1992
DOI: 10.1128/iai.60.11.4460-4467.1992
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Role of crl in avian pathogenic Escherichia coli: a knockout mutation of crl does not affect hemagglutination activity, fibronectin binding, or Curli production

Abstract: 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 har… Show more

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Cited by 80 publications
(41 citation statements)
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“…An intriguing observation that now seems relevant to Crl's function is that the requirement of crl for curli production is variable between strains (Olsen et al, 1989;Provence and Curtiss, 1992). For example, provision of crl on a multicopy plasmid restored curli production in the curlideficient strain, HB101 (Olsen et al, 1989).…”
Section: Discussionmentioning
confidence: 99%
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“…An intriguing observation that now seems relevant to Crl's function is that the requirement of crl for curli production is variable between strains (Olsen et al, 1989;Provence and Curtiss, 1992). For example, provision of crl on a multicopy plasmid restored curli production in the curlideficient strain, HB101 (Olsen et al, 1989).…”
Section: Discussionmentioning
confidence: 99%
“…For example, provision of crl on a multicopy plasmid restored curli production in the curlideficient strain, HB101 (Olsen et al, 1989). In contrast, E. coli chi 7122 produces curli even if it lacks a functional crl gene (Provence and Curtiss, 1992). Moreover, crl, like rpoS, stimulates transcription of csgBA, which encodes the actual curlin subunit (Arnqvist et al, 1992).…”
Section: Discussionmentioning
confidence: 99%
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“…Non-pathogenic as well as human, avian and animal pathogenic Escherichia coli isolates and Salmonella enterica serovars produce adhesive fimbrial structures collectively referred to as curli (Olsen et al, 1989;Collinson et al, 1991;Collinson et al, 1992;Provence and Curtiss, 1992). Morphologically, curli are thin (2-5 nm diameter), coiled, highly aggregative fibres of varying length that protrude from the bacterial surface as an amorphous matrix (Olsen et al, 1989;Bian and Normark, 1997;Collinson et al, 1997;Prigent-Combaret et al, 2000;Brown et al, 2001;Chapman et al, 2002).…”
Section: Introductionmentioning
confidence: 99%
“…Together with cellulose, curli form a honeycomb-like structure that enables biofilm development through bacteria-bacteria interactions and adhesion to biotic and abiotic surfaces, conferring protection against environmental foes (Gerstel and Romling, 2001;Zogaj et al, 2001;Solano et al, 2002;Jain and Chen, 2007;Jonas et al, 2007;Gualdi et al, 2008). Due to these features, curli are considered a virulence attribute in these bacteria (Provence and Curtiss, 1992;Bian et al, 2000).…”
Section: Introductionmentioning
confidence: 99%