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• W2023160761 startingPage "14851" @default.
• W2023160761 abstract "Neisseria gonorrhoeae (GC) or Escherichia coli expressing phase-variable opacity (Opa) protein (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 ) 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. 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." @default.
• W2023160761 created "2016-06-24" @default.
• W2023160761 creator A5000815195 @default.
• W2023160761 creator A5015996720 @default.
• W2023160761 date "1996-12-10" @default.
• W2023160761 modified "2023-09-23" @default.
• W2023160761 title "CGM1a antigen of neutrophils, a receptor of gonococcal opacity proteins" @default.
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• W2023160761 doi "https://doi.org/10.1073/pnas.93.25.14851" @default.
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