Penetration of fimbriate enteric bacteria through basement membranes: A hypothesis

Korhonen, Timo; Virkola, Ritva; Lähteenmäki, Kaarina; Björkman, Yvonne; Kukkonen, Maini; Raunio, Tiina; Tarkkanen, A; Westerlund, Benita

doi:10.1111/j.1574-6968.1992.tb05720.x

Cited by 38 publications

(13 citation statements)

References 32 publications

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“…The K1 capsule of E. coli contributes to bacterial resistance to phagosytosis and survival in circulation (Robbins et al ., 1974). We have earlier hypothesized that fimbriae and plasminogen receptors on E. coli O18acK1H7 potentiate bacterial penetration from circulation into the choroid plexus in the brain, where BM is accessible to circulation (Korhonen et al ., 1992). The type IV collagen is a major component of BMs and the type I collagen of ECMs (Kreis and Vale, 1993), and the adhesive characteristic here defined may have a pathogenetic function in the spread of E. coli through tissue barriers.…”

Section: Discussionmentioning

confidence: 99%

Amino acid residue Ala‐62 in the FimH fimbrial adhesin is critical for the adhesiveness of meningitis‐associated Escherichia coli to collagens

Pouttu

Puustinen

Virkola

et al. 1999

Molecular Microbiology

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107

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SummaryAdhesion of meningitis-associated Escherichia coli O18acK1H7 to collagens was characterized. The E. coli strain IHE 3034 adhered to type IV and type I collagens but not to type III collagen immobilized on glass. Collagens lack terminal mannosyl units, yet the bacterial adhesion was completely abolished in the presence of ␣-methyl-D-mannoside. A cat cassette was introduced into the fimA gene of IHE 3034, and the resulting mutant strain IHE 3034-2 failed to adhere to collagens. In contrast, insertion of a Gm cassette into the sfaA gene of IHE 3034, encoding the S-fimbrillin, had no significant effect on the adhesiveness. The fim cluster from IHE 3034 was cloned and expressed in trans in the fimA::cat mutant strain IHE 3034-2. The complemented strain IHE 3034-2(pRPO-1) exhibited adhesiveness to type IV and type I collagens, confirming the function of the type 1 fimbria in the adhesion. We have previously shown that the type 1 fimbria from E. coli K-12 strain PC31 does not confer bacterial adhesiveness to collagens. The fimH genes from E. coli IHE 3034 as well as from PC31 were expressed in the fimH-null strain MS4. The FimH from IHE 3034 potentiated collagen adherence, whereas the FimH from PC31 was inactive. Sequence comparison of fimH from IHE 3034 and PC31 revealed five amino-acid differences in the predicted mature FimH proteins: at residues 27, 62, 70, 78 and 201. Each of these residues in the IHE 3034-FimH were individually substituted to the corresponding amino acid in the PC31-FimH. The substitution S62→A completely abolished collagen adhesiveness. The reverse substitution A62→S in the PC31-FimH as well as in the FimH from another E. coli strain induced collagen adhesiveness to the level seen with IHE 3034-FimH. Out of nine fimH genes analysed from isolates of E. coli, collagen adhesiveness as well as alanine at position 62 in FimH were found only in two O18acK1H7 isolates with the isoenzyme profile ET type 1. Our results demonstrate that the amino-acid residue Ala-62 in the FimH lectin is critical for the adhesion to collagens by a highly virulent clonal group of E. coli.

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Section: Discussionmentioning

confidence: 99%

Amino acid residue Ala‐62 in the FimH fimbrial adhesin is critical for the adhesiveness of meningitis‐associated Escherichia coli to collagens

Pouttu

Puustinen

Virkola

et al. 1999

Molecular Microbiology

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107

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“…That Plg activation is involved in systemic infection was inferred from the observations that meningococcal meningitis is associated with enhanced fibrinolytic activity [75]. The finding of PlgR or PA function in several invasive bacterial pathogens has led to suggestions that plasmin formation has a role in tissue damage associated with or needed for invasive infections, including meningitis [215–218]. Although the number of bacterial species found to express PlgRs is appreciable (see Table 3), the pathogenetic function of Plg activation has been addressed with a limited group of invasive bacteria.…”

Section: Interaction Of Pathogenic Bacteria With the Plasminogen Systemmentioning

confidence: 99%

“…Although the number of bacterial species found to express PlgRs is appreciable (see Table 3), the pathogenetic function of Plg activation has been addressed with a limited group of invasive bacteria. These include Y. pestis [116] and other enteric bacteria [123,215], Borrelia [171,219–221], H. influenzae [222], staphylococci [73], group A streptococci [223], and Fusobacterium nucleatum [178]. The studies have mainly focused on testing whether bacterium‐associated plasmin activity degrades proteins of the ECM or BM and whether plasmin formation potentiates bacterial penetration through these tissue barriers.…”

