Conformational changes in influenza virus haemagglutinin and its monomer detected by monoclonal antibodies.
Exposure of influenza virus haemagglutinin to pH 5 results in conformational changes occurring in the molecule which are accompanied by antigenic modifications. Furthermore, isolated haemagglutinin (HA) at a concentration of 0.1 nM undergoes dissociation from the trimeric to a monomeric form when exposed to pH 5. Whether present on intact virus or as the isolated monomer, each form of haemagglutinin from pH 5 exhibits similar alterations in antigenic characteristics. These forms of HA show modifications in the antigenic sites located in the hinge (site C), tip (site B) and subunit interface (site D) regions. Whereas binding of monoclonal antibodies recognizing the tip and interface is abrogated or diminished, binding of antibodies to the hinge region is greatly enhanced following exposure of virus or the monomeric form of HA to pH 5.
Nestorowicz
A N
AN
White
D O
DO
Jackson
D C
DC
D000911:Antibodies, Monoclonal / Q000276:immunology; D001665:Binding Sites; D001963:Bromelains; D000939:Epitopes / Q000276:immunology; D006389:Hemagglutinins, Viral / Q000276:immunology*; D006863:Hydrogen-Ion Concentration; D009980:Influenza A virus / Q000276:immunology*; D008968:Molecular Conformation
D000911:Antibodies, Monoclonal; D000939:Epitopes; D006389:Hemagglutinins, Viral; D001963:Bromelains