Growth conditions for the expression of fibronectin, collagen type I, vitronectin, and laminin binding toEscherichia coli strain NG7C

Ljungh, Åsa; Emödy, Levente; Aleljung, Pär; Olusanya, O; Wadström, Torkel

doi:10.1007/bf02105383

Cited by 22 publications

(7 citation statements)

References 16 publications

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“…There are indications that vitronectin is an extracellular matrix receptor, among other cellmatrix proteins, for staphylococci, streptococci and Escherichia coli during colonization of various tissues [15][16][17][18][19][20]. H. pylori may also use vitronectin as a receptor for adhesion in the gastric mucosa.…”

Section: Introductionmentioning

confidence: 99%

Vitronectin binding by Helicobacter pylori

Ringnér

1992

FEMS Microbiology Letters

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Vitronectin, a serum and extracellular matrix protein involved in immunological reactions, interacts with Helicobacter pylori strains. Of the 20 H. pylori strains tested three strains bound more than 50% of the vitronectin added, five strains bound 25–40%, nine strains bound 10–20% and three strains bound 5–8% vitronectin. Two strains, one with high‐ and one with low‐binding properties, were selected for further characterization of 125I‐vitronectin binding. Binding to the urea‐activated 125I‐labelled vitronectin was fast, saturable and reversible when an excess of unlabelled vitronectin was added to the bacteria with bound 125I‐vitronectin. The binding was heat‐ and protease‐sensitive, suggesting that the binding was mediated by bacterial cell‐surface proteins. Since components such as fetuin and orosomucoid but not asialofetuin inhibited the binding, sialic‐acid specific proteins, related to H. pylori sialic‐acid specific haemagglutinins, were probably involved.

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Section: Introductionmentioning

confidence: 99%

Vitronectin binding by Helicobacter pylori

Ringnér

1992

FEMS Microbiology Letters

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“…Recently, aggregative diarrheagenic E. coli strains have been described (33,39), as have hydrophobic E. coli strains capable of binding tissue matrix proteins (13,27,28). However, the nature of the aggregative phenotype and the mechanism by which the E. coli strains bind to tissue matrix proteins are unknown.…”

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confidence: 99%

“…b S. entenitidis 27655-3b fimbrin N-terminal amino acid sequence previously determined (9). ability to bind Congo red and fibronectin (8a) and that E. coli NG7C and Gambia 3, which also bind Congo red and various tissue matrix proteins including fibronectin (13,27,28), are now known to produce GVVPQ fimbriae. It remains to be determined whether GVVPQ fimbriae are involved in bacterial colonization of host epithelial tissues and whether they are advantageous to enteropathogens faced with the challenge of establishing an intestinal infection.…”

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confidence: 99%

Thin aggregative fimbriae from diarrheagenic Escherichia coli

et al. 1992

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Four strains of diarrheagenic Escherichia coli originally isolated from distinct geographic regions were found to produce unusual thin aggregative fimbriae requiring depolymerization in formic acid prior to analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunoelectron microscopy of native fimbriae and Western blot (immunoblot) analysis of the corresponding 18-kDa fimbrins showed that these E. coli fimbriae were serologically cross-reactive with SEF 17 (Salmonella enteritidis fimbriae with a fimbrin molecular mass of 17 kDa). The E. coli and S. enteritidis fimbrins had similar total amino acid compositions and highly conserved N-terminal amino acid sequences. These results indicate that E. coli and S. enteritidis produce biochemically related, aggregative fimbriae which constitute a new type of intergenerically distributed fimbriae for which we propose the descriptive name GVVPQ fimbriae on the basis of the conserved N-terminal amino acid sequence.Successful bacterial pathogens present to their susceptible host complex cell surfaces which contain components enabling the bacteria to initially associate with and subsequently adhere to specific host tissues (2, 21). The attachment of enteropathogens to gastrointestinal epithelial cells is presumed to be essential if these bacteria are to avoid host clearance mechanisms and compete with normal flora for appropriate niches (2, 15). However, the specific attachment mechanism(s) of many enteropathogens in vivo has not been clearly established (2,14).

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“…We determined whether there were culture conditions that would cause the expression of only hemagglutination activity or fibronectin binding. Previous work demonstrated that an E. coli diarrheal isolate lost the ability to bind fibronectin after growth on CFA agar containing 0.06 to 0.17 M NaCl (19) and that HB1O1(pCRL20) did not bind fibronectin or produce curli when grown at 26°C on CFA agar containing 0.15 M NaCl (23). We investigated hemagglutination activity and fibronectin binding after the growth of strains on higherosmolarity media.…”

Section: Resultsmentioning

confidence: 99%

Role of crl in avian pathogenic Escherichia coli: a knockout mutation of crl does not affect hemagglutination activity, fibronectin binding, or Curli production

Provence

Curtiss

1992

Infect Immun

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This study determined the role of crl in the production of curli by, the hemagglutination activity of, and fibronectin binding by avian pathogenic Escherichia coli X7122. Curli, an extracellular structure that binds fibronectin, was recently described (A. Olsen, A. Jonsson, and S. Normark, Nature [London] 338:652-655, 1989). The crl gene product was hypothesized to be the subunit monomer of curli and to bind fibronectin. E. coli HB101, which does not contain crl, binds fibronectin and produces curli when harboring a plasmid containing the crl gene. We show that HB101 hemagglutinates chicken erythrocytes when harboring the crl * Corresponding author. 4460 on August 5, 2020 by guest http://iai.asm.org/ Downloaded from

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Growth conditions for the expression of fibronectin, collagen type I, vitronectin, and laminin binding toEscherichia coli strain NG7C

Cited by 22 publications

References 16 publications

Vitronectin binding by Helicobacter pylori

Vitronectin binding by Helicobacter pylori

Thin aggregative fimbriae from diarrheagenic Escherichia coli

Role of crl in avian pathogenic Escherichia coli: a knockout mutation of crl does not affect hemagglutination activity, fibronectin binding, or Curli production

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