Section: Interaction Of Pathogenic Bacteria With the Plasminogen Systemmentioning

confidence: 99%

Bacterial plasminogen activators and receptors

Lähteenmäki¹,

Kuusela²,

Korhonen³

2001

FEMS Microbiol Rev

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256

181

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Invasive bacterial pathogens intervene at various stages and by various mechanisms with the mammalian plasminogen/plasmin system. A vast number of pathogens express plasmin(ogen) receptors that immobilize plasmin(ogen) on the bacterial surface, an event that enhances activation of plasminogen by mammalian plasminogen activators. Bacteria also influence secretion of plasminogen activators and their inhibitors from mammalian cells. The prokaryotic plasminogen activators streptokinase and staphylokinase form a complex with plasmin(ogen) and thus enhance plasminogen activation. The Pla surface protease of Yersinia pestis resembles mammalian activators in function and converts plasminogen to plasmin by limited proteolysis. In essence, plasminogen receptors and activators turn bacteria into proteolytic organisms using a host-derived system. In Gram-negative bacteria, the filamentous surface appendages fimbriae and flagella form a major group of plasminogen receptors. In Gram-positive bacteria, surface-bound enzyme molecules as well as M-protein-related structures have been identified as plasminogen receptors, the former receptor type also occurs on mammalian cells. Plasmin is a broad-spectrum serine protease that degrades fibrin and noncollagenous proteins of extracellular matrices and activates latent procollagenases. Consequently, plasmin generated on or activated by Haemophilus influenzae, Salmonella typhimurium, Streptococcus pneumoniae, Y. pestis, and Borrelia burgdorferi has been shown to degrade mammalian extracellular matrices. In a few instances plasminogen activation has been shown to enhance bacterial metastasis in vitro through reconstituted basement membrane or epithelial cell monolayers. In vivo evidence for a role of plasminogen activation in pathogenesis is limited to Y. pestis, Borrelia, and group A streptococci. Bacterial proteases may also directly activate latent procollagenases or inactivate protease inhibitors of human plasma, and thus contribute to tissue damage and bacterial spread across tissue barriers.

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“…The S ®mbriae also immobilize human plasminogen and tissue-type plasminogen activator (tPA), facilitating activation of plasminogen and formation of plasmin proteolytic activity on the E. coli surface (Parkkinen et al 1991;Parkkinen 1992). These numerous tissue interactions suggest an important role for the S ®mbriae in conferring on the bacterial pathogen the ability to penetrate tissue barriers during the course of infection (Korhonen et al 1992). S ®mbriae are highly homologous to Sfr and F1C ®mbriae, neither of which, however, possess hemagglutinating ability (Hacker et al 1985; Moch et al 1987;Ott et al 1988;Pawelzik et al 1988;Van Die et al 1991).…”

Section: Introductionmentioning

confidence: 99%

Functional analysis of the minor subunits of S fimbrial adhesin (SfaI) in pathogenic Escherichia coli

et al. 2000

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S fimbrial adhesins I and II (SfaI and II), produced by extraintestinal Escherichia coli pathogens that cause urinary tract infections (UTI) and newborn meningitis (NBM), respectively, mediate bacterial adherence to sialic acid-containing glycoprotein receptors present on host epithelial cells and extracellular matrix. The S fimbrial adhesin complexes consist of four proteins: SfaI-A, the major subunit protein and the minor subunit proteins SfaI-G, SfaI-S and SfaI-H. Sialic acid-specific binding is mediated by the minor subunit protein SfaI-S. In order to determine whether the minor subunit proteins SfaI-G, -S and -H play a role in the modulation of adherence and the degree of fimbriation, a trans-complementation system was developed. A non-adhesive E. coli K-12 derivative, harbouring the sfaI-A gene but lacking sfaI-G, -S and -H, was transformed with sfaI-G, -S or -H. Only SfaI-S was able to increase the degree of fimbriation and to confer adhesion properties on the recombinant E. coli K-12 strains. Amino acid residues in SfaI-S that are involved in modulation of fimbriation as well as in receptor recognition were localized by random and site-directed mutagenesis.

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Penetration of fimbriate enteric bacteria through basement membranes: A hypothesis

Cited by 38 publications

References 32 publications

Amino acid residue Ala‐62 in the FimH fimbrial adhesin is critical for the adhesiveness of meningitis‐associated Escherichia coli to collagens

Amino acid residue Ala‐62 in the FimH fimbrial adhesin is critical for the adhesiveness of meningitis‐associated Escherichia coli to collagens

Bacterial plasminogen activators and receptors

Functional analysis of the minor subunits of S fimbrial adhesin (SfaI) in pathogenic Escherichia coli

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