CD66介导的淋病奈瑟菌Opa52吞噬作用需要一种Src样酪氨酸激酶和Rac1依赖性信号通路。
CD66-mediated phagocytosis of Opa52 Neisseria gonorrhoeae requires a Src-like tyrosine kinase- and Rac1-dependent signalling pathway.
作者信息
Hauck C R, Meyer T F, Lang F, Gulbins E
机构信息
Max-Planck-Institut für Biologie, Abteilung Infektionsbiologie, Tübingen, Germany.
出版信息
EMBO J. 1998 Jan 15;17(2):443-54. doi: 10.1093/emboj/17.2.443.
Abstract
The interaction of Neisseria gonorrhoeae with human phagocytes is a hallmark of gonococcal infections. Recently, CD66 molecules have been characterized as receptors for Opa52-expressing gonococci on human neutrophils. Here we show that Opa52-expressing gonococci or Escherichia coli or F(ab) fragments directed against CD66, respectively, activate a signalling cascade from CD66 via Src-like protein tyrosine kinases, Rac1 and PAK to Jun-N-terminal kinase. The induced signal is distinct from Fcgamma-receptor-mediated signalling and is specific for Opa52, since piliated Opa- gonococci, commensal Neisseria cinerea or E.coli do not stimulate this signalling pathway. Inhibition of Src-like kinases or Rac1 prevents the uptake of Opa52 bacteria, demonstrating the crucial role of this signalling cascade for the opsonin-independent, Opa52/CD66-mediated phagocytosis of pathogenic Neisseria.
摘要
淋病奈瑟菌与人类吞噬细胞的相互作用是淋球菌感染的一个标志。最近，CD66分子已被鉴定为人类中性粒细胞上表达Opa52的淋球菌的受体。在此我们表明，表达Opa52的淋球菌或大肠杆菌或分别针对CD66的F(ab)片段，通过Src样蛋白酪氨酸激酶、Rac1和PAK从CD66激活一个信号级联反应至Jun-氨基末端激酶。诱导的信号不同于Fcγ受体介导的信号，并且对Opa52具有特异性，因为有菌毛的Opa-淋球菌、共生的灰色奈瑟菌或大肠杆菌不会刺激这条信号通路。抑制Src样激酶或Rac1可阻止Opa52细菌的摄取，证明了这条信号级联反应对致病性奈瑟菌不依赖调理素、由Opa52/CD66介导的吞噬作用的关键作用。
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