The pilus is an extracellular structural part that can be detected in some () isolates (type I pili are found in approximately 30% of strains, while type II pili are found in approximately 20%). It is anchored to the cell wall by LPXTG-like motifs on the peptidoglycan. Two kinds of pili have been discovered, namely, pilus-1 and pilus-2. The former is encoded by pilus islet 1 (PI-1) and is a polymer formed by the protein subunits RrgA, RrgB and RrgC. The latter is encoded by pilus islet 2 (PI-2) and is a polymer composed mainly of the structural protein PitB. Although pili are not necessary for the survival of , they serve as the structural basis and as virulence factors that mediate the adhesion of bacteria to host cells and play a direct role in promoting the adhesion, colonization and pathogenesis of . In addition, as candidate antigens for protein vaccines, pili have promising potential for use in vaccines with combined immunization strategies. Given the current understanding of the pili of regarding the genes, proteins, structure, biological function and epidemiological relationship with serotypes, combined with the immunoprotective efficacy of pilins as protein candidates for vaccines, we here systematically describe the research status and prospects of pili and provide new ideas for subsequent vaccine research and development.
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http://dx.doi.org/10.3389/fcimb.2023.1270848 | DOI Listing |
J Bacteriol
January 2025
Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Canada.
Unlabelled: Type IV pili (T4P) are important virulence factors that allow bacteria to adhere to and rapidly colonize their hosts. T4P are primarily composed of major pilins that undergo cycles of extension and retraction and minor pilins that initiate pilus assembly. Bacteriophages use T4P as receptors and exploit pilus dynamics to infect their hosts.
View Article and Find Full Text PDFNat Commun
January 2025
National Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, TEDA Institute of Biological Sciences and Biotechnology, Nankai University, Tianjin, China.
Uropathogenic Escherichia coli (UPEC) is a major cause of urinary tract infections (UTIs). Invasion into bladder epithelial cells (BECs) on the bladder luminal surface via type 1 fimbria is the first critical step in UPEC infection. Although type 1 fimbria expression increases during UPEC invasion of BECs, the underlying regulatory mechanisms remain poorly understood.
View Article and Find Full Text PDFJ Vet Res
December 2024
Equipe de Recherche sur les Relations Matrice Extracellulaire-Cellule (ERRMECe) Laboratory, Site de St-Martin, CY Cergy Paris University, 95302 Cergy-Pontoise, France.
Introduction: is the most common uropathogen in humans, dogs and cats. Dietary consumption of cranberry () is known to be associated with a reduction in uropathogenic (UPEC) adhesion to human and canine urinary epithelial cell lines, but this has not been shown in cats.
Material And Methods: Six neutered domestic cats, one male and five females, were randomly fed three diets successively, one containing 0.
Viruses
November 2024
Key Laboratory of Tropical Marine Bio-Resources and Ecology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 510000, China.
is a major global threat to human health, and phage therapy has emerged as a promising strategy for treating infections caused by multidrug-resistant pathogens. In this study, we isolated and characterized a lytic phage, PaTJ, from wastewater. PaTJ belongs to the phage family , and is featured by short latency (30 min) and large burst size (10 PFU per infected cell).
View Article and Find Full Text PDFbioRxiv
December 2024
Department of Biochemistry, University of Washington, Seattle, WA.
A critical step in infections is the attachment of many microorganisms to host cells using lectins that bind surface glycans, making lectins promising antimicrobial targets. Upon binding mannosylated glycans, FimH, the most studied lectin adhesin of type 1 fimbriae in , undergoes an allosteric transition from an inactive to an active conformation that can act as a catch-bond. Monoclonal antibodies that alter FimH glycan binding in various ways are available, but the mechanisms of these antibodies remain unclear.
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