tetano
Editor, Senior Moderator
Arch Virol. 2013 Dec 20. [Epub ahead of print]
Location and architecture of an antibody-binding site of influenza A virus nucleoprotein.
Varich NL, Sadykova GK, Prilipov AG, Kochergin-Nikitsky KS, Webster RG, Kaverin NV.
Author information
Abstract
Amino acid positions recognized by monoclonal antibodies (MAbs) in the influenza A virus nucleoprotein (NP) have been reported. As these residues were scattered in the three-dimensional (3D) structure of NP, no patterns of the architecture of antibody-binding sites could be inferred. Here, we used site-specific mutagenesis and ELISA to screen the amino acids surrounding position 470 recognized by the MAb 3/1 as a linear epitope. Ten amino acid residues involved in the reaction of NP with the MAb 3/1 and the MAb 469/6 were identified. Our data are the first to outline a compact site recognized by MAbs in the 3D structure of the influenza virus NP.
PMID:
24357080
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24357080
Location and architecture of an antibody-binding site of influenza A virus nucleoprotein.
Varich NL, Sadykova GK, Prilipov AG, Kochergin-Nikitsky KS, Webster RG, Kaverin NV.
Author information
Abstract
Amino acid positions recognized by monoclonal antibodies (MAbs) in the influenza A virus nucleoprotein (NP) have been reported. As these residues were scattered in the three-dimensional (3D) structure of NP, no patterns of the architecture of antibody-binding sites could be inferred. Here, we used site-specific mutagenesis and ELISA to screen the amino acids surrounding position 470 recognized by the MAb 3/1 as a linear epitope. Ten amino acid residues involved in the reaction of NP with the MAb 3/1 and the MAb 469/6 were identified. Our data are the first to outline a compact site recognized by MAbs in the 3D structure of the influenza virus NP.
PMID:
24357080
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24357080