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rdf:type |
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lifeskim:mentions |
umls-concept:C0003316,
umls-concept:C0007301,
umls-concept:C0022564,
umls-concept:C0032120,
umls-concept:C0043250,
umls-concept:C0086418,
umls-concept:C0237876,
umls-concept:C0318143,
umls-concept:C0370215,
umls-concept:C0439064,
umls-concept:C0700271,
umls-concept:C1167622
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pubmed:issue |
1
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pubmed:dateCreated |
1999-12-3
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pubmed:databankReference |
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pubmed:abstractText |
Besides group A (GAS), Lancefield group C beta-haemolytic streptococci (GCS) have been implicated as a causative agent in outbreaks of purulent pharyngitis. In this study we have investigated a class CI M protein of a Streptococcus dysgalactiae1:256, revealed that 26% of these sera showed serological cross-reactivity between a 68-kDa cartilage protein and the N-terminal part of MC. Only 8% of the sera of healthy patients showed this property. In additional, MC also cross-reacted with antibodies recognising epidermal keratins. The cross-reacting 68-kDa protein from cartilage was different from human serum albumin, but was recognised with anti-vimentin immune serum. The MC was cloned and the gene sequenced. By using PCR, recombinant gene fragments encoding characteristic peptide fragments of MC were expressed in Escherichia coli. The peptides were used to map the binding sites for plasma proteins and to locate the cross-reacting epitopes on the MC molecule. In consequence, sequence alignments revealed that MC shared homologous regions with vimentin and different keratins. Our data, obtained with MC, suggest that not only infections with GAS but also infections with GCS and possibly GGS (the latter species can also produce class CI M-like proteins) may be responsible for the formation of streptococcal-associated sequel diseases.
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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 |
Oct
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pubmed:issn |
0928-8244
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-24
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10518039-Amino Acid Sequence,
pubmed-meshheading:10518039-Animals,
pubmed-meshheading:10518039-Antigens, Bacterial,
pubmed-meshheading:10518039-Bacterial Outer Membrane Proteins,
pubmed-meshheading:10518039-Bacterial Proteins,
pubmed-meshheading:10518039-Blood Proteins,
pubmed-meshheading:10518039-Blotting, Western,
pubmed-meshheading:10518039-Carrier Proteins,
pubmed-meshheading:10518039-Cartilage,
pubmed-meshheading:10518039-Chick Embryo,
pubmed-meshheading:10518039-Cross Reactions,
pubmed-meshheading:10518039-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10518039-Epitopes,
pubmed-meshheading:10518039-Humans,
pubmed-meshheading:10518039-Immune Sera,
pubmed-meshheading:10518039-Keratins,
pubmed-meshheading:10518039-Molecular Sequence Data,
pubmed-meshheading:10518039-Phagocytosis,
pubmed-meshheading:10518039-Protein Binding,
pubmed-meshheading:10518039-Rabbits,
pubmed-meshheading:10518039-Sequence Homology, Amino Acid,
pubmed-meshheading:10518039-Streptococcal Infections,
pubmed-meshheading:10518039-Streptococcus,
pubmed-meshheading:10518039-Virulence,
pubmed-meshheading:10518039-Wounds and Injuries
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pubmed:year |
1999
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pubmed:articleTitle |
M protein of a Streptococcus dysgalactiae human wound isolate shows multiple binding to different plasma proteins and shares epitopes with keratin and human cartilage.
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pubmed:affiliation |
Hospital of the Friedrich-Schiller-University, Institute of Medical Microbiology, Semmelweissstr. 4, D-07740, Jena, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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