Chen T, Gotschlich E C
Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, NY 10021, USA.
Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14851-6. doi: 10.1073/pnas.93.25.14851.
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 approximately 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.
表达相可变不透明蛋白（Opa）的淋病奈瑟菌（GC）或大肠杆菌（Opa + GC或Opa +大肠杆菌）可黏附于人类中性粒细胞并刺激吞噬作用，而不表达Opa蛋白的对应菌（Opa - GC或Opa -大肠杆菌）则不能。Opa + GC或大肠杆菌不黏附于人类淋巴细胞和早幼粒细胞系，如HL - 60细胞。如果中性粒细胞被预激活，Opa + GC对中性粒细胞的黏附会显著增强。这些数据表明，结合Opa +细菌的成分可能存在于颗粒中。CGM1a抗原是癌胚抗原家族的一种跨膜蛋白，仅在粒细胞系中表达。CGM1a的预测分子量约为30 kDa。我们观察到OpaI +大肠杆菌与多形核白细胞裂解物的一条30 kDa条带存在特异性结合。为了证明中性粒细胞中30 kDa的CGM1a抗原是Opa +细菌受体这一假设，我们发现表达人CGM1a抗原的HeLa细胞系（HeLa - CGM1a）能结合Opa +大肠杆菌并随后吞噬细菌。针对CGM1的单克隆抗体（COL - 1）可阻断Opa +大肠杆菌与HeLa - CGM1a之间的相互作用。这些结果表明，HeLa细胞在表达CGM1a抗原时能结合并内化OpaI +细菌。
