tetano
Editor, Senior Moderator
Biochem Biophys Res Commun. 2014 Sep 6. pii: S0006-291X(14)01616-7. doi: 10.1016/j.bbrc.2014.09.008. [Epub ahead of print]
A human monoclonal antibody derived from a vaccinated volunteer recognizes heterosubtypically a novel epitope on the hemagglutinin globular head of H1 and H9 influenza A viruses.
Boonsathorn N1, Panthong S1, Koksunan S2, Chittaganpitch M3, Phuygun S3, Waicharoen S3, Prachasupap A1, Sasaki T4, Kubota-Koketsu R5, Yasugi M6, Ono KI7, Arai Y8, Kurosu T4, Sawanpanyalert P9, Ikuta K10, Watanabe Y11.
Author information
Abstract
Most neutralizing antibodies elicited during influenza virus infection or by vaccination have a narrow spectrum because they usually target variable epitopes in the globular head region of hemagglutinin (HA). In this study, we describe a human monoclonal antibody (HuMAb), 5D7, that was prepared from the peripheral blood lymphocytes of a vaccinated volunteer using the fusion method. The HuMAb heterosubtypically neutralizes group 1 influenza A viruses, including seasonal H1N1, 2009 pandemic H1N1 (H1N1pdm) and avian H9N2, with a strong hemagglutinin inhibition activity. Selection of an escape mutant showed that the HuMAb targets a novel conformational epitope that is located in the HA head region but is distinct from the receptor binding site. Furthermore, Phe114Ile substitution in the epitope made the HA unrecognizable by the HuMAb. Amino acid residues in the predicted epitope region are also highly conserved in the HAs of H1N1 and H9N2. The HuMAb reported here may be a potential candidate for the development of therapeutic/prophylactic antibodies against H1 and H9 influenza viruses.
Copyright ? 2014. Published by Elsevier Inc.
KEYWORDS:
Conserved epitope in HA head region; Heterosubtypic neutralizing antibody; Human monoclonal antibody; Influenza A virus
PMID:
25204499
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25204499
A human monoclonal antibody derived from a vaccinated volunteer recognizes heterosubtypically a novel epitope on the hemagglutinin globular head of H1 and H9 influenza A viruses.
Boonsathorn N1, Panthong S1, Koksunan S2, Chittaganpitch M3, Phuygun S3, Waicharoen S3, Prachasupap A1, Sasaki T4, Kubota-Koketsu R5, Yasugi M6, Ono KI7, Arai Y8, Kurosu T4, Sawanpanyalert P9, Ikuta K10, Watanabe Y11.
Author information
Abstract
Most neutralizing antibodies elicited during influenza virus infection or by vaccination have a narrow spectrum because they usually target variable epitopes in the globular head region of hemagglutinin (HA). In this study, we describe a human monoclonal antibody (HuMAb), 5D7, that was prepared from the peripheral blood lymphocytes of a vaccinated volunteer using the fusion method. The HuMAb heterosubtypically neutralizes group 1 influenza A viruses, including seasonal H1N1, 2009 pandemic H1N1 (H1N1pdm) and avian H9N2, with a strong hemagglutinin inhibition activity. Selection of an escape mutant showed that the HuMAb targets a novel conformational epitope that is located in the HA head region but is distinct from the receptor binding site. Furthermore, Phe114Ile substitution in the epitope made the HA unrecognizable by the HuMAb. Amino acid residues in the predicted epitope region are also highly conserved in the HAs of H1N1 and H9N2. The HuMAb reported here may be a potential candidate for the development of therapeutic/prophylactic antibodies against H1 and H9 influenza viruses.
Copyright ? 2014. Published by Elsevier Inc.
KEYWORDS:
Conserved epitope in HA head region; Heterosubtypic neutralizing antibody; Human monoclonal antibody; Influenza A virus
PMID:
25204499
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25204499