N-linked oligosaccharides of human transferrin are not required for binding to bacterial transferrin receptors.
Derivatives of human transferrin (hTf) with removed or modified N-linked oligosaccharides were compared with native hTf with respect to their binding to bacterial hTf receptors from Neisseria meningitidis, N. gonorrhoeae, and Haemophilus influenzae. Partially and fully deglycosylated hTf were prepared by enzymatic deglycosylation with glycopeptidase F and isolated by concanavalin A-Sepharose affinity chromatography. Oligosaccharide-modified hTf was prepared via mild periodate oxidation. Competition and direct binding experiments with the hTf derivatives demonstrated that the hTf oligosaccharides are not essential for binding to the bacterial hTf receptors.
Padda
J S
JS
Department of Microbiology and Infectious Diseases, University of Calgary, Alberta, Canada.
Schryvers
A B
AB
D000581:Amidohydrolases; D001667:Binding, Competitive; D002846:Chromatography, Affinity; D006031:Glycosylation; D006193:Haemophilus influenzae / Q000378:metabolism; D006801:Humans; D009344:Neisseria gonorrhoeae / Q000378:metabolism; D009345:Neisseria meningitidis / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism*; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D011990:Receptors, Transferrin / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*
D009844:Oligosaccharides; D011990:Receptors, Transferrin; D014168:Transferrin; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase