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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-5-27
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pubmed:databankReference | |
pubmed:abstractText |
A two-dimensional structural model was devised for the Opc outer membrane protein invasin which contains 10 transmembrane strands and five surface-exposed loops. One continuous epitope recognized by three monoclonal antibodies was localized to the tip of loop 2 by synthetic peptides and site-directed mutagenesis while a second, discontinuous epitope recognized by a fourth antibody was localized to loops 4 and 5 by insertion mutagenesis. These monoclonal antibodies are bactericidal and inhibit adhesion and invasion. Most of the T-cell epitopes defined by Wiertz et al. (1996) were localized to the transmembrane strands. Oligonucleotides encoding a foreign epitope (nabla) from Semliki Forest virus were inserted into BglII restriction sites created by site-directed mutagenesis. The nabla epitopes inserted in all five predicted loops were recognized on the cell surface of live Escherichia coli bacteria by a monoclonal antibody and are exposed while nabla epitopes in the N-terminus or three predicted turns were not. The results thus confirm important predictions of the model and define five permissive sites within surface-exposed loops which can be used to insert foreign epitopes.
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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/Adhesins, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/invasin, Yersinia,
http://linkedlifedata.com/resource/pubmed/chemical/opc protein, bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
281-93
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9044262-Adhesins, Bacterial,
pubmed-meshheading:9044262-Amino Acid Sequence,
pubmed-meshheading:9044262-Bacterial Outer Membrane Proteins,
pubmed-meshheading:9044262-Bacterial Proteins,
pubmed-meshheading:9044262-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:9044262-Fluorescent Antibody Technique,
pubmed-meshheading:9044262-Molecular Sequence Data,
pubmed-meshheading:9044262-Neisseria meningitidis,
pubmed-meshheading:9044262-Protein Structure, Secondary
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pubmed:year |
1997
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pubmed:articleTitle |
Two-dimensional structure of the Opc invasin from Neisseria meningitidis.
|
pubmed:affiliation |
Max-Planck Institut für molekulare Genetik, Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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