| Literature DB >> 31214993 |
Magdalena Lukaszczyk1,2, Brajabandhu Pradhan1,2, Han Remaut3,4.
Abstract
To interact with the external environments, bacteria often display long proteinaceous appendages on their cell surface, called pili or fimbriae. These non-flagellar thread-like structures are polymers composed of covalently or non-covalently interacting repeated pilin subunits. Distinct pilus classes can be identified on basis of their assembly pathways, including chaperone-usher pili, type V pili, type IV pili, curli and fap fibers, conjugative and type IV secretion pili, as well as sortase-mediated pili. Pili play versatile roles in bacterial physiology, and can be involved in adhesion and host cell invasion, DNA and protein secretion and uptake, biofilm formation, cell motility and more. Recent advances in structure determination of components involved in the various pilus systems has enabled a better molecular understanding of their mechanisms of assembly and function. In this chapter we describe the diversity in structure, biogenesis and function of the different pilus systems found in Gram-positive and Gram-negative bacteria, and review their potential as anti-microbial targets.Entities:
Keywords: Adhesion; Biofilm; Chaperone-usher; Conjugation; Curli; Fimbriae; Pili; Secretion; Sortase
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Year: 2019 PMID: 31214993 DOI: 10.1007/978-3-030-18768-2_12
Source DB: PubMed Journal: Subcell Biochem ISSN: 0306-0225