木桩
菌毛
霍乱弧菌
分泌物
霍乱毒素
生物
细胞生物学
微生物学
操纵子
毒力因子
殖民地化
毒力
细菌
基因
生物化学
遗传学
大肠杆菌
作者
Hiroya Oki,Kazuki Kawahara,Minato Iimori,Yuka Imoto,Haruka Nishiumi,Takahiro Maruno,Susumu Uchiyama,Yuki Muroga,Akihiro Yoshida,Takuya Yoshida,Tadayasu Ohkubo,Shigeaki Matsuda,Tetsuya Iida,Shota Nakamura
出处
期刊:Science Advances
[American Association for the Advancement of Science (AAAS)]
日期:2022-10-14
卷期号:8 (41)
被引量:4
标识
DOI:10.1126/sciadv.abo3013
摘要
Colonization of the host intestine is the most important step in Vibrio cholerae infection. The toxin-coregulated pilus (TCP), an operon-encoded type IVb pilus (T4bP), plays a crucial role in this process, which requires an additional secreted protein, TcpF, encoded on the same TCP operon; however, its mechanisms of secretion and function remain elusive. Here, we demonstrated that TcpF interacts with the minor pilin, TcpB, of TCP and elucidated the crystal structures of TcpB alone and in complex with TcpF. The structural analyses reveal how TCP recognizes TcpF and its secretory mechanism via TcpB-dependent pilus elongation and retraction. Upon binding to TCP, TcpF forms a flower-shaped homotrimer with its flexible N terminus hooked onto the trimeric interface of TcpB. Thus, the interaction between the minor pilin and the N terminus of the secreted protein, namely, the T4bP secretion signal, is key for V. cholerae colonization and is a new potential therapeutic target.
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