Evidence That Agaricus Bisporus Agglutinin (Aba) Has Dual Sugar-binding Specificity.
From: Glycostructure Analysis Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, AIST Tsukuba Central 2, Ibaraki, Japan.
Biochemical and biophysical research communications
- Publish Date: Aug 2006
- ISSN: 0006-291X
- Volume: 347
- Issue: 1
- Pages: 215-20
- Medium: Print
- Language: English
- Citation (JAMA): Nakamura-Tsuruta Sachiko, Kominami Junko, Kuno Atsushi, et al. Evidence That Agaricus Bisporus Agglutinin (Aba) Has Dual Sugar-binding Specificity.. Biochem. Biophys. Res. Commun. Aug 2006;347:215-20
Abstract
Agaricus bisporus agglutinin (ABA) is known as a useful lectin to detect T-antigen (Core1) disaccharide (Galbeta1-3GalNAcalpha) and related O-linked glycans. However, a recent X-ray crystallographic study revealed the presence of another intrinsic sugar-binding site, i.e., for GlcNAc. To confirm this possibility, detailed analysis was performed using two advanced methods: lectin microarray and frontal affinity chromatography (FAC). In the lectin microarray, intense signals were observed on ABA spots for both N-glycanase-treated and O-glycanase/beta1-4galactosidase-treated Cy3-labeled asialofetuin. This indicates substantial affinity for both O-linked and agalactosylated (GlcNAc-exposed) N-linked glycans. A further approach by FAC using 20 pNP and 130 PA-oligosaccharides demonstrated that ABA bound to Core1 (K(d) = 3.4 x 10(-6) M) and Core2 (1.9 x 10(-5) M) but not to Core3 and Core6 O-linked glycans. It also showed substantial affinity to mono-, bi-, and tri-antennary agalactosylated complex-type N-linked glycans (K(d) > 1.8 x 10(-5) M). These results establish ABA as a lectin having dual sugar-binding sites with distinct specificity, i.e., for Gal-exposed O-linked glycans and GlcNAc-exposed N-linked glycans.
Mesh Headings (Keywords): Agglutinins, Binding Sites, Carbohydrates, Evidence-Based Medicine, Lectins, Protein Binding, Protein Interaction Mapping
Check for Full Text / PubMed Unique Identifier (PMID): 16824489
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.