An alpha2,6-sialyltransferase cloned from Photobacterium leiognathi strain JT-SHIZ-119 shows both sialyltransferase and neuraminidase activity

We cloned, expressed, and characterized a novel beta-galactoside alpha2,6-sialyltransferase from Photobacterium leiognathi strain JT-SHIZ-119. The protein showed 56-96% identity to the marine bacterial alpha2,6-sialyltransferases classified into glycosyltransferase family 80. The sialyltransferase a...

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Bibliographic Details
Published in:Glycobiology (Oxford) 2010-02, Vol.20 (2), p.158-165
Main Authors: Mine, Toshiki, Katayama, Sakurako, Kajiwara, Hitomi, Tsunashima, Masako, Tsukamoto, Hiroshi, Takakura, Yoshimitsu, Yamamoto, Takeshi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Cloning, Molecular
Hydrogen-Ion Concentration
Molecular Sequence Data
Neuraminidase - biosynthesis
Neuraminidase - isolation & purification
Neuraminidase - metabolism
Photobacterium - enzymology
Recombinant Proteins - metabolism
Sequence Alignment
Sequence Analysis, DNA
Sialyltransferases - biosynthesis
Sialyltransferases - isolation & purification
Sialyltransferases - metabolism
Temperature
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Summary:We cloned, expressed, and characterized a novel beta-galactoside alpha2,6-sialyltransferase from Photobacterium leiognathi strain JT-SHIZ-119. The protein showed 56-96% identity to the marine bacterial alpha2,6-sialyltransferases classified into glycosyltransferase family 80. The sialyltransferase activity of the N-terminal truncated form of the recombinant enzyme was 1477 U/L of Escherichia coli culture. The truncated recombinant enzyme was purified as a single band by sodium dodecyl sulfate polyacrylamide gel electrophoresis through 3 column chromatography steps. The enzyme had distinct activity compared with known marine bacterial alpha2,6-sialyltransferases. Although alpha2,6-sialyltransferases cloned from marine bacteria, such as Photobacterium damselae strain JT0160, P. leiognathi strain JT-SHIZ-145, and Photobacterium sp. strain JT-ISH-224, show only alpha2,6-sialyltransferase activity, the recombinant enzyme cloned from P. leiognathi strain JT-SHIZ-119 showed both alpha2,6-sialyltransferase and alpha2,6-linkage-specific neuraminidase activity. Our results provide important information toward a comprehensive understanding of the bacterial sialyltransferases belonging to the group 80 glycosyltransferase family in the CAZy database.
ISSN:1460-2423
DOI:10.1093/glycob/cwp157