A new alpha-galactosyl-binding protein from the mushroom Lyophyllum decastes.
A new alpha-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 10,276Da. 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 alpha1,4Gal), 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.
Goldstein
Irwin J
IJ
Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-0606, USA.
Winter
Harry C
HC
Aurandt
Jennifer
J
Confer
Laura
L
Adamson
Julie T
JT
Hakansson
Kristina
K
Remmer
Henriette
H
D000363:Agaricales / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002241:Carbohydrates / Q000737:chemistry*; D005690:Galactose / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding
D002241:Carbohydrates; D037102:Lectins; D005690:Galactose