tetano
Editor, Senior Moderator
J Gen Virol. 2010 Oct 21. [Epub ahead of print]
Antiserum against the conserved nine-amino-acid N-terminal peptide of influenza A virus matrix protein 2 is not immuno-protective.
De Filette M, Ysenbaert T, Roose K, Schotsaert M, Roels S, Goossens E, Schepens B, Fiers W, Saelens X.
VIB-UGent;
Abstract
The recent emergence and rapid spread of the pandemic H1N1 swine influenza virus (H1N1v) reminded us once again of the need for a universal influenza vaccine that can elicit heterosubtypic protection. Here, we show the superior immunogenicity and immunoprotective capacity of the full-length matrix protein 2 ectodomain (M2e) peptide coupled to keyhole limpet hemocyanin (KLH) compared to the N-terminal nine amino acid residues of M2e (SP1). Immunization with M2e-KLH protected mice against a lethal challenge with influenza A virus and significantly reduced weight loss and lung virus titres. In addition, passive transfer of serum raised in rabbits against M2e-KLH protected mice against a lethal influenza virus challenge, whereas serum from rabbits immunized with SP1-KLH did not. Nevertheless, immunofluorescence staining revealed that rabbit serum raised against SP1-KLH bound specifically to infected MDCK cells. We conclude that the peptide SP1 contains an immunogenic epitope that is not sufficient for immunoprotection.
PMID: 20965983 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/20965983
Antiserum against the conserved nine-amino-acid N-terminal peptide of influenza A virus matrix protein 2 is not immuno-protective.
De Filette M, Ysenbaert T, Roose K, Schotsaert M, Roels S, Goossens E, Schepens B, Fiers W, Saelens X.
VIB-UGent;
Abstract
The recent emergence and rapid spread of the pandemic H1N1 swine influenza virus (H1N1v) reminded us once again of the need for a universal influenza vaccine that can elicit heterosubtypic protection. Here, we show the superior immunogenicity and immunoprotective capacity of the full-length matrix protein 2 ectodomain (M2e) peptide coupled to keyhole limpet hemocyanin (KLH) compared to the N-terminal nine amino acid residues of M2e (SP1). Immunization with M2e-KLH protected mice against a lethal challenge with influenza A virus and significantly reduced weight loss and lung virus titres. In addition, passive transfer of serum raised in rabbits against M2e-KLH protected mice against a lethal influenza virus challenge, whereas serum from rabbits immunized with SP1-KLH did not. Nevertheless, immunofluorescence staining revealed that rabbit serum raised against SP1-KLH bound specifically to infected MDCK cells. We conclude that the peptide SP1 contains an immunogenic epitope that is not sufficient for immunoprotection.
PMID: 20965983 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/20965983