Hemagglutinin/Adhesin domains of Porphyromonas gingivalis play key roles in coaggregation with Treponema denticola
Hemagglutinin/Adhesin domains of Porphyromonas gingivalis play key roles in coaggregation with Treponema denticola
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DOI：
10.1111/j.1574-695x.2010.00737.x
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发表时间：
2010-12-01
影响因子：
--
通讯作者：
Okuda, Katsuji
中科院分区：
文献类型：
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作者：
Ito, Rieko;Ishihara, Kazuyuki;Okuda, Katsuji
牙龈卟啉单胞菌和齿垢密螺旋体是牙周病的主要致病菌。微生物之间的共聚集在龈沟的定植和牙周病生物膜的组织中起着关键作用。我们研究了牙龈卟啉单胞菌表面配体参与共聚集的情况。缺失Arg牙龈卟啉菌蛋白酶A（RgpA）、Lys牙龈卟啉菌蛋白酶（Kgp）和血凝素A（HagA）或缺失Arg牙龈卟啉菌蛋白酶B（RgpB）和Kgp的牙龈卟啉单胞菌的两个三联突变体与T的共聚集性显著降低。而与主要菌毛（FimA）缺陷型突变体的共聚集与牙龈卟啉单胞菌野生型亲本菌株相同。rgpA、kgp和hagA编码含有44kDa Hgp 44粘附素结构域的蛋白质。rgpA kgp突变体的共聚集活性显著高于rgpA kgp hagA突变体。此外，抗Hgp44免疫球蛋白G减少了牙龈卟啉单胞菌野生型和T.齿垢齿垢密螺旋体超声处理物粘附于重组Rgp结构域。表达RgpB蛋白酶的rgpA kgp hagA突变体与表达未加工的HagA蛋白的rgpA rgpB kgp突变体共培养后的共聚集与每个三重突变体与T.齿垢这些结果表明，加工的牙龈卟啉单胞菌表面Hgp44结构域是与T.齿垢
Porphyromonas gingivalis and Treponema denticola are major pathogens of periodontal disease. Coaggregation between microorganisms plays a key role in the colonization of the gingival crevice and the organization of periodontopathic biofilms. We investigated the involvement of surface ligands of P. gingivalis in coaggregation. Two triple mutants of P. gingivalis lacking Arg-gingipain A (RgpA), Lys-gingipain (Kgp) and Hemagglutinin A (HagA) or RgpA, Arg-gingipain B (RgpB) and Kgp showed significantly decreased coaggregation with T. denticola, whereas coaggregation with a major fimbriae (FimA)-deficient mutant was the same as that with the P. gingivalis wild-type parent strain. rgpA, kgp and hagA code for proteins that contain 44 kDa Hgp44 adhesin domains. The coaggregation activity of an rgpA kgp mutant was significantly higher than that of the rgpA kgp hagA mutant. Furthermore, anti-Hgp44 immunoglobulin G reduced coaggregation between P. gingivalis wild type and T. denticola. Treponema denticola sonicates adhered to recombinant Rgp domains. Coaggregation following co-culture of the rgpA kgp hagA mutant expressing the RgpB protease with the rgpA rgpB kgp mutant expressing the unprocessed HagA protein was enhanced compared with that of each triple mutant with T. denticola. These results indicate that the processed P. gingivalis surface Hgp44 domains are key adhesion factors for coaggregation with T. denticola.