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Biochem Biophys Res Commun. 2009 Apr 30. [Epub ahead of print]
Monoclonal antibody recognizing SLLTEVET epitope of M2 protein potently inhibited the replication of influenza A viruses in MDCK cells.
Wang Y, Zhou L, Shi H, Xu H, Yao H, Xi XG, Toyoda T, Wang X, Wang T. - Laboratory of Wildlife Epidemic Diseases, East China Normal University, Shanghai 200062, China.
The ectodomain of influenza A virus M2 protein (M2e) is composed of 24 amino acids and induces antibodies with inhibitory effect against a broad spectrum of influenza A subtypes in vitro and in vivo.
Although relatively conserved, 21 M2e variants emerged in recent influenza A strains, most of the mutations appeared in the middle part of M2e domain.
In this study, we characterized the in vitro inhibition efficacy of a monoclonal antibody (mAb) M2e8-7 recognizing the N terminus highly conserved epitope SLLTEVET (aa 2-9) which is common for both M1 and M2 proteins.
Peptide binding assay showed that mAb M2e8-7 reacted strongly with M2e and 19 M2e variant peptides.
The mAb M2e8-7 potently inhibited the replication of influenza A virus H1 and H3 subtypes in MDCK cells.
Two important amino acids in M2e epitope, Threonine at position 5 and the Glutamic acid at position 6, were identified to lead antibody-escaping variants.
These results brought new insight in developing vaccine and therapeutic agents against influenza A virus infections.
PMID: 19410554 [PubMed - as supplied by publisher]
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Monoclonal antibody recognizing SLLTEVET epitope of M2 protein potently inhibited the replication of influenza A viruses in MDCK cells.
Wang Y, Zhou L, Shi H, Xu H, Yao H, Xi XG, Toyoda T, Wang X, Wang T. - Laboratory of Wildlife Epidemic Diseases, East China Normal University, Shanghai 200062, China.
The ectodomain of influenza A virus M2 protein (M2e) is composed of 24 amino acids and induces antibodies with inhibitory effect against a broad spectrum of influenza A subtypes in vitro and in vivo.
Although relatively conserved, 21 M2e variants emerged in recent influenza A strains, most of the mutations appeared in the middle part of M2e domain.
In this study, we characterized the in vitro inhibition efficacy of a monoclonal antibody (mAb) M2e8-7 recognizing the N terminus highly conserved epitope SLLTEVET (aa 2-9) which is common for both M1 and M2 proteins.
Peptide binding assay showed that mAb M2e8-7 reacted strongly with M2e and 19 M2e variant peptides.
The mAb M2e8-7 potently inhibited the replication of influenza A virus H1 and H3 subtypes in MDCK cells.
Two important amino acids in M2e epitope, Threonine at position 5 and the Glutamic acid at position 6, were identified to lead antibody-escaping variants.
These results brought new insight in developing vaccine and therapeutic agents against influenza A virus infections.
PMID: 19410554 [PubMed - as supplied by publisher]
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