Porphyromonas gingivalis (P. gingivalis) is regarded as a keystone pathogen in destructive periodontal diseases. It expresses a variety of virulence factors, amongst them fimbriae that are involved in colonization, invasion, establishment and persistence of the bacteria inside the host cells. The fimbriae also were demonstrated to affect the host immune-response mechanisms. The major fimbriae are able to bind specifically to different host cells, amongst them peripheral blood monocytes. The interaction of these cells with fimbriae induces release of cytokines such as interleukin-1 (IL-1), IL-6, and tumor necrosis factor-α (TNF-α). The aim of this study was to generate recombinant major FimA protein from P. gingivalis W83 fimbriae and to prove its biological activity. FimA of P. gingivalis W83 was amplified from chromosomal DNA, cloned in a vector and transferred into Listeria innocua. (L. innocua).The expressed protein was harvested and purified using FPLC via a His trap HP column. The identity and purity was demonstrated by gel-electrophoresis and mass-spectrometry. The biological activity was assessed by stimulation of human oral epithelial cells and peripheral blood monocytes with the protein and afterwards cytokines in the supernatants were quantified by enzyme linked immunosorbent assay (ELISA) and cytometric bead array. Recombinant FimA could successfully be generated and purified. Gel-electrophoresis and mass-spectrometry confirmed that the detected sequences are identical with FimA. Stimulation of human monocytes induced the release of high concentrations of IL-1β, IL-6, IL-10 and TNF-α by these cells. In conclusion, a recombinant FimA protein was established and its biological activity was proven. This protein may serve as a promising agent for further investigation of its role in periodontitis and possible new therapeutic approaches.

牙龈卟啉单胞菌（P. gingivalis）被认为是破坏性牙周病的主要病原体。它表达多种毒力因子，其中涉及细菌在宿主细胞内的定植、入侵、建立和持续存在的菌毛。菌毛也被证明会影响宿主的免疫反应机制。主要的菌毛能够与不同的宿主细胞特异性结合，其中包括外周血单核细胞。这些细胞与菌毛的相互作用诱导细胞因子的释放，如白细胞介素-1 (IL-1)、IL-6 和肿瘤坏死因子-α (TNF-α)。本研究的目的是从牙龈卟啉单胞菌中产生重组主要 FimA 蛋白W83 菌毛并证明其生物活性。牙龈卟啉单胞菌W83 的FimA从染色体 DNA 中扩增，克隆到载体中并转移到无害李斯特菌中。( L. innocua ) 。通过His trap HP柱使用FPLC收获和纯化表达的蛋白质。通过凝胶电泳和质谱法证明了同一性和纯度。通过用蛋白质刺激人口腔上皮细胞和外周血单核细胞来评估生物活性，然后通过酶联免疫吸附测定 (ELISA) 和细胞计数珠阵列对上清液中的细胞因子进行量化。可以成功地产生和纯化重组 FimA。凝胶电泳和质谱证实检测到的序列与FimA相同。人单核细胞的刺激诱导这些细胞释放高浓度的 IL-1β、IL-6、IL-10 和 TNF-α。综上所述，建立了重组FimA蛋白并证明了其生物学活性。