ArticleInfection and immunity1989
Vimentin-cross-reactive epitope of type 12 streptococcal M protein.
Article in Infection and immunity, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 33 citations in OpenAlex.
- Suggested organism entry portal of necrotizing fasciitis with complete DNA from fascia, blood, and pharyngeal ulcers: A case report.Annals of medicine and surgery (2012) · 2022Article
- Vimentin as a Multifaceted Player and Potential Therapeutic Target in Viral Infections.International journal of molecular sciences · 2020Review
- Molecular Mimicry, Autoimmunity, and Infection: The Cross-Reactive Antigens of Group A Streptococci and their Sequelae.Microbiology spectrum · 2019Review
- Relevance of molecular mimicry in the mediation of infectious myocarditis.Journal of cardiovascular translational research · 2014Review
- Vimentin compartmentalization in discoid lupus.North American journal of medical sciences · 2010Article
- Association of mannose-binding lectin gene polymorphism but not of mannose-binding serine protease 2 with chronic severe aortic regurgitation of rheumatic etiology.Clinical and vaccine immunology : CVI · 2008Article
- Cytotoxic mAb from rheumatic carditis recognizes heart valves and laminin.The Journal of clinical investigation · 2000Article
- Molecular analysis of human cardiac myosin-cross-reactive B- and T-cell epitopes of the group A streptococcal M5 protein.Infection and immunity · 1997Article
- gp330 associates with a 44-kDa protein in the rat kidney to form the Heymann nephritis antigenic complex.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- The cytoskeleton and its importance as a mediator of inflammation.Annals of the rheumatic diseases · 1992Review
- Cytotoxic and viral neutralizing antibodies crossreact with streptococcal M protein, enteroviruses, and human cardiac myosin.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- Immunoreactivity of anti-streptococcal monoclonal antibodies to human heart valves. Evidence for multiple cross-reactive epitopes.The American journal of pathology · 1991Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The NH2-terminal amino acid sequence of type 12 M protein was determined by automated Edman degradation of a 38-kilodalton polypeptide fragment purified from a limited pepsin digest of intact type 12 streptococci. The sequence of the first 13 amino acid residues of the polypeptide confirmed that predicted by the nucleotide sequence of the mature type 12 M protein. A chemically synthesized peptide copying the NH2-terminal 25 residues, SM12(1-25)C, evoked opsonic antibodies against type 12 streptococci as well as renal glomerular cross-reactive antibodies. The serum from one of six rabbits reacted in immunofluorescence tests with human glomeruli in a mesangial staining pattern. The cross-reactive antibodies were completely inhibited by the immunizing peptide and absorption with type 12 streptococci. Subpeptides of the 25-residue synthetic peptide were without inhibitory effect, suggesting that the cross-reactive antibodies are directed against a conformational epitope of SM12(1-25)C. Anti-SM12(1-25)C antisera reacted specifically with the intermediate filament protein vimentin extracted from mesangial cells. None of the cross-reactions of anti-SM12(1-25)C were inhibited by a synthetic peptide SM1(1-26)C of type 1 M protein, which was previously shown to share a cross-reactive epitope with vimentin. These results indicate that type 12 M protein contains at least one vimentin cross-reactive epitope that is clearly distinct from the tetrapeptide epitope shared with vimentin by type 1 M protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.