The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase.
Type IV pili are dynamic cell surface appendages found throughout the bacteria. The ability of these structures to undergo repetitive cycles of extension and retraction underpins their crucial roles in adhesion, motility and natural competence for ...
David W Adams +4 more
doaj +5 more sources
Architecture of the type IVa pilus machine [PDF]
How the bacterial pilus works Many bacteria, including important pathogens, move by projecting grappling-hook–like extensions called type IV pili from their cell bodies. After these pili attach to other cells or objects in their environment, the bacteria retract the pili to pull themselves forward. Chang
Yi-Wei Chang +2 more
exaly +8 more sources
Functional role of the type 1 pilus rod structure in mediating host-pathogen interactions
Uropathogenic E. coli (UPEC), which cause urinary tract infections (UTI), utilize type 1 pili, a chaperone usher pathway (CUP) pilus, to cause UTI and colonize the gut.
Caitlin N Spaulding +12 more
doaj +2 more sources
Electron Transport Chain Is Biochemically Linked to Pilus Assembly Required for Polymicrobial Interactions and Biofilm Formation in the Gram-Positive Actinobacterium
The Gram-positive actinobacteria Actinomyces spp. are key colonizers in the development of oral biofilms due to the inherent ability of Actinomyces to adhere to receptor polysaccharides on the surface of oral streptococci and host cells.
Belkys C. Sanchez +4 more
doaj +4 more sources
Subinhibitory Concentrations of Trimethoprim and Sulfamethoxazole Prevent Biofilm Formation by Acinetobacter baumannii through Inhibition of Csu Pilus Expression [PDF]
Acinetobacter baumannii is emerging as a multidrug-resistant nosocomial pathogen of increasing threat to human health worldwide. Pili are important bacterial virulence factors, playing a role in attachment to host cells and biofilm formation.
Ki Hwan Moon +2 more
openalex +4 more sources
Mechanical architecture and folding of E. coli type 1 pilus domains
Uropathogenic Escherichia coli attach to tissues using pili type 1. Each pilus is composed by thousands of coiled FimA domains followed by the domains of the tip fibrillum, FimF-FimG-FimH. The domains are linked by non-covalent β-strands that must resist
Alvaro Alonso-Caballero, Alonso A +2 more
exaly +2 more sources
Contribution of pilus type 2b to invasive disease caused by a Streptococcus agalactiae ST-17 strain
Background Group B Streptococcus (GBS) is a major cause of invasive disease especially in neonates. In GBS three structurally distinct pilus polymers have been identified as important virulence factors and promising vaccine candidates.
Maddalena Lazzarin +6 more
doaj +2 more sources
Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD
Pathogenic bacteria such as Escherichia coli assemble surface structures termed pili, or fimbriae, to mediate binding to host-cell receptors1. Type 1 pili are assembled via the conserved chaperone–usher pathway2–5.
Minge Du +2 more
exaly +2 more sources
Characterization of Pilin A and Thioredoxin A Mutant Strains of Acinetobacter baumannii, From a Transposon Insertion Library, for Pili Production and Virulence‐Associated Properties [PDF]
Acinetobacter baumannii is a multi‐drug resistant Gram‐negative coccobacillus. It is responsible for high mortality among patients in the intensive care unit. Reported A.
Jadelynn Aki +11 more
doaj +2 more sources
The structure of the Tad pilus alignment complex reveals a periplasmic conduit for pilus extension [PDF]
The Tad (Tight adherence) pilus is a bacterial appendage implicated in virulence, cell-cell aggregation, and biofilm formation. Despite its homology to the well-characterised Type IV pilus, the structure and assembly mechanism of the Tad pilus are poorly
Sasha L. Evans +8 more
doaj +2 more sources

