Isolation and Characterization of Human Monoclonal Antibodies That Recognize the Influenza A(H1N1)pdm09 Virus Hemagglutinin Receptor-Binding Site and Rarely Yield Escape Mutant Viruses

The influenza A virus rapidly mutates to escape from antibodies. Here, we isolated and characterized three human monoclonal antibodies (mAbs) that neutralize A(H1N1)pdm09 viruses. Generation of escape mutant viruses suggested that these antibodies recognized conserved residues of the receptor-bindin...

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Published inFrontiers in microbiology Vol. 9; p. 2660
Main Authors Yasuhara, Atsuhiro, Yamayoshi, Seiya, Ito, Mutsumi, Kiso, Maki, Yamada, Shinya, Kawaoka, Yoshihiro
Format Journal Article
LanguageEnglish
Published Switzerland Frontiers Media S.A 01.11.2018
Subjects
antiviral agent
escape mutant virus
human monoclonal antibody
influenza A virus
Microbiology
HA
antiviral agent
escape mutant virus
human monoclonal antibody
influenza A virus
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Summary:The influenza A virus rapidly mutates to escape from antibodies. Here, we isolated and characterized three human monoclonal antibodies (mAbs) that neutralize A(H1N1)pdm09 viruses. Generation of escape mutant viruses suggested that these antibodies recognized conserved residues of the receptor-binding site (RBS) of hemagglutinin (HA) and that mutant viruses that escaped from these mAbs rarely appeared. Moreover, the escape mutant viruses grew significantly slower than wild-type virus, indicating their reduced fitness. These results indicate that these three human mAbs against the RBS of HA have the potential to be anti-influenza agents with a low propensity for the development of resistant viruses.
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This article was submitted to Virology, a section of the journal Frontiers in Microbiology
Edited by: Aeron Hurt, WHO Collaborating Centre for Reference and Research on Influenza (VIDRL), Australia
Reviewed by: Hadi M. Yassine, Qatar University, Qatar; Luis Martinez-Sobrido, University of Rochester, United States
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2018.02660