Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049525 | FEBS Letters | 2010 | 6 Pages |
Abstract
For the GalNAcα1→ specific Agaricus bisporus agglutinin (ABA) from an edible mushroom, the mechanism of polyvalent Galβ1→3/4GlcNAcβ1→ complex in ABA–carbohydrate recognition has not been well defined since Gal and GlcNAc are weak ligands. By enzyme-linked lectinosorbent and inhibition assays, we show that the polyvalent Galβ1→3/4GlcNAcβ1→ in natural glycans also play vital roles in binding and we propose that four different intensities of glycotopes (Galβ1-3GalNAcα1-, GalNAcα1-Ser/Thr and Galβ1-3/4GlcNAcβ1-) construct three recognition systems at the same domain. This peculiar concept provides the most comprehensive mechanism for the attachment of ABA to target glycans and malignant cells at the molecular level.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Albert M. Wu, Jia-Hau Liu, Yu-Ping Gong, Chia-Chen Li, En-Tzu Chang,