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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2008-2-14
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pubmed:databankReference |
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pubmed:abstractText |
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 (VLR) 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 Bacillus anthracis 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 beta-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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-12618454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-14113107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-14238932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-15241406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-15964979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-16030225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-16249180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-16373579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-16670316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-17187071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-17192264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-17468760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-4099053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-4195499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18238899-5690272
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2040-5
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pubmed:dateRevised |
2010-9-22
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pubmed:meshHeading |
pubmed-meshheading:18238899-Amino Acid Sequence,
pubmed-meshheading:18238899-Animals,
pubmed-meshheading:18238899-Antibodies, Monoclonal,
pubmed-meshheading:18238899-Antibody Specificity,
pubmed-meshheading:18238899-Antigens,
pubmed-meshheading:18238899-Cell Line,
pubmed-meshheading:18238899-Dimerization,
pubmed-meshheading:18238899-Humans,
pubmed-meshheading:18238899-Lampreys,
pubmed-meshheading:18238899-Models, Molecular,
pubmed-meshheading:18238899-Molecular Sequence Data,
pubmed-meshheading:18238899-Protein Conformation,
pubmed-meshheading:18238899-Sequence Homology, Amino Acid
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pubmed:year |
2008
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pubmed:articleTitle |
Structure and specificity of lamprey monoclonal antibodies.
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pubmed:affiliation |
Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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