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. 1984 Jun;44(3):592–598. doi: 10.1128/iai.44.3.592-598.1984

Characterization of nonfimbrial mannose-resistant protein hemagglutinins of two Escherichia coli strains isolated from infants with enteritis.

P H Williams, S Knutton, M G Brown, D C Candy, A S McNeish
PMCID: PMC263636  PMID: 6373609

Abstract

Escherichia coli strains 444-3 and 469-3, isolated from patients with severe infantile enteritis, are able to adhere to and penetrate human epithelial cells in culture. In addition to type 1 fimbriae and glycocalyces , both strains elaborate mannose-resistant nonfimbrial protein hemagglutinins specific for human erythrocytes. Purified agglutinins are aggregates (greater than 4 X 10(6) daltons) of a single protein subunit of apparent Mr 14,000 (469-3) to 14,500 (444-3). The optimal temperature for expression of the agglutinins is 37 degrees C. Bacteria grown at 22 degrees C, which show 1% or less of maximal activity, and mutants deficient in the ability to agglutinate human erythrocytes do not synthesize detectable levels of these surface proteins and, moreover, do not adhere to cultured epithelial cells. Coupled with the observation that purified agglutinins competitively inhibit bacterial adherence to cultured cells, these data indicate that the nonfimbrial surface proteins expressed by strains 444-3 and 469-3 are essential for adherence both to erythrocytes and to cultured epithelial cells.

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Selected References

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