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Type IV pili |
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Type IVa pili. Plays a role in adherence. ... |
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Type IV pili |
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Type IVa pili. Plays a role in adherence. ... |
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Type IV pili |
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Type IVa pili. Plays a role in adherence. ... |
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Type IV pili |
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Type IVa pili. Plays a role in adherence. ... |
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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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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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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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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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