Comparison of the binding properties of the mushroom Marasmius oreades lectin and Griffonia simplicifolia I-B4 isolectin to αgalactosyl carbohydrate antigens in the surface phase

doi:10.1111/j.1399-3089.2004.00108.x

If you are seeing this message, you may be experiencing temporary network problems. Please wait a few minutes and refresh the page. If the problem persists, you may wish to report it to your local Network Manager.

It is also possible that your web browser is not configured or not able to display style sheets. In this case, although the visual presentation will be degraded, the site should continue to be functional. We recommend using the latest version of Microsoft or Mozilla web browser to help minimise these problems.

Wiley InterScience

Xenotransplantation

Volume 11 Issue 3, Pages 254 - 261

Published Online: 19 Feb 2004

The International Xenotransplantation Association, a section of The Transplantation Society

Go to Society Site

< Previous Abstract | Next Abstract >

Save Article to My Profile Download Citation Request Permissions

Abstract | References | Full Text: HTML, PDF (Size: 170K) | Related Articles | Citation Tracking

Comparison of the binding properties of the mushroom Marasmius oreades lectin and Griffonia simplicifolia I-B₄ isolectin to αgalactosyl carbohydrate antigens in the surface phase

Svend Kirkeby ¹ , Harry C. Winter ² and Irwin J. Goldstein ²

¹ Department of Oral Medicine, Dental School, The Panum Institute, University of Copenhagen, Copenhagen, Denmark , ² Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, MI, USA

Correspondence to Address reprint requests to Svend Kirkeby, Department of Oral Medicine, Dental School, The Panum Institute, University of Copenhagen, Nørre Allé 20, Copenhagen 2200 N, Denmark
(E-mail: sk@odont.ku.dk)

KEYWORDS

Galα • Griffonia simplicifolia • lectins • Marasmius oreades • xenotransplantation

Kirkeby S, Winter HC, Goldstein IJ. Comparison of the binding properties of the mushroom Marasmius oreades lectin and Griffonia simplicifolia I-B₄ isolectin to αgalactosyl carbohydrate antigens in the surface phase.
Xenotransplantation 2004; 11: 1–8. © Blackwell Munksgaard, 2004

ABSTRACT

Abstract: The binding of two α-galactophilic lectins, Marasmius oreades agglutinin (MOA), and Griffonia simplicifolia I isolectin B₄ (GS I-B₄) to neoglycoproteins and natural glycoproteins were compared in a surface phase assay. Neoglycoproteins carrying various α-galactosylated glycans and laminin from basement membrane of mouse sarcoma that contains the xenogenic Galα1–3Gal1–4GlcNAc epitope were immobilized in microtiter plate wells and lectin binding determined with an enzyme-linked assay. After 24 h of incubation, MOA had higher affinity for the xenogenic pentasaccharide (Galα1–3Gal1–4GlcNAcβ1–3Galβ1–4Glc) than for the Galα-monosaccharide. The binding properties of MOA and GS I-B₄ to the xenogenic disaccharide (Galα1–3Galβ1) were comparable while the binding of MOA to the xenogenic pentasaccharide was much stronger than the binding of GS I-B₄ to the same epitope. Non-xenogenic disaccharide-coupled neoglycoproteins having galactose end groups linked α1–2 or α1–4 to Gal or linked α1–3 to GalNAc bound very weakly to MOA, whereas GS I-B₄ recognized all of these disaccharides with similarly high affinity. MOA also showed high affinity for laminin. The results indicate that the Marasmius oreades lectin has nearly the same affinities as does GS I-B₄ for the simple xenogenic carbohydrate antigens, but MOA has greater affinity for the pentasaccharide and is far more specific in its binding preferences than the Griffonia lectin.