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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Hamachi</name></author><author><name sortKey="Hamachi, M" sort="Hamachi, M" uniqKey="Hamachi M" first="M" last="Hamachi">M. Hamachi</name></author><author><name sortKey="Tribbick, G" sort="Tribbick, G" uniqKey="Tribbick G" first="G" last="Tribbick">G. Tribbick</name></author></analytic><series><title level="j">Clinical and experimental immunology</title><idno type="ISSN">0009-9104</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><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></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Protéines de la membrane externe bactérienne</term></keywords><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><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Hamachi, M" sort="Hamachi, M" uniqKey="Hamachi M" first="M" last="Hamachi">M. Hamachi</name><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></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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