Source:http://linkedlifedata.com/resource/pubmed/id/11420143
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
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| pubmed:dateCreated |
2001-6-22
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| pubmed:abstractText |
The dystroglycan gene produces two products from a single mRNA, the extracellular alpha-dystroglycan and the transmembrane beta-dystroglycan. The Duchenne muscular dystrophy protein, dystrophin, associates with the muscle membrane via beta-dystroglycan, the WW domain of dystrophin interacting with a PPxY motif in beta-dystroglycan. A panel of four monoclonal antibodies (MANDAG1-4) was produced using the last 16 amino acids of beta-dystroglycan as immunogen. The mAbs recognized a 43 kDa band on Western blots of all cells and tissues tested and stained the sarcolemma in immunohistochemistry of skeletal muscle over a wide range of animal species. A monoclonal antibody (mAb) against the WW domain of dystrophin, MANHINGE4A, produced using a 16-mer synthetic peptide, recognized dystrophin on Western blots and also stained the sarcolemma. We have identified the precise sequences recognized by the mAbs using a phage-displayed random 15-mer peptide library. A 7-amino-acid consensus sequence SPPPYVP involved in binding all four beta-dystroglycan mAbs was identified by sequencing 17 different peptides selected from the library. PPY were the most important residues for three mAbs, but PxxVP were essential residues for a fourth mAb, MANDAG2. By sequencing five different random peptides from the library, the epitope on dystrophin recognized by mAb MANHINGE4A was identified as PWxRA in the first beta-strand of the WW domain, with the W and R residues invariably present. A recent three-dimensional structure confirms that the two epitopes are adjacent in the dystrophin-dystroglycan complex, highlighting the question of how the two interacting motifs can also be accessible to antibodies during immunolocalization in situ.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dystroglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0006-3002
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
2
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| pubmed:volume |
1527
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
54-60
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11420143-Amino Acid Motifs,
pubmed-meshheading:11420143-Amino Acid Sequence,
pubmed-meshheading:11420143-Animals,
pubmed-meshheading:11420143-Antibodies, Monoclonal,
pubmed-meshheading:11420143-Antibody Specificity,
pubmed-meshheading:11420143-Blotting, Western,
pubmed-meshheading:11420143-Cytoskeletal Proteins,
pubmed-meshheading:11420143-Dystroglycans,
pubmed-meshheading:11420143-Dystrophin,
pubmed-meshheading:11420143-Epitope Mapping,
pubmed-meshheading:11420143-Epitopes,
pubmed-meshheading:11420143-Escherichia coli,
pubmed-meshheading:11420143-Membrane Glycoproteins,
pubmed-meshheading:11420143-Mice,
pubmed-meshheading:11420143-Models, Molecular,
pubmed-meshheading:11420143-Molecular Sequence Data,
pubmed-meshheading:11420143-Protein Structure, Tertiary,
pubmed-meshheading:11420143-Sequence Homology, Amino Acid
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| pubmed:year |
2001
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| pubmed:articleTitle |
Epitopes in the interacting regions of beta-dystroglycan (PPxY motif) and dystrophin (WW domain).
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| pubmed:affiliation |
MRIC Biochemistry Group, North East Wales Institute, Mold Road, LL11 2AW, Wrexham, UK.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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