Binding of the galactose-specific Pseudomonas aeruginosa lectin, PA-I, to glycosphingolipids and other glycoconjugates.
The carbohydrate-binding specificity of Pseudomonas aeruginosa lectin I (PA-I) in iodinated or biotinylated form was studied. A large number of glycosphingolipids, as well as some glycoproteins and neoglycoproteins were used as ligands. Also, inhibition by free saccharides of PA-I binding to glycosphingolipids was tested. It was found that the lectin binds most strongly to terminal and nonsubstituted Gal alpha 3Gal- or Gal alpha 4Gal-structures.
Lanne
B
B
Department of Medical Biochemistry, Göteborg University, Sweden.
Cîopraga
J
J
Bergström
J
J
Motas
C
C
Karlsson
K A
KA
D018829:Adhesins, Bacterial; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism*; D002240:Carbohydrate Sequence; D002855:Chromatography, Thin Layer; D005690:Galactose / Q000378:metabolism*; D006001:Glycoconjugates / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism; D006028:Glycosphingolipids / Q000378:metabolism; D037102:Lectins / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D011549:Pseudomonas
D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D006001:Glycoconjugates; D006023:Glycoproteins; D006028:Glycosphingolipids; D037102:Lectins; C038692:adhesin, Pseudomonas; D005690:Galactose