Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1926947 | Archives of Biochemistry and Biophysics | 2007 | 7 Pages |
Abstract
A new α-galactosyl binding lectin was isolated from the fruiting bodies of the mushroom Lyopyllum decastes. It is a homodimer composed of noncovalently-associated monomers of molecular mass 10,276 Da. The lectin's amino acid sequence was determined by cloning from a cDNA library using partial sequences determined by automated Edman sequencing and by mass spectrometry of enzyme-derived peptides. The sequence shows no significant homology to any known protein sequence. Analysis of carbohydrate binding specificity by a variety of approaches including precipitation with glycoconjugates and microcalorimetric titration reveals specificity towards galabiose (Gal α1,4Gal), a relatively rare disaccharide in humans. The lectin shares carbohydrate binding preference with the Shiga-like toxin, also known as verocytoxin, present in the bacteria Shigella dysenteriae and Escherichia. coli 0157:H7, both of which are causes of outbreaks of sometimes fatal food-borne illnesses.
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Authors
Irwin J. Goldstein, Harry C. Winter, Jennifer Aurandt, Laura Confer, Julie T. Adamson, Kristina Hakansson, Henriette Remmer,