Analysis of the molecular mimicry between HLA-B27 and a bacterial OmpA protein using synthetic peptides.
Identifieur interne : 000643 ( Ncbi/Checkpoint ); précédent : 000642; suivant : 000644Analysis of the molecular mimicry between HLA-B27 and a bacterial OmpA protein using synthetic peptides.
Auteurs : D T Yu ; T. Hamachi ; M. Hamachi ; G. TribbickSource :
- Clinical and experimental immunology [ 0009-9104 ] ; 1991.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Peptides.
- chemical , chemistry : Bacterial Outer Membrane Proteins, HLA-B27 Antigen.
- chemical , immunology : Antibodies, Monoclonal, Bacterial Outer Membrane Proteins.
- Amino Acid Sequence, Escherichia coli, Humans, Molecular Sequence Data.
Abstract
In spite of a lack of sequence 'homology' between HLA-B27 and the bacterial OmpA outer membrane proteins, they both react with the Ye-2 monoclonal anti-HLA-B27 antibody. The Ye-2 antibody also reacted positively in ELISA with a synthetic peptide derived from the segment spanning residues 63-84 of B*2705. The critical peptide residues were determined by testing first with overlapping peptides, followed by a replacement set made according to the determined epitope. The results were compared with those with overlapping eight mers made to span a carboxyl fragment of the Escherichia coli OmpA protein. They indicate the reason why Ye-2 reacts with both sets of peptides is because it has a preference for polymers of arginine.
DOI: 10.1111/j.1365-2249.1991.tb05758.x
PubMed: 1893633
Affiliations:
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pubmed:1893633Le document en format XML
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<series><title level="j">Clinical and experimental immunology</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Antibodies, Monoclonal (immunology)</term>
<term>Bacterial Outer Membrane Proteins (chemistry)</term>
<term>Bacterial Outer Membrane Proteins (immunology)</term>
<term>Escherichia coli</term>
<term>HLA-B27 Antigen (chemistry)</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Peptides (analysis)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps monoclonaux (immunologie)</term>
<term>Antigène HLA-B27 ()</term>
<term>Données de séquences moléculaires</term>
<term>Escherichia coli</term>
<term>Humains</term>
<term>Peptides (analyse)</term>
<term>Protéines de la membrane externe bactérienne ()</term>
<term>Protéines de la membrane externe bactérienne (immunologie)</term>
<term>Séquence d'acides aminés</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Peptides</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Outer Membrane Proteins</term>
<term>HLA-B27 Antigen</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Bacterial Outer Membrane Proteins</term>
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<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Peptides</term>
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<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term>
<term>Protéines de la membrane externe bactérienne</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Escherichia coli</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Antigène HLA-B27</term>
<term>Données de séquences moléculaires</term>
<term>Escherichia coli</term>
<term>Humains</term>
<term>Protéines de la membrane externe bactérienne</term>
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<front><div type="abstract" xml:lang="en">In spite of a lack of sequence 'homology' between HLA-B27 and the bacterial OmpA outer membrane proteins, they both react with the Ye-2 monoclonal anti-HLA-B27 antibody. The Ye-2 antibody also reacted positively in ELISA with a synthetic peptide derived from the segment spanning residues 63-84 of B*2705. The critical peptide residues were determined by testing first with overlapping peptides, followed by a replacement set made according to the determined epitope. The results were compared with those with overlapping eight mers made to span a carboxyl fragment of the Escherichia coli OmpA protein. They indicate the reason why Ye-2 reacts with both sets of peptides is because it has a preference for polymers of arginine.</div>
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<name sortKey="Hamachi, T" sort="Hamachi, T" uniqKey="Hamachi T" first="T" last="Hamachi">T. Hamachi</name>
<name sortKey="Tribbick, G" sort="Tribbick, G" uniqKey="Tribbick G" first="G" last="Tribbick">G. Tribbick</name>
<name sortKey="Yu, D T" sort="Yu, D T" uniqKey="Yu D" first="D T" last="Yu">D T Yu</name>
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