Growth Kinetics of Influenza C Virus Antigenic Mutants That Escaped from Anti-Hemagglutinin Esterase Monoclonal Antibodies and Viral Antigenic Changes Found in Field Isolates
Autor: | Seiji Hongo, Hidekazu Nishimura, Yoko Matsuzaki, Yoshitaka Shimotai, Katsumi Mizuta, Kanetsu Sugawara, Yoko Kadowaki |
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Rok vydání: | 2021 |
Předmět: |
0301 basic medicine
Antigenicity Influenzavirus C medicine.drug_class viruses 030106 microbiology Mutant lcsh:QR1-502 escape mutant Biology Monoclonal antibody lcsh:Microbiology Article Antigenic drift Virus Madin Darby Canine Kidney Cells 03 medical and health sciences Dogs Virology medicine Animals Antigens Viral antigenic drift growth kinetics chemistry.chemical_classification Hemagglutinin esterase virus diseases Antigenic Variation influenza C virus 030104 developmental biology Infectious Diseases chemistry surveillance Influenza C Virus Glycoprotein |
Zdroj: | Viruses Volume 13 Issue 3 Viruses, Vol 13, Iss 401, p 401 (2021) |
ISSN: | 1999-4915 |
Popis: | The antigenicity of the hemagglutinin esterase (HE) glycoprotein of influenza C virus is known to be stable however, information about residues related to antigenic changes has not yet been fully acquired. Using selection with anti-HE monoclonal antibodies, we previously obtained some escape mutants and identified four antigenic sites, namely, A-1, A-2, A-3, and Y-1. To confirm whether the residues identified as the neutralizing epitope possibly relate to the antigenic drift, we analyzed the growth kinetics of these mutants. The results showed that some viruses with mutations in antigenic site A-1 were able to replicate to titers comparable to that of the wild-type, while others showed reduced titers. The mutants possessing substitutions in the A-2 or A-3 site replicated as efficiently as the wild-type virus. Although the mutant containing a deletion at positions 192 to 195 in the Y-1 site showed lower titers than the wild-type virus, it was confirmed that this region in the 190-loop on the top side of the HE protein is not essential for viral propagation. Then, we revealed that antigenic changes due to substitutions in the A-1, A-3, and/or Y-1 site had occurred in nature in Japan for the past 30 years. These results suggest that some residues (i.e., 125, 176, 192) in the A-1 site, residue 198 in the A-3 site, and residue 190 in the Y-1 site are likely to mediate antigenic drift while maintaining replicative ability. |
Databáze: | OpenAIRE |
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