Abstract
Genes encoding the Escherichia coli IH11165 hemagglutinins with specificity for terminal N-acetyl-D-glucosamine and blood group M antigen, respectively, were cloned by a cosmid cloning procedure. A 22-kilobase-pair subclone expressed both hemagglutination specificities in the nonhemagglutinating E. coli HB101 recipient strain. Derivatives obtained by insertion and deletion mutagenesis expressed either one of the two hemagglutination specificities. Both agglutinins were purified; the agglutinin recognizing terminal N-acetyl-D-glucosamine was associated with a new type of fimbria (G fimbria) with an apparent subunit molecular mass of 19.5 kilodaltons, whereas the blood group M agglutinin (M agglutinin) was nonfimbrial and had an apparent subunit mass of 21 kilodaltons.