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    Bacterial Pili (I)

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    somchais
    The pilus is an important virulent factor of many bacterial pathogens and thus is a subject of extensive study for the target of vaccination research. Here is a note on bacterial pili.

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    Bacterial Pili (I)

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    somchais
    838 views4 pages
    The pilus is an important virulent factor of many bacterial pathogens and thus is a subject of extensive study for the target of vaccination research. Here is a note on bacterial pili.

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    The pilus is an important virulent factor of many bacterial pathogens and thus is a subject of extensive study for the target of vaccination research. Here is a note on bacterial pili.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    838 views4 pages

    Bacterial Pili (I)

    Uploaded by

    somchais
    The pilus is an important virulent factor of many bacterial pathogens and thus is a subject of extensive study for the target of vaccination research. Here is a note on bacterial pili.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    of 4

    Note on Pili (Part I)

    S. Saengamnatdej, Ph.D.

    • Overview:
    • Pilus shaft (or fimbrial rod) : contains hundreds (or thousands) of protein
    subunits (called pilin, 15-25 kDa).
    • Important virulence factors (in UT, GI, genital infections).
    • Targets for vaccination.
    • Have adhesive structure
    • Adhesins
    • at the tip of pili (hair) or fimbriae (thread or fiber)
    • behave as lectins
    • their ligands = cell receptor (Oligosaccharide residues of
    glycoprotein or glycolipid receptors)
    • also bind to structural elements of the basement membrane
    (collagen, fibronectin, etc.)
    • Functions
    • Site for phage attachment
    • DNA transfer
    • Biofilm formation
    • Cell aggregation
    • Cell invasion
    • Motility (twitching)

    Pili of G(-) bacteria

    • Structure typically: non-covalent homopolymerization of pilins (form the pilus shaft)


    • Classified into 4 groups (depend on assembly pathways).
    1. Pili with chaperone-usher pathway.
    1. Assembly:
    • The pilin is secreted into the periplasmic space. In there, it binds
    to specific a chaperone (FimC) which helps protein folding &
    prevents premature assembly. The complex is then delivered to
    the outer membrane usher, which serves as a platform for pilus
    assembly. Adhesive structures: (1.) heteropolymers, flexible
    fibrillar tip, with a single specific adhesive protein at the end. (2.)
    homopolymers of non-pilus adhesins
    2. Members
    • Type I :
    • found in Enterobacteriaceae & in most E. coli strains
    • is most prevalent type of pilus in uropathogenic
    Escherichia coli (UPEC) adhesive structure (adhesion
    causes cystitis).
    • encoded by the fim gene cluster (fimA-fimH).
    • helical rod (right-handed helical array of 500-3000 copies
    of FimA) with the size of 6.9 nm thick x 1-2 micrometers
    long is connected via FimF to a short stubby 3 mm wide
    linear tip fibrillum containing FimG and the specific
    adhesin FimH (Fig.1 below)
    • FimH has 2 domains: receptor-binding domain (N-
    terminal) & pilin domain (C-terminal).
    • FimH binds to mannose-containing receptors. (uroplakins;
    integral glycoprotein receptors coating luminal surface of
    bladder epithelium.)
    • FimH binding to bladder cells triggers a signal transduction
    cascade (leading to actin reorganization,
    phosphoinositide-3-kinase activation and protein tyrosine
    phosphorylation).
    • Type I pili are required for initial surface attachment in
    biofilm formation.
    • P pili
    • UPEC.
    • Virulent factor (pyelonephritis).
    • Encoded by 11 pap genes (pyelonephritis-associated pili
    genes).
    • Structure similar to type I pili.
    • Rod (a right-handed helical cylinder) with the
    dimension of 6.8 nm wide x many micrometers long
    have PapG adhesin (and three minor pilus proteins
    PapE, PapF, and PapK) on the tip of fibrillum.
    • Three PapG variants (PapGI, -II, and -III) have different
    receptor specificity, binding preferentially to
    globotriaosylceramide or GbO3 (abundant on human
    uroepithelial cells), globoside or GbO4 (glycolipid iso-
    receptor of the human kidney, primarily associated with
    human pyelonephritis & bacteremia), and Forssman
    antigen or globopentosylceramide, GbO5, (associated with
    cystitis), respectively
    • flexible tip fibrillum
    • has 2 domains (see Fig. 2)
    • S pili
    • in E. coli causing sepsis, meningitis, & UTI.
    • SfaS adhesin binds to SA on endothelial cells & to kidney
    epithelial cell receptors.
    • major SfaA pilins have adhesive properties binding to
    glycolipids & plasminogen.
    • Hif pili
    • in Haemophilus influenza
    • PMF (Proteus mirabilis fimbriae) pili
    • in Proteus mirabilis (cystitis & polynephritis).
    • pmf operon encodes 5 predicted proteins
    • PmfA (major pilin)
    • PmfC (usher)
    • PmfD (chaperone)
    • PmfE (minor pilin)
    • PmfF (adhesin)
    • Dr/ Afa adhesin family pili
    • with homopolymer adhesin
    • in UPEC
    • in diffusely adhering E. coli (DAEC)
    • encoded by at least 5 afa genes (A-E)
    • AfaE is adhesin
    • most Afa/Dr adhesins recognize DAF (a complement-
    regulatory membrane protein, on RBC, uroepithelium, and
    CEACAMs). Fig. 3.
    • AfaE-I, AfaE-III, DraE and DaaE have 2 independently
    functional binding sites.
    • DraE (not AfaE-III, a homologue) binds to Type IV collagen.
    • may facilitate ascending colonization & chronic infection
    of UT.
    • some associated with enteric infection.
    • facilitate UPEC invasion of uroepithelial cells.
    • AfaD adhesin has invasin properties.
    • Dr fimbriae can be released into medium (in response to
    temperature & reduced oxygen).
    • F1 pili
    • in Yersinia pestis
    • F1 (polymeric capsular antigen)
    • in ETEC (enterotoxigenic E. coli)
    • CFA/I (colonization factor antigen I)
    • Others (K99, K88, F17, or F6 pili)
    • thinner fibers (2-5 nm thick).
    • mostly associated with animal ETEC.
    2. Type IV pili (more details from here onwards, will be continued on a new page;
    part 2).
    3. Pili with extracellular nucleation/precipitation pathway (curli pili)
    4. Pili with alternative chaperone-usher pathway (CS1 pilus family)

    Figure 1 Type I Pilus (note: FimC = chaperone, FimD = usher) (Michael Vetsch, et al, 2004)

    see http://www.nature.com/nature/journal/v431/n7006/images/nature02891-f1.2.jpg

    Figure 2 FimH and PapG (Source: Steve Matthews, Biological Nuclear Magnetic Resonance
    (NMR)) http://www.bio.ic.ac.uk/research/matthews/papg.jpg

    Figure 3 DraE/AfaE Adhesin (green = DAF-binding site, red = CEA-binding site)

    (Korotkova et al, 2004)

    http://www.jbc.org/content/vol281/issue39/images/medium/zbc0410669330007.gif

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