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Gonococcal opacity: lectin-like interactions between Opa proteins and lipooligosaccharide

M S Blake1, C M Blake, M A Apicella

  • 1Laboratory of Bacteriology and Immunology, Rockefeller University, New York, New York 10021.

Infection and Immunity
|April 1, 1995
PubMed
Summary

Neisseria gonorrhoeae Opa proteins bind to specific lipooligosaccharide (LOS) structures, particularly the Gal beta 1-4GlcNAc residue. This interaction is similar to mammalian asialoglycoprotein receptor binding and is disrupted by sialylation of the LOS.

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Area of Science:

  • Microbiology
  • Bacteriology
  • Molecular Biology

Background:

  • Neisseria gonorrhoeae Opa proteins mediate intercellular adhesion via interactions with bacterial lipooligosaccharide (LOS).
  • Previous studies suggested Opa-LOS interactions are crucial for gonococcal pathogenesis.

Purpose of the Study:

  • To characterize the specific gonococcal LOS structures recognized by Opa proteins.
  • To compare the binding specificities of Opa proteins with mammalian asialoglycoprotein receptors.

Main Methods:

  • A modified noncompetitive inhibition assay was employed.
  • LOS structures from Neisseria gonorrhoeae mutants were used.
  • Direct enzyme-linked immunosorbent assays and antibody inhibition assays measured Opa-LOS binding affinities.

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Main Results:

  • Gonococcal Opa proteins exhibited highest affinity for the Gal beta 1-4GlcNAc residue on lactoneoseries LOS.
  • This binding affinity was comparable to that of hepatic asialoglycoprotein receptors for similar carbohydrate structures.
  • Sialylation of the lactoneoseries LOS abolished Opa protein binding.

Conclusions:

  • Gonococcal Opa proteins specifically recognize the Gal beta 1-4GlcNAc moiety on LOS.
  • Opa-LOS interactions share similar specificities with mammalian asialoglycoprotein receptor-carbohydrate interactions.
  • These findings provide insights into gonococcal adhesion mechanisms and potential host-pathogen interactions.