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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1996-12-26
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pubmed:abstractText |
Immunological mimicry between host and microbial proteins has been suggested as a potential mechanism in the development of uveitis in humans. In this study immunological crossreactivity between anti-streptococcal monoclonal antibodies (MAbs) and the human eye was investigated. In indirect immunofluorescence, we demonstrated novel immunological crossreactivity of two anti-streptococcal MAbs (27 and 112) with the rod outer (and inner) segments of the retina of the human eye. In further studies, retinal S-Ag, a uveitogenic protein in the rod outer (and inner) segments, was found to react with the anti-streptococcal MAbs. In addition, several uveitogenic peptides of S-Ag were recognized by the anti-streptococcal MAbs. In the ELISA and Western immunoblot, anti-S-Ag MAbs crossreacted with group A streptococci and the streptococcal M protein further demonstrating sites of antigenic similarity. Homology between the retinal S-Ag and streptococcal M protein was observed in amino acid sequences repeated in the B repeat region of the streptococcal M5 protein. These data show that retinal S-antigen has immunological similarities with streptococcal M protein, a major virulence determinant and strong bacterial cell surface antigen.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Arrestin,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/streptococcal M protein
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pubmed:status |
MEDLINE
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pubmed:issn |
0891-6934
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
95-106
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8722579-Amino Acid Sequence,
pubmed-meshheading:8722579-Antigens, Bacterial,
pubmed-meshheading:8722579-Arrestin,
pubmed-meshheading:8722579-Bacterial Outer Membrane Proteins,
pubmed-meshheading:8722579-Bacterial Proteins,
pubmed-meshheading:8722579-Blotting, Western,
pubmed-meshheading:8722579-Carrier Proteins,
pubmed-meshheading:8722579-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:8722579-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:8722579-Humans,
pubmed-meshheading:8722579-Molecular Mimicry,
pubmed-meshheading:8722579-Molecular Sequence Data,
pubmed-meshheading:8722579-Sequence Homology, Amino Acid,
pubmed-meshheading:8722579-Streptococcus pyogenes,
pubmed-meshheading:8722579-Uveitis
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pubmed:year |
1995
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pubmed:articleTitle |
Immunological mimicry between retinal S-antigen and group A streptococcal M proteins.
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pubmed:affiliation |
Department of Ophthalmology, University of Oklahoma Health Science Center, Oklahoma City 73190, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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