Title of article :
A new α-galactosyl-binding protein from the mushroom Lyophyllum decastes
Author/Authors :
Goldstein، نويسنده , , Irwin J. and Winter، نويسنده , , Harry C. and Aurandt، نويسنده , , Jennifer and Confer، نويسنده , , Laura and Adamson، نويسنده , , Julie T. and Hakansson، نويسنده , , Kristina and Remmer، نويسنده , , Henriette، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
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.
Keywords :
Alpha-galactosyl , Lyophyllum decastes , Verocytoxin , Shiga-like toxin , Galabiose , P antigens , Mushroom lectin
Journal title :
Archives of Biochemistry and Biophysics
Journal title :
Archives of Biochemistry and Biophysics