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Novel Molecular Insights about Lactobacillar Sortase-Dependent Piliation.
- Source :
-
International journal of molecular sciences [Int J Mol Sci] 2017 Jul 18; Vol. 18 (7). Date of Electronic Publication: 2017 Jul 18. - Publication Year :
- 2017
-
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.<br />Competing Interests: The author declares no conflict of interest.
- Subjects :
- Aminoacyltransferases chemistry
Bacterial Proteins chemistry
Cysteine Endopeptidases chemistry
Fimbriae, Bacterial genetics
Fimbriae, Bacterial ultrastructure
Lactobacillus ultrastructure
Models, Molecular
Aminoacyltransferases metabolism
Bacterial Proteins metabolism
Cysteine Endopeptidases metabolism
Fimbriae, Bacterial metabolism
Lactobacillus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1422-0067
- Volume :
- 18
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- International journal of molecular sciences
- Publication Type :
- Academic Journal
- Accession number :
- 28718795
- Full Text :
- https://doi.org/10.3390/ijms18071551