receptor for infection [4].

High impact information on G

• Functional expression of NiV F and G was verified by complementation with the corresponding glycoprotein, which resulted in the development of syncytia [5].
• Glycoprotein function and cellular tropism were examined with a quantitative assay for HeV-mediated membrane fusion [6].

Biological context of G

• Recombinant vaccinia viruses encoding the HeV F and G open reading frames were generated and glycoprotein expression was verified by metabolic labeling and detection using specific antisera [6].

Analytical, diagnostic and therapeutic context of G

• Taken together, the data indicate the potential usefulness of the purified G protein for structural or functional studies and the development of immunoassay for detection of the NiV antibodies [2].

References