tetano
Editor, Senior Moderator
Microbiol Immunol. 2012 Feb 7. doi: 10.1111/j.1348-0421.2012.00412.x. [Epub ahead of print]
Reactivity of human convalescent sera with influenza virus HA protein mutants at antigenic site A.
Nobusawa E, Omagari K, Nakajima S, Nakajima K.
Source
Department of Virology, Nagoya City University Graduate School of Medical Science, Nagoya City, Aichi, Japan.
Abstract
It is not well understood how the antibodies of individual convalescent human serum bind to each amino acid residue at the antigenic sites of hemagglutinin (HA) of influenza viruses, and how the antigenic drift strains of influenza viruses are selected by the human sera. In our previous study we indicated that the convalescent human sera, following A/Kamata/14/91(Ka/91)-like (H3N2) virus infection, bind to antigenic site A of Ka/91 HA, by a binding assay with a chimeric HA between Ka/91 and A/Aichi/2/68. Here we show how those human sera recognized each amino acid residue at antigenic site A, using the chimeric HAs possessing single amino acid substitutions at site A. The results showed; 1) there was a difference from person to person in the capacity of the human sera to recognize amino acid substitutions at site A, and 2) some amino acid substitutions caused all convalescent human sera to lose their binding capacity. Among them certain amino acid substitutions might be selected by chance for the successive antigenic drift. Phylogenetic analysis of the drift strains of Ka/91 showed amino acid substitutions at positions 133, 135 and 145 were on the main stream of the phylogenetic tree. Indeed, one of them was not recognized by all the investigated convalescent sera.
? 2012 The Societies and Blackwell Publishing Asia Pty Ltd.
PMID:
22309642
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22309642
Reactivity of human convalescent sera with influenza virus HA protein mutants at antigenic site A.
Nobusawa E, Omagari K, Nakajima S, Nakajima K.
Source
Department of Virology, Nagoya City University Graduate School of Medical Science, Nagoya City, Aichi, Japan.
Abstract
It is not well understood how the antibodies of individual convalescent human serum bind to each amino acid residue at the antigenic sites of hemagglutinin (HA) of influenza viruses, and how the antigenic drift strains of influenza viruses are selected by the human sera. In our previous study we indicated that the convalescent human sera, following A/Kamata/14/91(Ka/91)-like (H3N2) virus infection, bind to antigenic site A of Ka/91 HA, by a binding assay with a chimeric HA between Ka/91 and A/Aichi/2/68. Here we show how those human sera recognized each amino acid residue at antigenic site A, using the chimeric HAs possessing single amino acid substitutions at site A. The results showed; 1) there was a difference from person to person in the capacity of the human sera to recognize amino acid substitutions at site A, and 2) some amino acid substitutions caused all convalescent human sera to lose their binding capacity. Among them certain amino acid substitutions might be selected by chance for the successive antigenic drift. Phylogenetic analysis of the drift strains of Ka/91 showed amino acid substitutions at positions 133, 135 and 145 were on the main stream of the phylogenetic tree. Indeed, one of them was not recognized by all the investigated convalescent sera.
? 2012 The Societies and Blackwell Publishing Asia Pty Ltd.
PMID:
22309642
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22309642