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Complement consumption gonococcal peptidoglycan.

B H Petersen, R S Rosenthal

    Infection and Immunity
    |February 1, 1982
    PubMed
    Summary
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    Neisseria gonorrhoeae peptidoglycan consumes complement via the classical pathway, requiring anti-peptidoglycan antibodies and intact polymer structures. Lysozyme digestion inactivates this complement-consuming activity.

    Area of Science:

    • Immunology
    • Microbiology
    • Biochemistry

    Background:

    • Neisseria gonorrhoeae peptidoglycan (PG) is a key component of the bacterial cell wall.
    • The complement system is a crucial part of innate immunity.

    Purpose of the Study:

    • To investigate the ability of purified Neisseria gonorrhoeae peptidoglycan to activate and consume complement in human serum.
    • To elucidate the mechanism and requirements for peptidoglycan-mediated complement consumption.

    Main Methods:

    • Purified Neisseria gonorrhoeae peptidoglycan (intact and sonicated) was incubated with normal human serum.
    • Complement levels and specific complement components (C3, C4) were measured.
    • Experiments were conducted using C4-deficient serum and complement pathway-inhibited serum.

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  • The effect of anti-peptidoglycan antibody and lysozyme digestion was assessed.
  • Main Results:

    • Sonicated and intact peptidoglycan consumed hemolytic complement in normal human serum.
    • Complement consumption was dependent on the presence of C4 and antibody to peptidoglycan.
    • Lysozyme digestion of peptidoglycan abolished its complement-consuming activity.
    • Complement consumption involved depletion of C3 and C4, indicating classical pathway activation.

    Conclusions:

    • Neisseria gonorrhoeae peptidoglycan consumption of complement is mediated by the classical pathway.
    • This process requires glycosidically linked polymers of peptidoglycan and is enhanced by anti-PG antibody.
    • Variability in complement consumption among individuals may be due to natural antibody levels or PG hydrolase activity.