Article
Functional analysis of the sialic acid-binding adhesin SfaS of pathogenic Escherichia coli by site-specific mutagenesis.
Infection and immunity - 1 Jul 1990
Morschhäuser J, Hoschützky H, Jann K, Hacker J
Abstract excerpt
The gene coding for the sialic acid-specific adhesin SfaS produced by the S fimbrial adhesin (sfa) determinant of Escherichia coli has been modified by oligonucleotide-directed, site-specific mutagenesis. Lysine 116, arginine 118, and lysine 122 were replaced by threonine, serine, and threonine, respectively. The mutagenized gene clusters were able to produce S fimbrial adhesin complexes consisting of the...
Topics
- Adhesins, Escherichia coli
- Amino Acid Sequence
- Bacterial Adhesion
- Bacterial Proteins
- Base Sequence
- Carbohydrate Sequence
- Enzyme-Linked Immunosorbent Assay
- Escherichia coli
- Hemagglutination Tests
- Molecular Sequence Data