Production of chemotactic factors for neutrophils following the interaction of Bacteroides gingivalis with purified C5.
Production of chemotactic factors for neutrophils following the interaction of Bacteroides gingivalis with purified C5.
复制标题
牙龈拟杆菌与纯化的 C5 相互作用后产生中性粒细胞趋化因子。
DOI：
10.1111/j.1600-0765.1988.tb01422.x
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发表时间：
1988
影响因子：
3.5
通讯作者：
Berry,CR
中科院分区：
文献类型：
--
作者：
Schenkein,HA;Berry,CR
本研究的目的是确定B相互作用后是否产生补体衍生的趋化因子。B.牙龈炎用纯化的C5蛋白。在厌氧条件下，将牙龈炎菌株ATCC 33277与纯化的人C5孵育;通过SDS-PAGE对上清液的测定证明了C5蛋白的蛋白水解，并且功能性溶血测定证明了C5活性的失活。然后在改良的Boyden室中检测上清液对PMN的趋化活性，并通过特异性放射免疫测定法检测C5 a des Arg的存在。有人指出，增加细菌浓度产生的免疫反应性C5 a des Arg的浓度增加，并在反应混合物中观察到PMN趋化活性。相比之下，非蛋白水解病原体伴放线放线杆菌Y 4不能裂解C5或从C5产生趋化活性。C5与B.在导致最大化趋化活性产生的条件下，牙龈炎细胞上清液与山羊抗C5的IgG级分反应，趋化性被抑制;用α-C5对FMLP进行类似处理未能抑制FMLP诱导的趋化性。因此，B。牙龈炎能够通过与纯化的C5直接相互作用产生C5衍生的趋化活性。
The aim of this study was to determine whether complement‐derived chemotactic factors are produced following the interaction ofB. gingivaliswith purified C5 protein.B. gingivalisstrain ATCC 33277 was incubated with purified human C5 under anaerobic conditions; assay of the supernatants by SDS‐PAGE demonstrated proteolysis of C5 protein and functional hemolytic assay demonstrated inactivation of C5 activity. Supernatants were then tested for chemotactic activity for PMN's in the modified Boyden chamber, and for the presence of C5a des Arg by specific radioimmunoassay. It was noted that increased bacterial concentrations produced increased concentrations of immunoreactive C5a des Arg, and that PMN chemotactic activity was observed in the reaction mixtures. In contrast, the non‐proteolylic pathogenActinobacillus actinomycetemcomitansY4 failed to cleave C5 or to generate chemotactic activity from C5. When C5 was incubated withB. gingivalisunder conditions resulting in maximal generation of chemotactic activity and supernatants were reacted with IgG fractions of goat anti‐C5, chemotaxis was inhibited; similar treatment of FMLP with a‐C5 failed to inhibit FMLP‐induced chemotaxis. Therefore,B. gingivalisis capable of producing C5 derived chemotactic activity by direct interaction with purified C5.