By M.A. Barocchi, J.L. Telford
Bacterial pili play very important roles as environmental sensors, in host colonization and in biofilm formation, permitting micro organism to engage with the surroundings, with surfaces and with different micro organism and host cells. so much micro organism, either Gram confident and Gram destructive, and just about all bacterial pathogens, are piliated. This ebook discusses the synthesis, constitution, evolution, functionality and function in pathogenesis of those advanced constructions, and their foundation for vaccine improvement and therapeutics for Streptococcus pathogens. it's a useful source for researchers and scholars of scientific microbiology.
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Extra resources for Bacterial Pili: Structure, Synthesis and Role in Disease
Horiuchi, T. and Komano, T. (1998) Mutational analysis of plasmid R64 thin pilus prepilin: the entire prepilin sequence is required for processing by type IV prepilin peptidase. Journal of Bacteriology 180, 4613–4620. Ippen-Ihler, K. and Maneewannakul, S. (1991) Conjugation among enteric bacteria: mating systems dependent on expression of pili. In: Dworkin, M. ) Microbial Cell–Cell Interactions. ASM, Washington, DC, pp. 35–69. , Waksman, G. J. (2009) Agrobacterium VirB10 domain requirements for type IV secretion and Conjugative Pili T pilus biogenesis.
Gram-negative bacteria elaborate a type IV secretion system (T4SS) composed of a mating channel and conjugative pilus. F-pili extend and retract to bring potential recipient cells into direct cell-to-cell contact, whereas P-pili are released from the cell surface where they form a hydrophobic mesh promoting aggregation of donor and potential recipient cells. Following mating junction formation, the DNA transfer and replication (Dtr) processing factors nick the DNA strand destined for transfer (T-strand) and the nicking enzyme, termed a relaxase, pilots the T-strand into the recipient cell.
2001; Schroder and Lanka, 2005). P-pili are abundantly present in the extracellular milieu, often as bundles, and are rarely found associated with cells (Fig. 2B). , 2001). , 2002). Recently, accessibility studies of Cys residues introduced along the length of the A. tumefaciens VirB2 pilin provided evidence that VirB2At adopts a similar overall architecture as TraAF in the assembled pilus (Silverman, 1997; Kerr and Christie, 2010). For example, the hydrophobic domains and intervening hydrophilic loops of VirB2At are buried in the pilus, the former probably forming packing interfaces between adjacent pilins or between pilins in adjacent helix stacks and the latter lining the inner lumen.