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Area of Science:

  • Microbiology
  • Immunology
  • Evolutionary Biology

Background:

  • Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) is an Ig-related glycoprotein acting as a receptor for Gram-negative bacterial pathogens.
  • Human pathogens including Neisseria gonorrhoeae, N. meningitidis, Moraxella catarrhalis, and Haemophilus influenzae utilize CEACAM1-binding adhesins.
  • CEACAM1 plays roles in cell adhesion, epithelial differentiation, and T-cell regulation, with mammalian orthologues existing.

Purpose of the Study:

  • To investigate if bacterial adhesins from human pathogens can recognize CEACAM1 orthologues in other mammals.
  • To determine the functional consequences of sequence divergence in CEACAM1 orthologues for bacterial recognition and cellular invasion.

Main Methods:

  • Sequence comparison of the amino-terminal Ig-variable-like domain of CEACAM1 orthologues (human, murine, canine, bovine).
  • Utilizing GFP-tagged, soluble amino-terminal domains of CEACAM1 to assess bacterial association.
  • Transfection of cells with full-length human and murine CEACAM1 to evaluate Neisseria gonorrhoeae internalization.

Main Results:

  • Significant sequence divergence in the bacteria-binding CC'FG-face of the Ig-fold among human, murine, canine, and bovine CEACAM1 orthologues.
  • Bacterial pathogens selectively associated with human CEACAM1, but not with CEACAM1 from other mammals.
  • Human CEACAM1 mediated Neisseria gonorrhoeae internalization, while murine CEACAM1 did not.

Conclusions:

  • Human-restricted bacterial pathogens exhibit selective interaction with human CEACAM1.
  • Co-evolution between microbial adhesins and mammalian cell receptors likely contributes to the limited host range of these pathogens.