Pili in Gram-negative and Gram-positive bacteria — structure, assembly and their role in disease

  title={Pili in Gram-negative and Gram-positive bacteria — structure, assembly and their role in disease},
  author={Thomas Proft and Edward N. Baker},
  journal={Cellular and Molecular Life Sciences},
  • T. Proft, E. Baker
  • Published 1 February 2009
  • Biology
  • Cellular and Molecular Life Sciences
Abstract.Many bacterial species possess long filamentous structures known as pili or fimbriae extending from their surfaces. Despite the diversity in pilus structure and biogenesis, pili in Gram-negative bacteria are typically formed by non-covalent homopolymerization of major pilus subunit proteins (pilins), which generates the pilus shaft. Additional pilins may be added to the fiber and often function as host cell adhesins. Some pili are also involved in biofilm formation, phage transduction… 
Bacterial Pili and Fimbriae
The current knowledge of assembly pathways, structure and function of pili in Gram-negative and Gram-positive pathogens, including pili that can activate or suppress immune cells, is reviewed.
The Biosynthesis and Structures of Bacterial Pili.
The diversity in structure, biogenesis and function of the different pilus systems found in Gram-positive and Gram-negative bacteria are described, and their potential as anti-microbial targets are reviewed.
Pilins in gram‐positive bacteria: A structural perspective
This review summarizes and discusses the current structural knowledge of pilins in Gram‐positive bacteria with emphasis on those pilins which are sortase substrates.
Pilus biogenesis of Gram‐positive bacteria: Roles of sortases and implications for assembly
Structural and functional data indicate that there are at least two groups of Gram‐positive pili, which require either the Class C sortase or Class B sortase in conjunction with LepA/SipA protein for major pilin polymerization, which suggests two distinct modes of sortase‐mediated pilus biogenesis in Gram‐ positive bacteria.
Relevance of pili in pathogenic streptococci pathogenesis and vaccine development.
The characterization of pili is a hot scientific issue that is believed to lead to important future developments in understanding bacterial dynamics that lead to successful occupation of microbial niches.
Cell Wall Structure and Pathogenicity
This chapter presents an overview rather than a comprehensive paper regarding the great variety of cell envelope components and pathogenicity.
Structural biology of gram‐positive bacterial adhesins
The recent focus is on the newly discovered pili of Gram‐positive bacteria, and this review highlights the advances in understanding of the individual pilus constituents and their associations and stresses the similarities between the individual Pilins and surface proteins.


Pili in Gram-positive pathogens
Evidence from studies of pili in the three principal streptococcal pathogens of humans indicates that the genes that encode the pilin subunits and the enzymes that are required for the assembly of these subunits into pili have been acquired en bloc by the horizontal transfer of a pathogenicity island.
Assembly of pili on the surface of Corynebacterium diphtheriae
It is shown here that pili of Corynebacterium diphtheriae are composed of three pilin subunits, SpaA, SpaB and SpaC, which suggest that the pilus fibres may be anchored to the cell wall envelope.
Structure-function and biogenesis of the type IV pili.
Regulation of synthesis and posttranslational modification and assembly of type IV pili serves as a useful model for a number of diverse biological processes in the bacterial cell.
Type IV pili: paradoxes in form and function.
PilC of pathogenic Neisseria is associated with the bacterial cell surface
The complete nucleotide sequence of pilC1 and pilC2 of N. meningitidis was determined and it was demonstrated that PilC is composed of both conserved and variable regions and is associated with the bacterial cell surface.
Pneumococcal Pili Are Composed of Protofilaments Exposing Adhesive Clusters of Rrg A
A model emerges where the pilus RrgB backbone serves as a carrier for surface located adhesive clusters of RrgA that facilitates the interaction with the host.
New tools in an old trade: CS1 pilus morphogenesis
The proteins of CS1 pili have no significant homology to those of the well‐characterized Pap (pyelonephritis‐associated) pili and related systems, although most of the features of pilus morphogenesis are similar, and appear to be among the rare cases of convergent evolution.
Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili
This finding is the first demonstration of a specific translocation defect associated with loss of secretin function and additionally confirms the role of PilT as a conditional antagonist of stable pilus fiber formation.
Structural polymorphism of bacterial adhesion pili
The three-dimensional reconstruction indicates that pili are formed by the tight winding of a much thinner structure, and a structural transition allows the pilus to unravel without depolymerizing, producing a thin, extended structure five times the length of the original pilus.