Müller A, Günther D, Düx F, Naumann M, Meyer T F, Rudel T
Max-Planck-Institut für Infektionsbiologie, Abteilung Molekulare Biologie, Monbijoustrasse 2, 10117 Berlin, Germany.
EMBO J. 1999 Jan 15;18(2):339-52. doi: 10.1093/emboj/18.2.339.
The porin (PorB) of Neisseria gonorrhoeae is an intriguing bacterial factor owing to its ability to translocate from the outer bacterial membrane into host cell membranes where it modulates the infection process. Here we report on the induction of programmed cell death after prolonged infection of epithelial cells with pathogenic Neisseria species. The underlying mechanism we propose includes translocation of the porin, a transient increase in cytosolic Ca2+ and subsequent activation of the Ca2+ dependent protease calpain as well as proteases of the caspase family. Blocking the porin channel by ATP eliminates the Ca2+ signal and also abolishes its pro-apoptotic function. The neisserial porins share structural and functional homologies with the mitochondrial voltage-dependent anion channels (VDAC). The neisserial porin may be an analogue or precursor of the ancient permeability transition pore, the putative central regulator of apoptosis.
淋病奈瑟菌的孔蛋白（PorB）是一种引人关注的细菌因子，因为它能够从细菌外膜转运至宿主细胞膜，在那里调节感染过程。在此我们报告致病性奈瑟菌属长时间感染上皮细胞后程序性细胞死亡的诱导情况。我们提出的潜在机制包括孔蛋白的转运、胞质Ca2+的短暂增加以及随后Ca2+依赖性蛋白酶钙蛋白酶和半胱天冬酶家族蛋白酶的激活。ATP阻断孔蛋白通道可消除Ca2+信号，并消除其促凋亡功能。奈瑟菌孔蛋白与线粒体电压依赖性阴离子通道（VDAC）具有结构和功能同源性。奈瑟菌孔蛋白可能是古老的通透性转换孔的类似物或前体，而通透性转换孔被认为是细胞凋亡的主要调节因子。
