Abstract
One of the more conspicuous structural features that punctuate the outer cell surface of certain bacterial Gram-positive genera and species is the sortase-dependent pilus. As these adhesive and variable-length protrusions jut outward from the cell, they provide a physically expedient and useful means for the initial contact between a bacterium and its ecological milieu. The sortase-dependent pilus displays an elongated macromolecular architecture consisting of two to three types of monomeric protein subunits (pilins), each with their own specific function and location, and that are joined together covalently by the transpeptidyl activity of a pilus-specific C-type sortase enzyme. Sortase-dependent pili were first detected among the Gram-positive pathogens and subsequently categorized as an essential virulence factor for host colonization and tissue invasion by these harmful bacteria. However, the sortase-dependent pilus was rebranded as also a niche-adaptation factor after it was revealed that "friendly" Gram-positive commensals exhibit the same kind of pilus structures, which includes two contrasting gut-adapted species from the Lactobacillus genus, allochthonous Lactobacillus rhamnosus and autochthonous Lactobacillus ruminis. This review will highlight and discuss what has been learned from the latest research carried out and published on these lactobacillar pilus types.
Original language | English |
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Article number | 1551 |
Number of pages | 30 |
Journal | International Journal of Molecular Sciences |
Volume | 18 |
Issue number | 7 |
DOIs | |
Publication status | Published - Jul 2017 |
MoE publication type | A2 Review article, Literature review, Systematic review |
Keywords
- sortase-dependent pili
- pilin
- Gram-positive
- Lactobacillus rhamnosus
- Lactobacillus ruminis
- commensal
- niche-adaptation factor
- adhesion
- GRAM-POSITIVE BACTERIA
- RAY-DIFFRACTION ANALYSIS
- BACKBONE-PILIN SUBUNIT
- RHAMNOSUS GG PILI
- STREPTOCOCCUS-PYOGENES
- CORYNEBACTERIUM-DIPHTHERIAE
- FUNCTIONAL-ANALYSIS
- PNEUMOCOCCAL PILUS
- CRYSTALLOGRAPHIC ANALYSIS
- STABILIZING ISOPEPTIDE