Comparative Analyses of the Antiviral Activities of IgG and IgA Antibodies to Influenza A Virus M2 Protein.
Kosuke OkuyaNao EguchiRashid ManzoorReiko YoshidaShinji SaitoTadaki SuzukiMichihito SasakiTakeshi SaitoYurie KidaAkina Mori-KajiharaHiroko MiyamotoOsamu IchiiMasahiro KajiharaHideaki HigashiAyato TakadaPublished in: Viruses (2020)
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.
Keyphrases
- protein protein
- mass spectrometry
- escherichia coli
- amino acid
- room temperature
- small molecule
- binding protein
- induced apoptosis
- cell surface
- signaling pathway
- transcription factor
- cell therapy
- oxidative stress
- liquid chromatography
- bone marrow
- tandem mass spectrometry
- cell cycle arrest
- peripheral blood
- simultaneous determination
- aedes aegypti