JBC Avanti Polar Lipids

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on April 19, 2002
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
277/17/14996    most recent
M200161200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Winter, H. C.
Right arrow Articles by Goldstein, I. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Winter, H. C.
Right arrow Articles by Goldstein, I. J.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print February 8, 2002
J. Biol. Chem, 10.1074/jbc.M200161200
Submitted on January 7, 2002
Revised on February 6, 2002
Accepted on February 8, 2002

The mushroom Marasmius oreades lectin is a blood group type B agglutinin that recognizes the Galalpha 1,3Gal and Galalpha 1,3Galbeta 1,4GlcNAc porcine xenotransplantation epitopes with high affinity

Harry C. Winter, Kazem Mostafapour, and Irwin J. Goldstein

Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-0606

Corresponding Author: igoldste{at}umich.edu

A blood group B-specific lectin from the mushroom Marasmius oreades (MOA) was investigated with respect to its molecular structure and carbohydrate binding properties. SDS-PAGE mass spectrometric analysis showed it to consist of an intact (H; Mr 33 kDa) and truncated (L; Mr 23 kDa) subunit in addition to a small polypeptide (P; Mr 10 kDa). Isolation in the presence of EDTA produced only the H subunits, indicating that the latter two are formed by metalloprotease cleavage of the intact H subunit. Tryptic digestion of the H, L, and P polypeptide chains followed by mass spectral analysis support this view. The lectin strongly precipitated blood group B substance, was non-reactive with type A substance, and reacted weakly with type H substance. Carbohydrate binding studies reveal a high affinity for Galalpha 1,3Gal (but not for the isomeric alpha 1,2-, alpha 1,4- and alpha 1,6-disaccharides): Galalpha 1,3Galbeta 1,4GlcNAc; and the type B branched trisaccharide. MOA also reacts strongly with murine laminin from the EHS sarcoma and bovine thyroglobulin, both of which contain multiple Galalpha 1,3Galbeta 1,4GlcNAc end groups. This linear B trisaccharide is a component of porcine tissues and organs, preventing their transplantation into humans. MOA also shares carbohydrate recognition of this trisaccharide with toxin A elaborated by Clostridium difficile.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
L. Ma, H. Lu, A. Sprinkle, M. R. Parsek, and D. J. Wozniak
Pseudomonas aeruginosa Psl Is a Galactose- and Mannose-Rich Exopolysaccharide
J. Bacteriol., November 15, 2007; 189(22): 8353 - 8356.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
D. Loganathan, H. C. Winter, W. J. Judd, J. Petryniak, and I. J. Goldstein
Immobilized Marasmius oreades agglutinin: use for binding and isolation of glycoproteins containing the xenotransplantation or human type B epitopes
Glycobiology, December 1, 2003; 13(12): 955 - 960.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Tateno and I. J. Goldstein
Molecular Cloning, Expression, and Characterization of Novel Hemolytic Lectins from the Mushroom Laetiporus sulphureus, Which Show Homology to Bacterial Toxins
J. Biol. Chem., October 17, 2003; 278(42): 40455 - 40463.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
S. Teneberg, B. Alsen, J. Angstrom, H. C. Winter, and I. J. Goldstein
Studies on Gal{alpha}3-binding proteins: comparison of the glycosphingolipid binding specificities of Marasmius oreades lectin and Euonymus europaeus lectin
Glycobiology, June 1, 2003; 13(6): 479 - 486.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Tateno, H. C. Winter, J. Petryniak, and I. J. Goldstein
Purification, Characterization, Molecular Cloning, and Expression of Novel Members of Jacalin-related Lectins from Rhizomes of the True Fern Phlebodium aureum (L) J. Smith (Polypodiaceae)
J. Biol. Chem., March 21, 2003; 278(13): 10891 - 10899.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. P. Kruger, H. C. Winter, N. Simonson-Leff, J. A. Stuckey, I. J. Goldstein, and J. E. Dixon
Cloning, Expression, and Characterization of the Galalpha 1,3Gal High Affinity Lectin from the Mushroom Marasmius oreades
J. Biol. Chem., April 19, 2002; 277(17): 15002 - 15005.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.