Hauck C R, Meyer T F
Max-Planck-Institut für Biologie, Abteilung Infektionsbiologie, Tübingen, Germany.
FEBS Lett. 1997 Mar 17;405(1):86-90. doi: 10.1016/s0014-5793(97)00163-4.
Lysosomal/phagosomal membranes of mammalian cells are coated by highly conserved glycoproteins (lamps) that are thought to protect the membranes from degradation. Interestingly, we identified an amino acid sequence in human lamp-1 characteristic of a cleavage site for the Neisseria gonorrhoeae IgA1 protease. Furthermore, gonococci are detected in h-lamp-1-positive vacuoles after their uptake by professional phagocytes and epithelial cells. Here we demonstrate cleavage of glycosylated h-lamp-1 by the secreted gonococcal IgA1 protease. The cleavage was observed with h-lamp-1 purified from epithelial cells but not from professional phagocytes. The biological role of lamp-1 cleavage by the gonococcal protease is discussed.
哺乳动物细胞的溶酶体/吞噬体膜由高度保守的糖蛋白（LAMP）包被，这些糖蛋白被认为可保护膜不被降解。有趣的是，我们在人LAMP-1中鉴定出一段氨基酸序列，它是淋病奈瑟菌IgA1蛋白酶切割位点的特征序列。此外，专业吞噬细胞和上皮细胞摄取淋球菌后，在h-LAMP-1阳性的液泡中可检测到淋球菌。在此，我们证明了分泌型淋球菌IgA1蛋白酶可切割糖基化的h-LAMP-1。从上皮细胞而非专业吞噬细胞中纯化得到的h-LAMP-1可观察到这种切割。本文还讨论了淋球菌蛋白酶切割LAMP-1的生物学作用。
