Adherence of Escherichia coli is facilitated by fimbriae and several outer membrane proteins (OMPs). Hypertonic conditions, salicylate, and Mar mutations are known to reduce OmpF expression. We speculated that OMPs involved in export or assembly of fimbrial subunits might be similarly affected. To explore this hypothesis, E. coli expressing P, type 1, S, colonization factor antigen I (CFA/I), or CFA/II fimbriae was grown in the presence of salicylate, bismuth salts, NaCl, and nonfermented sugars. Tetracycline-resistant clones were derived from several P-fimbriated strains. The bacteria were tested for the ability to agglutinate erythrocytes, yeast cells, and alpha-D-Gal(-4)-beta-D-Gal-bonded latex (Gal-Gal) beads and were examined for fimbriae by electron microscopy. Hyperosmolar conditions decreased fimbrial expression for all strains. Expression of P fimbriae by pyelonephritic strains, all of which were OmpF+, was reversibly repressed by salicylate and bismuth salts. CFA strains were similarly affected. Tetracycline-resistant P-fimbriated strains were OmpF deficient, were unable to agglutinate erythrocytes and Gal-Gal beads, and lacked fimbriae as observed by electron microscopy. Strains with plasmid-encoded P-fimbrial genes did not demonstrate OmpF on polyacrylamide gel electrophoresis profiles and were not affected by salicylate. The type 1-fimbriated phenotype was not affected by salicylate or bismuth unless the strains also expressed P fimbriae. S-fimbriated strains were not affected. The mechanism by which salicylates, bismuth salts, and tetracycline resistance inhibit or modulate the expression of P fimbriae may be mediated through OmpF and other OMPs.