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.tb14057.x

Cited by 23 publications

(9 citation statements)

References 35 publications

(23 reference statements)

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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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“…Pathogens then use the proteolytic activity of plasmin as a mechanism to degrade host cell barriers and ECM proteins ( Fig. 6) (Korhonen et al, 1992;Lahteenmaki et al, 2001aLahteenmaki et al, , b, 2005. Streptokinase from Streptococcus spp., staphylokinase from S. aureus, Plg activator (Pla) from Y. pestis and finally Plg activator A (PauA) from Streptococcus uberis are well-known PAs (Parry et al, 2000;Lahteenmaki et al, 2001a, b).…”

Section: Functions and Distributionmentioning

confidence: 99%

“…Similar to enterococci, enteropathogenic E. coli O157: H7 (EPEC) immobilized on a dextran surface (Biacore) binds collagen I, Ln, Fn and glycosaminoglycans (Medina & Fratamico, 1998;Medina, 2001). This attachment of EPEC to host cells is often mediated by the surfaceexposed fimbriae, and these are known to bind Plg involved in the degradation of the epithelial BM (described in section 'The BM is breached by pathogenbound Plg and host proteases that degrade Ln and collagens') (Korhonen et al, 1992;Kukkonen et al, 1998). In the Shiga-toxigenic E. coli (STEC) O157:H7, two proteins present at the surface have been reported as adhesins.…”

Section: Pathogensmentioning

confidence: 99%

“…Generation of DraE mutants demonstrated the importance of the presence of DraE in the Dr haemagglutinin complex to achieve binding to DAF but not to collagen IV, and subsequently the importance of the interaction of fimbriae with collagen IV to achieve an efficient infection (Van Loy et al, 2002;Selvarangan et al, 2004). Moreover, type-G fimbriae have been defined to bind Plg, and other surface proteins such as curli fimbriae and the UPEC trimeric autotransporter were found to bind Ln (Korhonen et al, 1992;Kukkonen et al, 1998;Antao et al, 2009).…”

Section: Urogenital and Skin Pathogens Also Interact With Ln And Collmentioning

confidence: 99%

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Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host

et al. 2012

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Laminin (Ln) and collagen are multifunctional glycoproteins that play an important role in cellular morphogenesis, cell signalling, tissue repair and cell migration. These proteins are ubiquitously present in tissues as a part of the basement membrane (BM), constitute a protective layer around blood capillaries and are included in the extracellular matrix (ECM). As a component of BMs, both Lns and collagen(s), thus function as major mechanical containment molecules that protect tissues from pathogens. Invasive pathogens breach the basal lamina and degrade ECM proteins of interstitial spaces and connective tissues using various ECM-degrading proteases or surface-bound plasminogen and matrix metalloproteinases recruited from the host. Most pathogens associated with the respiratory, gastrointestinal, or urogenital tracts, as well as with the central nervous system or the skin, have the capacity to bind and degrade Lns and collagen(s) in order to adhere to and invade host tissues. In this review, we focus on the adaptability of various pathogens to utilize these ECM proteins as enhancers for adhesion to host tissues or as a targets for degradation in order to breach the cellular barriers. The major pathogens discussed are Streptococcus, Staphylococcus, Pseudomonas, Salmonella, Yersinia, Treponema, Mycobacterium, Clostridium, Listeria, Porphyromonas and Haemophilus; Candida, Aspergillus, Pneumocystis, Cryptococcus and Coccidioides; Acanthamoeba, Trypanosoma and Trichomonas; retrovirus and papilloma virus.

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“…Plasmin is a potent proteolytic enzyme that can dissolve blood clots and degrade the basement membrane proteins (Lottenberg et al, 1994). Degradation of the basement membrane proteins of BMEC was found to occur via activation of plasminogens tethered to bacterial receptors, thereby promoting bacterial penetration through the basement membranes (Korhonen et al, 1992;Lottenberg et al, 1994). Interestingly, the urokinase-type plasminogen activator receptor (uPAR) was found to be associated with parasitemia, disease progression and poor clinical outcome of P. falciparum malaria infection (Perch et al, 2004;Ostrowski et al, 2005).…”

Section: Contact-independent Mechanismsmentioning

confidence: 99%

Protozoa traversal of the blood–brain barrier to invade the central nervous system

Elsheikha

Khan

2010

FEMS Microbiol Rev

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Neuropathogenic protozoa have evolved strategies to breach the blood-brain barrier and invade the central nervous system. These include transcellular, paracellular and the Trojan horse routes but the associated molecular mechanisms remain incompletely understood. Here, we summarize the current understanding of protozoa penetration across the blood-brain barrier, focusing on Plasmodium, Babesia, Trypanosoma, Toxoplasma, Acanthamoeba and Balamuthia. Advances in understanding the molecular pathways will offer opportunities for the rational development of novel therapeutic interventions.

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Penetration of fimbriate enteric bacteria through basement membranes: A hypothesis

Cited by 23 publications

References 35 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

Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host

Protozoa traversal of the blood–brain barrier to invade the central nervous system

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