Identification and functional characterization of the NanH extracellular sialidase from Corynebacterium diphtheriae

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Title
Identification and functional characterization of the NanH extracellular sialidase from Corynebacterium diphtheriae
Author(s)
Seong Hun KimDoo-Byoung OhOh Suk Kwon; H A Kang
Bibliographic Citation
Journal of Biochemistry, vol. 147, no. 4, pp. 523-533
Publication Year
2010
Abstract
Corynebacterium diphtheriae, a pathogenic Gram-positive bacterium, contains sialic acids on its cell surface, but no genes related to sialic acid decoration or metabolism have been reported in C. diphtheriae. In the present study, we have identified a putative sialidase gene, nanH, from C. diphtheriae KCTC3075 and characterized its product for enzyme activity. Interestingly, the recombinant NanH protein was secreted as a catalytically active sialidase into the periplasmic space in Escherichia coli, while the short region at its C-terminus was truncated by proteolysis. We reconstructed a truncated NanH protein His6-NanHΔN devoid of its signal sequence as a mature enzyme fused with the 6xHis tag at the N-terminal region. The purified His6-NanHΔN can cleave α-2,3- and α-2,6-linked sialic acid from sialic acid-containing substrates. In addition, even though the efficiency was low, the recombinant His6-NanHΔN was able to catalyse the transfer of sialic acid using several sialoconjugates as donor, suggesting that the reversible nature of C. diphtheriae NanH can be used for the synthesis of sialyl oligosaccharides via transglycosylation reaction.
Keyword
Corynebacterium diphtheriaeExtracellular proteinSialic acidSialidaseSialoglycoconjugate
ISSN
0021-924X
Publisher
Oxford Univ Press
DOI
http://dx.doi.org/10.1093/jb/mvp198
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Aging Convergence Research Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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