ITEM METADATA RECORD
Title: Expression analysis of a type S2 EUL-related lectin from rice in Pichia pastoris
Authors: Al Atalah, Bassam ×
Rougé, Pierre
Smith, David F
Proost, Paul
Lasanajak, Yi
Van Damme, Els J M #
Issue Date: Oct-2012
Publisher: The Journal
Series Title: Glycoconjugate Journal vol:29 issue:7 pages:467-479
Abstract: Rice (Oryza sativa) expresses different putative carbohydrate-binding proteins belonging to the class of lectins containing an Euonymus lectin (EUL)-related domain, one of them being OrysaEULS2. The OrysaEULS2 sequence consists of a 56 amino acid N-terminal domain followed by the EUL sequence. In this paper the original sequence of the EUL domain of OrysaEULS2 and some mutant forms have been expressed in Pichia pastoris. Subsequently, the recombinant proteins were purified and their carbohydrate binding properties determined. Analysis of the original protein on the glycan array revealed interaction with mannose containing structures and to a lesser extent with glycans containing lactosamine related structures. It was shown that mutation of tryptophan residue 134 into leucine resulted in an almost complete loss of carbohydrate binding activity of OrysaEULS2. Our results show that the EUL domain in OrysaEULS2 interacts with glycan structures, and hence can be considered as a lectin. However, the binding of the protein with the array is much weaker than that of other EUL-related lectins. Furthermore, our results indicate that gene divergence within the family of EUL-related lectins lead to changes in carbohydrate binding specificity.
ISSN: 0282-0080
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Molecular Immunology (Rega Institute)
× corresponding author
# (joint) last author

Files in This Item:
File Description Status SizeFormat
2012131.pdf Published 622KbAdobe PDFView/Open

These files are only available to some KU Leuven staff members

 


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science