Antigenic analysis of H4 influenza virus isolates using monoclonal antibodies to defined antigenic sites on the hemagglutinin of A/budgerigar/Hokkaido/1/77 strain

1985 ◽  
Vol 84 (3-4) ◽  
pp. 251-259 ◽  
Author(s):  
T. Ito ◽  
H. Kida ◽  
R. Yanagawa
Keyword(s):  
Influenza Virus ◽  
Monoclonal Antibodies ◽  
Antigenic Analysis ◽  
Antigenic Sites ◽  
Virus Isolates

scholarly journals M protein (M1) of influenza virus: antigenic analysis and intracellular localization with monoclonal antibodies.

1989 ◽  
Vol 63 (9) ◽  
pp. 3622-3633 ◽  
Author(s):  
D Bucher ◽  
S Popple ◽  
M Baer ◽  
A Mikhail ◽  
Y F Gong ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Monoclonal Antibodies ◽  
Intracellular Localization ◽  
M Protein ◽  
Antigenic Analysis

scholarly journals Identification of antibodies targeting the H3N2 hemagglutinin receptor binding site following vaccination of humans

2019 ◽  
Author(s):  
Seth J. Zost ◽  
Juhye Lee ◽  
Megan E. Gumina ◽  
Kaela Parkhouse ◽  
Carole Henry ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Monoclonal Antibodies ◽  
Binding Site ◽  
Receptor Binding ◽  
Receptor Binding Site ◽  
Antigenic Sites ◽  
Influenza Virus Hemagglutinin ◽  
Ha Protein

SUMMARYAntibodies targeting the receptor binding site (RBS) of the influenza virus hemagglutinin (HA) protein are usually not broadly-reactive because their footprints are typically large and extend to nearby variable HA residues. Here, we identified several human H3N2 HA RBS-targeting monoclonal antibodies (mAbs) that were sensitive to substitutions in conventional antigenic sites and were not broadly-reactive. However, we also identified one H3N2 HA RBS-targeting mAb that was exceptionally broadly reactive despite being sensitive to substitutions in residues outside of the RBS. We determined that similar antibodies are present at measurable levels in the sera of some individuals but that they are inefficiently elicited by conventional vaccines. Our data indicate that some HA RBS-targeting antibodies can be surprisingly effective against variable viral strains even if they are somewhat sensitive to substitutions in HA residues adjacent to the RBS.

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