A new α-galactosyl-binding protein from the mushroom Lyophyllum decastes

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 sequen...

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Veröffentlicht in:Archives of biochemistry and biophysics 2007-11, Vol.467 (2), p.268-274
Hauptverfasser: Goldstein, Irwin J., Winter, Harry C., Aurandt, Jennifer, Confer, Laura, Adamson, Julie T., Hakansson, Kristina, Remmer, Henriette
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Sprache:eng
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Zusammenfassung: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.
ISSN:0003-9861
1096-0384
DOI:10.1016/j.abb.2007.08.017