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Fimbrial adhesins enable bacteria to attach to eucaryotic cells. The genetic determinants for S fimbrial adhesins (sfa) and for F1C ("pseudotype I") fimbriae (foc) were compared. Sfa and F1C represent functionally distinct adhesins in their receptor specificities. Nevertheless, a high degree of homology between both determinants was found on the basis of DNA-DNA hybridizations. Characteristic differences in the restriction maps of the corresponding gene clusters, however, were visible in regions coding for the fimbrial subunits and for the S-specific adhesin. While a plasmid carrying the genetic determinant for F1C fimbriae was able to complement transposon-induced sfa mutants, a plasmid carrying the genetic determinant for a third adhesin type, termed P fimbriae, was unable to do so. Proximal sfa-specific sequences carrying the S fimbrial structural gene were fused to sequences representing the distal part of the foc gene cluster to form a hybrid cluster, and the foc proximal region coding for the structural protein was ligated to sfa distal sequences to form a second hybrid. Both hybrid clones produced intact fimbriae. Anti-F1C monoclonal antibodies (MAbs) only recognized clones which produced F1C fimbriae, and an anti-S adhesin MAb marked clones which expressed the S adhesin. However, one of four other anti-S fimbriae-specific MAbs reacted with both fimbrial structures, S and F1C, indicating a common epitope on both antigens. The results presented here support the view that sfa and foc determinants code for fimbriae that are similar in several aspects, while the P fimbriae are members of a more distantly related group.

Gene clusters for S fimbrial adhesin (sfa) and F1C fimbriae (foc) of Escherichia coli: comparative aspects of structure and function