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Role of Arg-Gingipain A in Virulence of Porphyromonas gingivalis

机译：Arg-Gingipain A在牙龈卟啉单胞菌毒力中的作用

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In order to access the role of the Porphyromonas gingivalis Arg-gingipain proteases in the virulence of this organism, a mutant defective in the rgpA gene was constructed in strain 381. This mutant, MT10, displayed only 40% of the Arg-specific cysteine protease activity of the wild-type strain. In addition, MT10, as well as the recently characterized protease mutant G-102, which is defective in the rgpB gene, displayed reduced self-aggregation, hemagglutination, and the ability to bind to immobilized type I collagen compared to levels of the wild-type parent. However, unlike mutant G-102, the rgpA mutant displayed increased binding to epithelial cells relative to that of the parental organism. Mutant MT10 also did not express detectable levels of the FimA protein as assessed by both Western and Northern blotting or fimbriae visible by electron microscopy of the cells. Furthermore, the ability of MT10 to degrade rat tail collagen fibers when it was cultured at 37°C was markedly attenuated compared to that of strain 381. These results suggest that Arg-gingipain A may play a significant role in the pathogenicity of P. gingivalis by altering the colonization and toxic properties of the organism.
机译：为了获得牙龈卟啉单胞菌 Arg-齿龈蛋白酶在该生物体毒力中的作用，在菌株381中构建了一个 rgpA 基因缺陷的突变体。 MT10仅显示野生型菌株的Arg特异性半胱氨酸蛋白酶活性的40％。此外，MT10以及最近鉴定的蛋白酶突变体G-102（其在 rgpB 基因中存在缺陷）显示出降低的自聚集，血凝和结合固定的I型胶原蛋白的能力与野生型亲本的水平相比。然而，与突变体G-102不同，相对于亲本生物体， rgpA 突变体显示出与上皮细胞的结合增加。通过Western和Northern印迹或通过细胞的电子显微镜可见的菌毛，MT10突变体也未表达FimA蛋白的可检测水平。此外，与菌株381相比，MT10在37°C下培养时降解大鼠尾部胶原纤维的能力明显减弱。这些结果表明，Arg-gingipain A可能在的致病性中起重要作用。 P.改变生物体的定殖和毒性，从而清除牙龈炎。

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