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Antibodies to streptococcal surface enolase react with human alpha-enolase: implications in poststreptococcal
P A Fontán1, V Pancholi, M M Nociari
1Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, New York 10021, USA.
The Journal of Infectious Diseases
|November 9, 2000
Summary
Group A Streptococcus bacteria have a protein, enolase, that is similar to human enolase. Antibodies against this bacterial enolase may trigger autoimmune responses in acute rheumatic fever.
Area of Science:
- Immunology
- Microbiology
- Rheumatology
Background:
- Pathogenic mechanisms of acute rheumatic fever (ARF) post-group A streptococcal (GAS) pharyngitis remain unclear.
- GAS bacteria possess surface glycolytic enzyme enolase, a potential virulence factor.
- Human and bacterial enolase share structural similarities.
Purpose of the Study:
- To investigate the role of streptococcal enolase in ARF pathogenesis.
- To determine if antibodies against GAS enolase cross-react with human enolase.
- To explore the potential of GAS enolase as an autoimmune target in ARF.
Main Methods:
- Fluorocytometric analysis to detect antibody cross-reactivity.
- Assessment of enolase expression on hematopoietic cells.
- Measurement of antibody titers in patient serum samples.
Main Results:
- Significant cross-reactivity observed between streptococcal and human enolase.
- Anti-streptococcal enolase antibodies bind to human enolase on hematopoietic cells.
- Enolase expression on leukocytes is upregulated by inflammatory stimuli.
- Elevated antibody titers against both bacterial and human enolase in ARF patients compared to controls.
Conclusions:
- Streptococcal enolase acts as a novel cross-reactive antigen.
- This cross-reactivity may initiate autoimmune responses in ARF.
- GAS enolase is a potential key player in ARF development.