A review on pilus assembly mechanisms in Gram-positive and Gram-negative bacteria

被引:29
作者
Shanmugasundarasamy, Tamilarasi [1 ]
Govindarajan, Deenadayalan Karaiyagowder [1 ]
Kandaswamy, Kumaravel [1 ]
机构
[1] Kumaraguru Coll Technol, Ctr Excellence Microscopy, Dept Biotechnol, Lab Genet Engn & Mol Biol, Coimbatore 641049, Tamil Nadu, India
关键词
Pilin subunits; Pili; Pili assembly; Pili termination; Bacteria;
D O I
10.1016/j.tcsw.2022.100077
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The surface of Gram-positive and Gram-negative bacteria contains long hair-like proteinaceous protrusion known as pili or fimbriae. Historically, pilin proteins were considered to play a major role in the transfer of genetic material during bacterial conjugation. Recent findings however elucidate their importance in virulence, biofilm formation, phage transduction, and motility. Therefore, it is crucial to gain mechanistic insights on the subcellular assembly of pili and the localization patterns of their subunit proteins (major and minor pilins) that aid the macromolecular pilus assembly at the bacterial surface. In this article, we review the current knowledge of pilus assembly mechanisms in a wide range of Gram-positive and Gram-negative bacteria, including subcellular localization patterns of a few pilin subunit proteins and their role in virulence and pathogenesis.
引用
收藏
页数:15
相关论文
共 143 条
  • [1] Allen W.J., Phan G., Hultgren S.J., Waksman G., Dissection of pilus tip assembly by the FimD usher monomer, J. Mol. Biol., 425, 5, pp. 958-967, (2013)
  • [2] Andersson E., Bengtsson C., Evans M., Chorell E., Sellstedt M., Lindgren A.G., Hufnagel D., Bhattacharya M., Tessier P., Wittung-Stafshede P., Almqvist F., Chapman M., Modulation of curli assembly and pellicle biofilm formation by chemical and protein chaperones, Chem. Biol., 20, 10, pp. 1245-1254, (2013)
  • [3] Baga M., Norgren M., Normark S., Biogenesis of E. coli Pap pili: PapH, a minor pilin subunit involved in cell anchoring and length modulation, Cell, 49, 2, pp. 241-251, (1987)
  • [4] Barnhart M.M., Pinkner J.S., Soto G.E., Sauer F.G., Langermann S., Waksman G., Frieden C., Hultgren S.J., PapD-like chaperones provide the missing information for folding of pilin proteins, Proc. Natl. Acad. Sci., 97, 14, pp. 7709-7714, (2000)
  • [5] Beaussart A., Baker A.E., Kuchma S.L., El-Kirat-Chatel S., O'Toole G.A., Dufrene Y.F., Nanoscale adhesion forces of Pseudomonas aeruginosa type IV pili, ACS Nano, 8, 10, pp. 10723-10733, (2014)
  • [6] Berry J.-L., Pelicic V., Exceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knives, FEMS Microbiol. Rev., 39, 1, pp. 134-154, (2015)
  • [7] Bjornham O., Nilsson H., Andersson M., Schedin S., Physical properties of the specific PapG–galabiose binding in E. coli P pili-mediated adhesion, Eur. Biophys. J., 38, 2, pp. 245-254, (2009)
  • [8] Borriello S., Davies H., Kamiya S., Reed P., Seddon S., Virulence factors of Clostridium difficile, Rev. Infect. Dis., 12, pp. S185-S191, (1990)
  • [9] Bradshaw W.J., Davies A.H., Chambers C.J., Roberts A.K., Shone C.C., Acharya K.R., Molecular features of the sortase enzyme family, FEBS J., 282, 11, pp. 2097-2114, (2015)
  • [10] Burdman S., Bahar O., Parker J.K., De La Fuente L., Involvement of type IV pili in pathogenicity of plant pathogenic bacteria, Genes, 2, 4, pp. 706-735, (2011)