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Ebp pili
(Endocarditis- and biofilm-associated pilus) |
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Ebp pili comprise one to three structural subunits. One major pilin, EbpC forms the fiber backbone. The remaining minor or ancillary structural subunits, EbpA at the tip and EbpB at the base of an EbpC polymer. ... |
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| GAS pili |
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The GAS pili are encoded in the variable FCT (fibronectin- and collagen-binding T-antigen) region. The C-terminal domain of Cpa, residues 286–723, mediates its adhesive properties and contains three domains: the middle domain (residues 291–372 and 590–597), the top domain (residues 390–583) and the bottom domain (residues 603–719). The middle domain and the bottom domain each adopt an Ig-like all- fold with an intramolecular isopeptide bond involving residues Lys297 and Asp595 in the middle domain and residues Lys610 and Asn715 in the bottom domain, similar to those found in other pilins. ... |
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| PI-2 |
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The type PI-2 streptococcal pilus presents in a number of invasive pneumococcal serotypes and consists of repeated units of a single protein, PitB, whose covalent association is catalyzed by cognate sortase SrtG-1 and partner protein SipA. ... |
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| rlrA islet |
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Pili are encoded by the rlrA pathogenicity islet, which carries genes for three pilin proteins (the major pilin RrgB and two minor pilins, RrgA and RrgC, RrgA is the tip adhesin) as well as three sortases. ... |
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| SpaA-type pili |
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The presence of pili has been for many years the hallmark of Gram-negative bacteria. However, in several Gram-positive microorganisms, fimbrial structures have been described. In C. diphtheriae, the pili are generated by the sortase machinery. The sortase-mediated export of pilin subunits seems to exist in other pathogenic species such as Clostridium perfringens, Actinomyces naeslundii, Streptococcus agalactiae, Streptococcus mutans, and Streptococcus pneumoniae. Sortase is a cysteine transpeptidase conserved in all Gram-positive bacterial genomes. Sortase cleaves pilin precursors at the conserved LPXTG motif between threonine and glycine and tethers the threonine carboxyl group of the precursor protein to the amino group of cell wall cross-bridges within the lipid II precursor, or to the amino group of the conserved pilin motif within the surface protein precursor. The latter reaction leads to the formation of pilus fibres on the bacterial surface. ... |
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PI-1
(Pilus island 1) |
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The genes encoding pili are located within 2 distinct loci, denoted pilus islands 1 and 2 (PI-1 and PI-2), the latter having 2 allelic variants (PI-2a and PI-2b). Each pilus island (PI) comprises 3 genes that encode structural proteins with a characteristic LPXTG anchoring motif recognised by sortase transpeptidases: backbone (Bkb) subunit (forming the polymeric shaft of the pilus), ancillary subunit 1 (An1, the functional tip), and ancillary subunit 2 (An2, the C-terminal anchor following attachment to peptidoglycan in the cell wall by sortase A). ... |
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PI-2a
(Pilus island 2a) |
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Mediating cell attachment, promoting the invasion of human endothelial cells and may facilitate paracellular translocation across the epithelial barrier. Promoting biofilm formation. ... |
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| SpaA-type pili |
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The presence of pili has been for many years the hallmark of Gram-negative bacteria. However, in several Gram-positive microorganisms, fimbrial structures have been described. In C. diphtheriae, the pili are generated by the sortase machinery. The sortase-mediated export of pilin subunits seems to exist in other pathogenic species such as Clostridium perfringens, Actinomyces naeslundii, Streptococcus agalactiae, Streptococcus mutans, and Streptococcus pneumoniae. Sortase is a cysteine transpeptidase conserved in all Gram-positive bacterial genomes. Sortase cleaves pilin precursors at the conserved LPXTG motif between threonine and glycine and tethers the threonine carboxyl group of the precursor protein to the amino group of cell wall cross-bridges within the lipid II precursor, or to the amino group of the conserved pilin motif within the surface protein precursor. The latter reaction leads to the formation of pilus fibres on the bacterial surface. ... |
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| SpaA-type pili |
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The presence of pili has been for many years the hallmark of Gram-negative bacteria. However, in several Gram-positive microorganisms, fimbrial structures have been described. In C. diphtheriae, the pili are generated by the sortase machinery. The sortase-mediated export of pilin subunits seems to exist in other pathogenic species such as Clostridium perfringens, Actinomyces naeslundii, Streptococcus agalactiae, Streptococcus mutans, and Streptococcus pneumoniae. Sortase is a cysteine transpeptidase conserved in all Gram-positive bacterial genomes. Sortase cleaves pilin precursors at the conserved LPXTG motif between threonine and glycine and tethers the threonine carboxyl group of the precursor protein to the amino group of cell wall cross-bridges within the lipid II precursor, or to the amino group of the conserved pilin motif within the surface protein precursor. The latter reaction leads to the formation of pilus fibres on the bacterial surface. ... |
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Ebp pili
(Endocarditis- and biofilm-associated pilus) |
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Ebp pili comprise one to three structural subunits. One major pilin, EbpC forms the fiber backbone. The remaining minor or ancillary structural subunits, EbpA at the tip and EbpB at the base of an EbpC polymer. ... |
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