Characterisation of receptor binding by the chemotaxis inhibitory protein of Staphylococcus aureus and the effects of the host immune response
2007

Understanding the Chemotaxis Inhibitory Protein of Staphylococcus aureus

Sample size: 31 publication 10 minutes Evidence: moderate

Author Information

Author(s): Wright Andrew J., Higginbottom Adrian, Philippe Didier, Upadhyay Abhishek, Bagby Stefan, Read Robert C., Monk Peter N., Partridge Lynda J.

Primary Institution: University of Sheffield

Hypothesis

Can the chemotaxis inhibitory protein of Staphylococcus aureus (CHIPS) bind to human receptors and affect the immune response?

Conclusion

CHIPS is likely too immunogenic to be used as an anti-inflammatory treatment, but some antibodies against CHIPS may be useful in treating S. aureus infections.

Supporting Evidence

  • Recombinant CHIPS28–149 binds with high affinity to the human C5a receptor.
  • All human sera examined contained high titres of IgG and IgA reactivity against CHIPS28–149.
  • Sera from infected individuals were more likely to inhibit CHIPS28–149 binding than sera from healthy controls.
  • High antibody titres correlated with both inhibition and enhancement of CHIPS28–149 binding to C5aR.

Takeaway

This study looks at a protein from Staphylococcus aureus that can stop the immune system from working too hard, but it might not be safe to use as a medicine because it can make the body react too strongly.

Methodology

The study involved producing recombinant CHIPS, testing its binding to human receptors, and analyzing serum samples from infected and uninfected individuals for antibody responses.

Potential Biases

Potential bias in serum sample selection and the interpretation of antibody effects.

Limitations

The study's findings may not be applicable to all populations due to the limited sample size and the specific focus on certain patient groups.

Participant Demographics

31 serum samples from 7 S. aureus infected patients and 24 normal donors.

Digital Object Identifier (DOI)

10.1016/j.molimm.2006.12.022

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