Herrin, Brantley R.;
Alder, Matthew N.;
Roux, Kenneth H.;
Sina, Christina;
Ehrhardt, Götz R. A.;
Boydston, Jeremy A.;
Turnbough, Charles L.;
Cooper, Max D.
Structure and specificity of lamprey monoclonal antibodies
Sie können Bookmarks mittels Listen verwalten, loggen Sie sich dafür bitte in Ihr SLUB Benutzerkonto ein.
Medientyp:
E-Artikel
Titel:
Structure and specificity of lamprey monoclonal antibodies
Beteiligte:
Herrin, Brantley R.;
Alder, Matthew N.;
Roux, Kenneth H.;
Sina, Christina;
Ehrhardt, Götz R. A.;
Boydston, Jeremy A.;
Turnbough, Charles L.;
Cooper, Max D.
Erschienen:
Proceedings of the National Academy of Sciences, 2008
Erschienen in:Proceedings of the National Academy of Sciences
Beschreibung:
<jats:p>
Adaptive immunity in jawless vertebrates (lamprey and hagfish) is mediated by lymphocytes that undergo combinatorial assembly of leucine-rich repeat (LRR) gene segments to create a diverse repertoire of variable lymphocyte receptor (
<jats:italic>VLR</jats:italic>
) genes. Immunization with particulate antigens induces VLR-B-bearing lymphocytes to secrete antigen-specific VLR-B antibodies. Here, we describe the production of recombinant VLR-B antibodies specific for BclA, a major coat protein of
<jats:italic>Bacillus anthracis</jats:italic>
spores. The recombinant VLR-B antibodies possess 8–10 uniform subunits that collectively bind antigen with high avidity. Sequence analysis, mutagenesis, and modeling studies show that antigen binding involves residues in the β-sheets lining the VLR-B concave surface. EM visualization reveals tetrameric and pentameric molecules having a central core and highly flexible pairs of stalk-region “arms” with antigen-binding “hands.” Remarkable antigen-binding specificity, avidity, and stability predict that these unusual LRR-based monoclonal antibodies will find many biomedical uses.
</jats:p>