Structure-function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli.
Several in-frame linker insertions have been made in various positions in the faeG gene encoding the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. The effects of the linker insertions have been investigated with regard to the ability of the mutated fimbrial subunits to be exported to the surface of the bacterial cell and assembled into a fimbrial structure. The structure/function relationship of the subunit protein is discussed in the light of the phenotypes of the mutations constructed, secondary structure predictions, and hydrophilicity plots.
Department of Microbiology, Technical University, Lyngby, Denmark.
P A
PA
Pedersen
D000595:Amino Acid Sequence; D000942:Antigens, Bacterial; D000954:Antigens, Surface / Q000235:genetics / Q000502:physiology*; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000502:physiology*; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D013329:Structure-Activity Relationship
D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C026888:K88 antigen, E coli; D036781:Fimbriae Proteins