ArticleClinical and diagnostic laboratory immunology1995
Analysis of immunoglobulin G-binding-protein expression by invasive isolates of Streptococcus pyogenes.
Article in Clinical and diagnostic laboratory immunology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Sequence element enrichment analysis to determine the genetic basis of bacterial phenotypes.Nature communications · 2016Article
- Streptococcus pyogenes infection in mouse skin leads to a time-dependent up-regulation of protein H expression.Infection and immunity · 2003Article
- Identification and characterization of a novel secreted immunoglobulin binding protein from group A streptococcus.Infection and immunity · 2001Article
- Restoration of Mga function to a Streptococcus pyogenes strain (M Type 50) that is virulent in mice.Infection and immunity · 2001Article
- Pathogenesis of group A streptococcal infections.Clinical microbiology reviews · 2000Review
- Distinct profiles of immunoglobulin G-binding-protein expression by invasive serotype M1 isolates of Streptococcus pyogenes.Clinical and diagnostic laboratory immunology · 1995Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Invasive group A streptococcal isolates collected as part of a Centers for Disease Control and Prevention surveillance study were analyzed for expression of immunoglobulin G (IgG)-binding proteins. Two IgG-binding phenotypes of group A isolates of the M1 serotype were identified. The first group expressed a surface protein that bound all four human IgG subclasses (type IIo) and was recognized by rabbit anti-serotype M1-specific antiserum but not by normal rabbit serum. The second group expressed an IgG-binding protein that was also recognized by the anti-serotype M1 antiserum but demonstrated significant nonimmune reactivity only with human IgG3 (type IIb). Analysis of extracts of the isolates for reactivity with human IgA, fibrinogen, and albumin was also performed. The importance of the binding of human plasma proteins to pathogenic group A streptococci remains to be established.
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Registered trials
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