Nonlethal adherence to human neutrophils mediated by Dr antigen-specific adhesins of Escherichia coli.

Uropathogenic Escherichia coli strains express a variety of adhesins, including members of the Dr adhesin family such as the Dr hemagglutinin, AFAI, and AFAIII. Certain E. coli adhesins (e.g., type 1 and S fimbriae) are known to mediate adherence to human polymorphonuclear leukocytes (PMNs). The receptor on erythrocytes for Dr family adhesins, decay accelerating factor, is also present on PMNs. To determine whether Dr family adhesins mediate adherence to PMNs and to characterize the specificity and consequences of such adherence, we studied agglutination of PMNs and adherence to PMNs by recombinant E. coli strains expressing various mannose-resistant or mannose-sensitive adhesins, in the presence or absence of inhibitors of adherence. Dr family adhesins, like type 1 fimbriae, mediated concentration-dependent adherence to PMNs. Adherence to PMNs was mannose sensitive for type 1 fimbriae but mannose resistant for Dr family adhesins. Chloramphenicol inhibited PMN adherence for the Dr hemagglutinin with the same potency as that with which it inhibited hemagglutination, but it was inactive against PMN adherence and hemagglutination mediated by other members of the Dr adhesin family. In contrast to PMN adherence mediated by type 1 fimbriae, adherence mediated by the Dr hemagglutinin did not lead to significantly increased bacterial killing. These data suggest that Dr family adhesins mediate a novel pattern of adherence to PMNs, probably by recognizing decay accelerating factor, with minimal consequent bacterial killing.