Shafer W M, Onunka V C, Martin L E
Infect Immun. 1986 Oct;54(1):184-8. doi: 10.1128/iai.54.1.184-188.1986.
We have shown that lysosomal cathepsin G, prepared from acid extracts of granules derived from human polymorphonuclear granulocytes, exhibits potent in vitro antimicrobial activity against Neisseria gonorrhoeae. An isolated isozyme of cathepsin G was found to exhibit antigonococcal activity by a nonenzymatic mechanism in a time-dependent manner. Moreover, we observed that the antigonococcal activity of cathepsin G was relatively independent of pH and evident over a pH range resembling that invoked for maturing phagolysosomes. Using a number of isogenic strains, we determined that certain mutations known to alter cell envelope structure rendered gonococci more susceptible to cathepsin G. This suggests that the susceptibility of gonococci to cathepsin G, and possibly other antimicrobial proteins derived from PMN granules, is genetically determined and possibly related to the structure of the gonococcal cell envelope.
我们已经证明，从人类多形核粒细胞颗粒的酸性提取物中制备的溶酶体组织蛋白酶G，对淋病奈瑟菌具有强大的体外抗菌活性。发现一种分离的组织蛋白酶G同工酶通过非酶机制以时间依赖性方式表现出抗淋球菌活性。此外，我们观察到组织蛋白酶G的抗淋球菌活性相对独立于pH值，并且在类似于吞噬溶酶体成熟时的pH范围内很明显。使用许多同基因菌株，我们确定某些已知会改变细胞包膜结构的突变使淋球菌对组织蛋白酶G更敏感。这表明淋球菌对组织蛋白酶G以及可能来自PMN颗粒的其他抗菌蛋白的敏感性是由基因决定的，并且可能与淋球菌细胞包膜的结构有关。
