Loaded Anti-Fusion Protein Antibody, Human IgG1 (5B3) on AHC Biosensor, can bind Hendra virus Fusion glycoprotein (A263T), His Tag (Cat. No. FUN-H52H4) with an affinity constant of 10.3 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).
Loaded Anti-Fusion Protein Antibody, Human IgG1 (5B3) on AHC Biosensor, can bind Nipah virus Fusion glycoprotein, His Tag (Cat. No. FUN-N52H3) with an affinity constant of 8.4 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).
Fusion glycoprotein, F protein, F, Nipah virus, Hendra virus
Hendra virus (HeV) and Nipah virus (NiV) are henipaviruses discovered in the mid-to late 1990s that possess a broad host tropism and are known to cause severe and often fatal disease in both humans and animals. HeV and NiV infect host cells through the coordinated efforts of two envelope glycoproteins. The G glycoprotein attaches to cell receptors, triggering the fusion (F) glycoprotein to execute membrane fusion. G is a type II homotetrameric transmembrane protein responsible for binding to ephrinB2 or ephrinB3 (ephrinB2/B3) receptors. F is a homotrimeric type I transmembrane protein that is synthesized as a premature F0 precursor and cleaved by cathepsin L during endocytic recycling to yield the mature, disulfide-linked, F1 and F2 subunits. Upon binding to ephrinB2/B3, NiV G undergoes conformational changes leading to F triggering and insertion of the F hydrophobic fusion peptide into the target membrane. Subsequent refolding into the more stable post-fusion F conformation drives merger of the viral and host membranes to form a pore for genome delivery to the cell cytoplasm.
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