Title: | Comparative Analyses of the Antiviral Activities of IgG and IgA Antibodies to Influenza A Virus M2 Protein |
Authors: | Okuya, Kosuke Browse this author |
Eguchi, Nao Browse this author |
Manzoor, Rashid Browse this author |
Yoshida, Reiko Browse this author →KAKEN DB |
Saito, Shinji Browse this author |
Suzuki, Tadaki Browse this author →KAKEN DB |
Sasaki, Michihito Browse this author →KAKEN DB |
Saito, Takeshi Browse this author →KAKEN DB |
Kida, Yurie Browse this author |
Mori-Kajihara, Akina Browse this author |
Miyamoto, Hiroko Browse this author |
Ichii, Osamu Browse this author →KAKEN DB |
Kajihara, Masahiro Browse this author →KAKEN DB |
Higashi, Hideaki Browse this author →KAKEN DB |
Takada, Ayato Browse this author →KAKEN DB |
Keywords: | influenza A virus |
matrix 2 protein |
antibody |
IgA |
budding inhibition |
cross-protective immunity |
Issue Date: | 20-Jul-2020 |
Publisher: | MDPI |
Journal Title: | Viruses-Basel |
Volume: | 12 |
Issue: | 7 |
Start Page: | 780 |
Publisher DOI: | 10.3390/v12070780 |
Abstract: | The influenza A virus (IAV) matrix-2 (M2) protein is an antigenically conserved viral envelope protein that plays an important role in virus budding together with another envelope protein, hemagglutinin (HA). An M2-specific mouse monoclonal IgG antibody, rM2ss23, which binds to the ectodomain of the M2 protein, has been shown to be a non-neutralizing antibody, but inhibits plaque formation of IAV strains. In this study, we generated chimeric rM2ss23 (ch-rM2ss23) IgG and IgA antibodies with the same variable region and compared their antiviral activities. Using gel chromatography, ch-rM2ss23 IgA were divided into three antibody subsets: monomeric IgA (m-IgA), dimeric IgA (d-IgA), and trimeric and tetrameric IgA (t/q-IgA). We found that t/q-IgA had a significantly higher capacity to reduce the plaque size of IAVs than IgG and m-IgA, most likely due to the decreased number of progeny virus particles produced from infected cells. Interestingly, HA-M2 colocalization was remarkably reduced on the infected cell surface in the presence of ch-rM2ss23 antibodies. These results indicate that anti-M2 polymeric IgA restricts IAV budding more efficiently than IgG and suggest a role of anti-M2 IgA in cross-protective immunity to IAVs. |
Rights: | https://creativecommons.org/licenses/by/4.0/ |
Type: | article |
URI: | http://hdl.handle.net/2115/79171 |
Appears in Collections: | 国際連携研究教育局 : GI-CoRE (Global Institution for Collaborative Research and Education : GI-CoRE) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc) 人獣共通感染症国際共同研究所 (International Institute for Zoonosis Control) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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