Title: The Gal/GalNAc-specific lectin from the plant pathogenic basidiomycete Rhizoctonia solani is a member of the ricin-B family
Authors: Candy, L ×
Peumans, WJ
Menu-Bouaouiche, L
Astoul, CH
Van Damme, Jozef
Van Damme, EJM
Erard, M
Rouge, P #
Issue Date: Apr-2001
Publisher: Academic press inc
Series Title: Biochemical and Biophysical Research Communications vol:282 issue:3 pages:655-61
Abstract: The lectin isolated from the phytopathogenic basidiomycete Rhizoctonia solani (RSA) is a homodimer of two noncovalently associated monomers of 15.5 kDa, RSA is a basic protein (pI > 9) which consists mainly of beta -sheets, A presumed relationship with ricin-B is supported by the sequence similarity between the N-terminus of RSA and the N-terminal subdomain of ricin-B, Hydrophobic cluster analysis confirms that the N-terminus of both proteins has a comparable folding. RSA exhibits specificity towards Gal/GalNAc whereby the hydroxyls at the C3 ', C4 ', and C6 ' positions of the pyranose ring play a key role in the interaction with simple sugars. The carbohydrate-binding site of RSA apparently accommodates only a single sugar unit, Our results demonstrate an obvious evolutionary relationship between some fungal and plant lectins, but also provide evidence for the occurrence of a lectin consisting of subunits corresponding to a single subdomain of ricin-B. (C) 2001 Academic Press.
ISSN: 0006-291X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Molecular Immunology (Rega Institute)
× corresponding author
# (joint) last author

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