EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity
2008
How EndoS and SpeB from Streptococcus pyogenes Interact
publication
Evidence: moderate
Author Information
Author(s): Maria Allhorn, Arne Olsén, Mattias Collin
Primary Institution: Lund University, Biomedical Center
Hypothesis
What are the amino acids required for the IgG glycan-hydrolyzing activity of EndoS?
Conclusion
EndoS is processed and inactivated by SpeB, with glutamic acid 235 being essential for its activity.
Supporting Evidence
- EndoS hydrolyzes IgG, impairing antibody function and enhancing bacterial survival.
- SpeB processes and degrades EndoS, leading to loss of its activity.
- Glutamic acid 235 is essential for EndoS's glycan-hydrolyzing activity.
Takeaway
EndoS helps bacteria survive by breaking down antibodies, but another enzyme, SpeB, can destroy EndoS, making it less effective.
Methodology
The study involved in vitro experiments examining the production, stability, and activity of EndoS and SpeB, along with site-directed mutagenesis and structural modeling.
Limitations
Attempts to express parts of EndoS separately for functional studies were unsuccessful.
Digital Object Identifier (DOI)
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