HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Research Center for Zoonosis Control >
Peer-reviewed Journal Articles, etc >

Comparative Analyses of the Antiviral Activities of IgG and IgA Antibodies to Influenza A Virus M2 Protein

This item is licensed under: Creative Commons Attribution 4.0 International

Files in This Item:

The file(s) associated with this item can be obtained from the following URL:https://doi.org/10.3390/v12070780


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)
人獣共通感染症リサーチセンター (Research Center for Zoonosis Control) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University