Multiple recognition systems adopting four different glycotopes at the same domain for the Agaricus bisporus agglutinin-glycan interactions.
For the GalNAcalpha1--> specific Agaricus bisporus agglutinin (ABA) from an edible mushroom, the mechanism of polyvalent Galbeta1-->3/4GlcNAcbeta1--> 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 Galbeta1-->3/4GlcNAcbeta1--> in natural glycans also play vital roles in binding and we propose that four different intensities of glycotopes (Galbeta1-3GalNAcalpha1-, GalNAcalpha1-Ser/Thr and Galbeta1-3/4GlcNAcbeta1-) 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.
Wu
Albert M
AM
Glyco-immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, College of Medicine, Chang-Gung University, Kwei-san, Tao-yuan 333, Taiwan. amwu@mail.cgu.edu.tw
Liu
Jia-Hau
JH
Gong
Yu-Ping
YP
Li
Chia-Chen
CC
Chang
En-Tzu
ET
D000364:Agaricus / Q000378:metabolism*; D000373:Agglutinins / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D000818:Animals; D000970:Antineoplastic Agents / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D001665:Binding Sites; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002417:Cattle; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000737:chemistry* / Q000378:metabolism*
C041433:Agaricus lectins; D000373:Agglutinins; D000970:Antineoplastic Agents; D006023:Glycoproteins; D037102:Lectins; D046911:Macromolecular Substances; D011134:Polysaccharides