CGM1a Antigen of Neutrophils, a Receptor of Gonococcal Opacity Proteins

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 93; no. 25; pp. 14851 - 14856
• Main Authors: Chen, Tie, Gotschlich, Emil C.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 10-12-1996; National Acad Sciences; National Academy of Sciences; The National Academy of Sciences of the USA
• Subjects: Antigens; Antigens, Bacterial - metabolism; Bacteria; Bacterial Adhesion; Bacterial Outer Membrane Proteins - metabolism; Biological Sciences; Carcinoembryonic Antigen - metabolism; Cell Adhesion Molecules - metabolism; Cell lines; Epithelial cells; Escherichia coli; HeLa Cells; Hematopoietic stem cells; Heparin; Humans; Neisseria gonorrhoeae; Neutrophils; Neutrophils - metabolism; Opal; Receptors
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.93.25.14851

Neisseria gonorrhoeae (GC) or Escherichia coli expressing phase-variable opacity (Opa) protein (Opa+GC or Opa+GC or Opa+E. coli) adhere to human neutrophils and stimulate phagocytosis, whereas their counterparts not expressing Opa protein (Opa-GC or Opa-E. coli) E. coli) adhere to human neutrophils and stimulate phagocytosis, whereas their counterparts not expressing Opa protein Opa+GC or E. coli do not adhere to human lymphocytes and promyelocytic cell lines such as HL-60 cells. The adherence of Opa+do not. Opa+GC or E. coli do not adhere to human lymphocytes and promyelocytic cell lines such as HL-60 cells. The adherence of Opa+GC to the neutrophils can be enhanced dramatically if the neutrophils are preactivated. These data suggest that the components binding the Opa+bacteria might exist in the granules. CGM1a antigen, a transmembrane protein of the carcinoembryonic antigen family, is exclusively expressed in the granulocytic lineage. The predicted molecular weight of CGM1a is ≈ 30 kDa. 30 kDa. We observed specific binding of OpaI+E. coli to a 30-kDa band of polymorphonuclear leukocytes lysates. To prove the hypothesis that the 30-kDa CGM1a antigen from neutrophils was the receptor of Opa+bacteria, we showed that a HeLa cell line expressing human CGM1a antigen (HeLa-CGM1a) bound Opa+E. coli and subsequently engulfed the bacteria. Monoclonal antibodies (COL-1) against CGM1 blocked the interaction between Opa+E. coli and HeLa-CGM1a. These results demonstrate that HeLa cells when expressing the CGM1a antigens bind and internalize OpaI+bacteria.