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 |
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Format: | Artikel |
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. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/j.abb.2007.08.017 |