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A pilus (Latin for 'hair'; pl.: pili) is a hair-like cell-surface appendage found on many bacteria and archaea. [1] The terms pilus and fimbria (Latin for 'fringe'; plural: fimbriae ) can be used interchangeably, although some researchers reserve the term pilus for the appendage required for bacterial conjugation .
P fimbriae are large, linear structures projecting from the surface of the bacterial cell. With lengths of 1-2um, the pili can be larger than the diameter of the bacteria itself. [4] The main body of the fimbriae is composed of approx. 1000 copies of the major fimbrial subunit protein PapA, forming a helical rod. [5]
The Pilus subunits polymerise via a non-covalent interaction to form the mature pilus which consists of an adhesive tip, helical body and an usher bound base. The P-pilus (pap) system is one of the best characterised and is shown below. [2] A schematic overview of the pap chaperone-usher system showing all subunits and their organisation.
Pili are similar in structure to fimbriae but are much longer and present on the bacterial cell in low numbers. Pili are involved in the process of bacterial conjugation where they are called conjugation pili or "sex pili". Type IV pili (non-sex pili) also aid bacteria in gripping surfaces.
A fimbria (plural fimbriae also known as a pilus, plural pili) is a short, thin, hair-like filament found on the surface of bacteria. Fimbriae are formed of a protein called pilin and are responsible for the attachment of bacteria to specific receptors on human cells (cell adhesion).
Pili (sing. pilus) are cellular appendages, slightly larger than fimbriae, that can transfer genetic material between bacterial cells in a process called conjugation where they are called conjugation pili or sex pili (see bacterial genetics, below). [87] They can also generate movement where they are called type IV pili. [88]
The fimbrial usher protein is involved in biogenesis of the pilus in Gram-negative bacteria.The biogenesis of some fimbriae (or pili) requires a two-component assembly and transport system which is composed of a periplasmic chaperone and a pore-forming outer membrane protein which has been termed a molecular 'usher'; this is the chaperone-usher pathway.
The Saf pilin N-terminal extension protein domain helps the pili to form, via a complex mechanism named the chaperone/usher pathway. It is found in all c-u pilins. [8] This protein domain is very important for such bacteria, as without pili formation, they could not infect the host. Saf is a Salmonella operon containing a c-u pilus system. [8]