Comparison of the lectin-like activity of pertussis toxin with two plant lectins that have differential specificities for alpha (2-6) and alpha (2-3)-linked sialic acid

• Published in: Biochemical and biophysical research communications Vol. 172; no. 3; p. 1224
• Main Authors: Heerze, L D, Armstrong, G D
• Format: Journal Article
• Language: English
• Published: United States 15-11-1990
• Subjects: Binding, Competitive; Carbohydrate Conformation; Glycoproteins - chemistry; Glycoproteins - metabolism; Hemagglutinins - metabolism; Isomerism; Lectins - metabolism; N-Acetylneuraminic Acid; Pertussis Toxin; Plant Lectins; Plants - analysis; Seeds - analysis; Sialic Acids - chemistry; Sialic Acids - metabolism; Virulence Factors, Bordetella - metabolism
• ISSN: 0006-291X
• DOI: 10.1016/0006-291X(90)91579-H

In this report we have compared the lectin-like properties of Pertussis toxin with two plant lectins which are known to possess different specificities towards terminal Neu5Ac Gal linkages on glycoconjugates. The hemagglutinin from elderberry bark (Sambucus nigra) has a binding specificity for terminal Neu5Ac alpha (2-6) Gal sequences and was found to bind a series of glycoconjugates with a similar specificity as Pertussis toxin. The binding specificity of Pertussis toxin was different from that of the leukoagglutinin from the seeds of Maackia amurensis which preferentially binds terminal Neu5Ac alpha (2-3) Gal sequences. These observations confirm the specificity of Pertussis toxin for Neu5Ac alpha (2-6) Gal glycoconjugate sequences.