Description
The influenza A virus is the leading cause of annual influenza epidemics and occasional influenza pandemics . Hemagglutinin (HA) is a trimeric glycoprotein that is present in multiple copies in the membrane envelope of infl uenza virus . HA contains a fusion peptide , a receptor binding site, a metastable structural motif, and the transmembrane domain. The first step of infl uenza virus entry is the recognition of the host cell receptor molecule, terminal ϫ -sialic acid, by HA. HA plays a key role in the entire entry pathway. Inhibitors of virus entry are potentially effective antiviral drugs of infl uenza viruses. The trimeric HA precursor travels through the secretory pathway from ER, Golgi apparatus, and secretory vesicles to the plasma membrane. The HA glycoprotein of influenza A virus has been classified in 20 subtypes (H1ÿH20) based on a hemagglutination -inhibition test. The key function of NA is to remove sialic acid moieties from oligosaccharides attached to HA on newly assembled influenza virus particles when they bud out ofthe infected cells.
Target
FluA HA
Isotype/Mimetic
Mouse IgG1
Animal-Derived Biomaterials Used
No
Sequence Available
Yes
Original Discovery Method
Unknown
Antibody/Binder Origins
Unknown discovery source/method, In vitro recombinant expression, Animal-derived biomaterials used in production or final formulation