Bacteroides gingivalis and Bacteroides intermedius recognize different sites on human fibrinogen.
Bacteroides gingivalis and Bacteroides intermedius recognize different sites on human fibrinogen.
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牙龈拟杆菌和中间拟杆菌识别人纤维蛋白原上的不同位点。
DOI：
10.1128/jb.172.2.716-726.1990
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发表时间：
1990
影响因子：
3.2
通讯作者：
Hook,M
中科院分区：
文献类型：
--
作者：
Lantz,MS;Allen,RD;Bounelis,P;Switalski,LM;Hook,M
牙龈类杆菌和中间类杆菌与人类牙周病的病因学密切相关。这些微生物能够结合和降解人类纤维蛋白原，这些相互作用可能在牙周病的发病机制中发挥作用。在试图绘制纤维蛋白原分子上的细菌结合部位图的过程中，我们发现牙龈假单胞菌和中间芽孢杆菌分别识别纤维蛋白原分子上距离较远和不同的位置。分离的还原的和烷基化的α-、β-和伽马纤维蛋白原链以浓度依赖的方式抑制125I-纤维蛋白原与这两种类杆菌的结合。然而，纤溶酶片段D和一定程度上的片段E对125I-纤维蛋白原与中间芽孢杆菌的结合有浓度依赖性的抑制作用，但不影响125I-纤维蛋白原与牙龈假单胞菌的结合。在与细菌结合的特异性和可逆性方面，比较了放射性标记的纤维蛋白原链和片段与125I-纤维蛋白原的结合。根据这些标准，伽马链在对牙龈假单胞菌菌株的行为上与天然纤维蛋白原分子最相似，而片段D在对中间芽孢杆菌菌株的行为上与纤维蛋白原最相似。含D片段的抗人纤维蛋白原免疫球蛋白G(Ig G)可显著抑制125I-纤维蛋白原与牙龈假单胞菌的结合，但不影响抗体抑制125I-纤维蛋白原与牙龈假单胞菌的结合。纯化的葡萄球菌纤维蛋白原结合蛋白可阻断~(125)I-纤维蛋白原与中间芽孢杆菌的结合，但不能与牙龈假单胞菌结合。
Bacteroides (Porphyromonas) gingivalis and Bacteroides (Porphyromonas) intermedius have been implicated in the etiology of human periodontal diseases. These organisms are able to bind and degrade human fibrinogen, and these interactions may play a role in the pathogenesis of periodontal disease. In attempts to map the bacterial binding sites along the fibrinogen molecule, we have found that strains of B. gingivalis and B. intermedius, respectively, recognize spatially distant and distinct sites on the fibrinogen molecule. Isolated reduced and alkylated alpha-, beta-, and gamma-fibrinogen chains inhibited binding of 125I-fibrinogen to both Bacteroides species in a concentration-dependent manner. Plasmin fragments D and to some extent fragment E, however, produced a concentration-dependent inhibition of 125I-fibrinogen binding to B. intermedius strains but did not affect binding of 125I-fibrinogen to B. gingivalis strains. Radiolabeled fibrinogen chains and fragments were compared with 125I-fibrinogen with respect to specificity and reversibility of binding to bacteria. According to these criteria, gamma chain most closely resembled the native fibrinogen molecule in behavior toward B. gingivalis strains and fragments D most closely resembled fibrinogen in behavior toward B. intermedius strains. The ability of anti-human fibrinogen immunoglobulin G (IgG) to inhibit binding of 125I-fibrinogen to B. intermedius strains was greatly reduced by absorbing the IgG with fragments D. Absorbing the IgG with fragments D had no effect on the ability of the antibody to inhibit binding of 125I-fibrinogen to B. gingivalis strains. A purified staphylococcal fibrinogen-binding protein blocked binding of 125I-fibrinogen to B. intermedius strains but not to B. gingivalis strains.