Glycobiology Advance Access published online on September 30, 2009
Glycobiology, doi:10.1093/glycob/cwp157
An
2,6-sialyltransferase cloned from Photobacterium leiognathi strain JT-SHIZ-119 shows both sialyltransferase and neuraminidase activity
Glycotechnology Business Unit, Japan Tobacco Inc., 700 Higashibara, Iwata, Shizuoka 438-0802, JAPAN
1 To whom correspondence should be addressed: Tel: +81-538-32-7389; Fax: +81-538-33-6046; e-mail: takeshi.yamamoto{at}jt.com
Received on July 29, 2009; accepted on September 28, 2009
We cloned, expressed, and characterized a novel β-galactoside
2,6-sialyltransferase from Photobacterium leiognathi strain JT-SHIZ-119. The protein showed 56% to 96% identity to the marine bacterial
2,6-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
2,6-sialyltransferases. Although
2,6-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
2,6-sialyltransferase activity, the recombinant enzyme cloned from P. leiognathi strain JT-SHIZ-119 showed both
2,6-sialyltransferase and
2,6-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.
Key words: bi-functional sialyltransferase / neuraminidase / Photobacterium leiognathi