2011年12月23日 · Here we present two new Type IV pilin crystal structures: the full-length FimA pilin from D. nodosus (DnFimA) and an ultrahigh resolution F. tularensis PilE (FtPilE) structure. Both pilins belong to the Type IVa pilin subclass, members of which are present on a broad range of bacterial pathogens, including N. gonorrhoeae and P. aeruginosa.

2015年7月14日 · Pilins or fimbrilins are a class of proteins found in bacterial surface pilus, a hair-like surface appendage. Both the Gram-negative and -positive bacteria produce pilins to assemble pili on their cell-surface for different purposes including adherence, twitching motility, conjugation, immunomodulation, biofilm formation, and electron transfer.

Pili, also known as fimbriae, are proteinaceous, filamentous polymeric organelles expressed on the surface of bacteria. They range from a few fractions of a micrometer to > 20 μm in length and vary from < 2 to 11 nm in diameter. Their functions include mediation of cell-to-cell interactions, motility, and DNA uptake.

Pilin refers to a class of fibrous proteins that are found in pilus structures in bacteria. These structures can be used for the exchange of genetic material, or as a cell adhesion mechanism. Although not all bacteria have pili or fimbriae, bacterial pathogens often use their fimbriae to attach to host cells.

Each pilin subunit has three helices termed: ɑ1, ɑ2, and ɑ3, respectively, from the N- to the C-termini (Supplementary Fig. 1a). The loop connecting ɑ2 and ɑ3 is located in the inner lumen of the pilus and interacts with a phospholipid, while the N- and C-termini of the pilin face outside, potentially interacting with ssRNA phages.

Here, we will review the structure and the function of the minor pilins from type IV pili. Keywords: Type IV pili, Minor pilins, Adhesion, Type II secretion system. Motility and pathogenicity of various bacteria are strongly dependent on proteinaceous appendages called …

2019年11月15日 · Type IV pilus-like systems are protein complexes that polymerize pilin fibres. They are critical for virulence in many bacterial pathogens. Pilin polymerization and depolymerization are powered...

In this review, we focus on recent advances in one of the longest-studied Gram-negative pilus systems, the chaperone/usher assembled pili, along with the newcomer to the field, the sortase-assembled pili of Gram-positive bacteria. In both systems, a wealth of new structural and molecular details has emerged recently.

Type IV pilins are small (∼7 to 20 kDa) structural proteins with a conserved, hydrophobic α-helical N terminus that is both a transmembrane (TM) domain and a protein-protein interaction domain. In general, the proteins function through their reversible polymerization into helical fibers by dedicated assembly/disassembly systems.

Both the Gram-negative and -positive bacteria produce pilins to assemble pili on their cell-surface for different purposes including adherence, twitching motility, conjugation, immunomodulation, biofilm formation, and electron transfer. Immunogenic properties of the pilins make them attractive vaccine candidates.