A new alpha-galactosyl-binding protein from the mushroom Lyophyllum decastes |
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Authors: | Goldstein Irwin J Winter Harry C Aurandt Jennifer Confer Laura Adamson Julie T Hakansson Kristina Remmer Henriette |
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Affiliation: | a Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-0606, USA b Department of Chemistry and Biochemistry, Kettering University, Flint, MI 48504, USA c Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA |
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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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Keywords: | Alpha-galactosyl Galabiose Mushroom lectin Lyophyllum decastes P antigens Verocytoxin Shiga-like toxin |
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