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Visualisation and Quantification of Intracellular Interactions of Neisseria meningitidis and Human α-actinin by Confocal Imaging
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CD66 carcinoembryonic antigens mediate interactions between Opa-expressing Neisseria gonorrhoeae and human

S D Gray-Owen1, C Dehio, A Haude

  • 1Max-Planck-Institut für Biologie, Abteilung Infektionsbiologie, Tübingen, Germany.

The EMBO Journal
|June 1, 1997
PubMed

Insights

Neisseria gonorrhoeae uses Opa52 outer membrane proteins to bind to CD66 receptors on human cells. This interaction facilitates bacterial entry into polymorphonuclear phagocytes (PMNs), contributing to infection.

Area of Science:

  • Microbiology
  • Immunology
  • Cell Biology

Background:

  • Neisseria gonorrhoeae colonization involves polymorphonuclear phagocytes (PMNs) and bacterial internalization.
  • Phase-variable opacity (Opa) proteins are key mediators of bacterial interactions with host cells.

Purpose of the Study:

  • To identify the specific cellular receptors for Neisseria gonorrhoeae Opa52 outer membrane proteins.
  • To elucidate the mechanism of Opa52-mediated bacterial entry into host cells.

Main Methods:

  • Overlay assays and affinity isolation techniques were used to identify bacterial-host cell interactions.
  • Transfected HeLa cell lines expressing CD66 family members were utilized to test receptor binding.
  • Confocal laser scanning microscopy visualized antigen recruitment during bacterial interaction.

Main Results:

  • Opa52-expressing Neisseria gonorrhoeae directly interacts with human carcinoembryonic antigen (CEA) family members (CD66a, CD66c, CD66d, CD66e).
  • Specific binding and internalization of Opa52 gonococci were observed in cells expressing CD66 family members.
  • Opa52-mediated interactions were inhibited by anti-CEA sera, confirming receptor specificity.

Conclusions:

  • Members of the CEA family serve as cellular receptors for Neisseria gonorrhoeae Opa52.
  • This interaction is crucial for the binding and internalization of gonococci by host cells, including PMNs.

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