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Engineering of the Glycan-binding Specificity of Agrocybe cylindracea Galectin toward {alpha}(2,3)-linked Sialic Acid by Saturation Mutagenesis.
MedLine Citation:
PMID:  21813503     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Sialic acid represents a critical sugar component located at the outermost position of glycoconjugates, playing important roles in extensive biological processes. To date, however, there have been only few probes which show affinity to α(2,3)-linked sialic acid-containing glycoconjugates. Agrocybe cylindracea galectin is known to have a relatively high affinity toward Neu5Acα(2,3)Galβ(1,4)Glc (3'-sialyl lactose), but it significantly recognizes various β-galactosides, such as Galβ(1,4)GlcNAcβ (LacNAc) and Galβ(1,3)GalNAcα (T-antigen). To eliminate this background specificity, we focused an acidic amino acid residue (Glu86), which interacts with the glucose unit of 3'-sialyl lactose, and substituted it with all other amino acids. Carbohydrate-binding specificity of the derived 14 mutants was analyzed by surface plasmon resonance, and it was found that E86D mutant (Glu86 substituted with Asp) substantially lost the binding ability to LacNAc and T-antigen, while it retained the high affinity for 3'-sialyl lactose. Further, frontal affinity chromatography analysis using 132 pyridylaminated oligosaccharides confirmed that the E86D mutant had a strong preference for α(2,3)-disialo biantennary N-linked glycan. However, it showed the large decrease in the affinity for any of the asialo-complex type N-glycans and the glycolipid-type glycans. Thus, the developed mutant E86D will be of practical use in various fields relevant to cell biology and glycotechnology.
Authors:
Koji Imamura; Hideaki Takeuchi; Rikio Yabe; Hiroaki Tateno; Jun Hirabayashi
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-8-3
Journal Detail:
Title:  Journal of biochemistry     Volume:  -     ISSN:  1756-2651     ISO Abbreviation:  -     Publication Date:  2011 Aug 
Date Detail:
Created Date:  2011-8-4     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Glyence Co., Ltd., Nagoya, Aichi 464-0858; Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8568, Japan.
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