Binding specificities of wild-type and cloned Escherichia coli strains that recognize globo-A.
In this study we compared the specificity for the globoseries of glycolipids of Escherichia coli expressing the O-negative, A-positive (ONAP) adhesin and clones transformed with the pap-like (prs or pap-2) gene cluster. Receptor-active glycolipids were identified by the ability of radiolabeled bacteria to bind to the glycolipids on thin-layer chromatogram plates. The ONAP adhesin and pap-like clones bound with high affinity to the globo-A and Forssman glycolipids. The ONAP strains did not recognize other glycolipids of the globoseries. In contrast, the pap-like clones also showed weak binding to globotriaosylceramide and reacted weakly with Gal alpha 1----4 Gal beta-latex beads. We suggest that the pap-like and ONAP adhesins recognize an epitope shared by the globo-A and Forssman structures, e.g., terminal GalNAc alpha 1----3 bound to Gal alpha 1----4Gal beta-containing glycolipids.
Lindstedt
R
R
Departments of Clinical Immunology, University of Göteborg, Sweden.
Baker
N
N
Falk
P
P
Hull
R
R
Hull
S
S
Karr
J
J
Leffler
H
H
Svanborg Edén
C
C
Larson
G
G
D018830:Adhesins, Escherichia coli; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D002240:Carbohydrate Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000502:physiology*; D005798:Genes, Bacterial; D005915:Globosides / Q000378:metabolism*; D006028:Glycosphingolipids / Q000378:metabolism*; D006388:Hemagglutinins / Q000235:genetics; D008969:Molecular Sequence Data; D010957:Plasmids; D015183:Restriction Mapping; D013329:Structure-Activity Relationship
D018830:Adhesins, Escherichia coli; D001425:Bacterial Outer Membrane Proteins; D005915:Globosides; D006028:Glycosphingolipids; D006388:Hemagglutinins