机构：[1]Center of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.四川大学华西医院[2]Henry M. Jackson Foundation for the Advancement of Military Medicine, Bethesda, MD, United States of America.[3]Enteric Diseases Department, Infectious Diseases Directorate, Naval Medical Research Center, Silver Spring, MD, United States of America.[4]Department of Laboratory medicine, West China Hospital, Sichuan University, Chengdu, China.四川大学华西医院[5]Department of Pediatrics, Uniformed Services University of the Health Sciences, Bethesda, MD, United States of America.[6]Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, United States of America.[7]Sanofi Pasteur, Swiftwater, Pennsylvania, United States of America
Colonization factor CFA/I defines the major adhesive fimbriae of enterotoxigenic Escherichia coli and mediates bacterial attachment to host intestinal epithelial cells. The CFA/I fimbria consists of a tip-localized minor adhesive subunit, CfaE, and thousands of copies of the major subunit CfaB polymerized into an ordered helical rod. Biosynthesis of CFA/I fimbriae requires the assistance of the periplasmic chaperone CfaA and outer membrane usher CfaC. Although the CfaE subunit is proposed to initiate the assembly of CFA/I fimbriae, how it performs this function remains elusive. Here, we report the establishment of an in vitro assay for CFA/I fimbria assembly and show that stabilized CfaA-CfaB and CfaA-CfaE binary complexes together with CfaC are sufficient to drive fimbria formation. The presence of both CfaA-CfaE and CfaC accelerates fimbria formation, while the absence of either component leads to linearized CfaB polymers in vitro. We further report the crystal structure of the stabilized CfaA-CfaE complex, revealing features unique for biogenesis of Class 5 fimbriae.
基金：
This work was supported in part by the National Key Research and Development Plan(Grant 2016YFA0502700), by National Natural Science Foundation of China (Grant No. 81501787,81670008 and 81871615), by Ministry of Science and Technology of the People’s Republic of China(No.2018ZX09201018-005), and National Megaproject for Innovative Drugs (2019ZX09721001-001-001). It is partially supported by the United States Army Infectious Disease Research Program Work Unit A1207 and the Henry M. Jackson Foundation for the Advancement of Military Medicine (to M.G.P.). This research was also supported in part by the Intramural Research Program of the NIH, National Cancer Institute,Center for Cancer Research
语种：
外文
PubmedID：
中科院(CAS)分区：
出版当年[2020]版：
大类|1 区医学
小类|1 区微生物学1 区寄生虫学1 区病毒学
最新[2023]版：
大类|1 区医学
小类|1 区微生物学1 区寄生虫学1 区病毒学
第一作者：
第一作者机构：[1]Center of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
通讯作者：
推荐引用方式(GB/T 7714)：
Li-hui He,Hao Wang,Yang Liu,et al.Chaperone-tip adhesin complex is vital for synergistic activation of CFA/I fimbriae biogenesis.[J].PLoS pathogens.2020,16(10):e1008848.doi:10.1371/journal.ppat.1008848.
APA：
Li-hui He,Hao Wang,Yang Liu,Mei Kang,Tao Li...&Rui Bao.(2020).Chaperone-tip adhesin complex is vital for synergistic activation of CFA/I fimbriae biogenesis..PLoS pathogens,16,(10)
MLA：
Li-hui He,et al."Chaperone-tip adhesin complex is vital for synergistic activation of CFA/I fimbriae biogenesis.".PLoS pathogens 16..10(2020):e1008848
医学