Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (15)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Endo, T.
Right arrow Articles by Ozaki, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Endo, T.
Right arrow Articles by Ozaki, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, 2000, Vol. 10, No. 8 809-813
© 2000 Oxford University Press

Cloning and expression of ß1,4-galactosyltransferase gene from Helicobacter pylori

Tetsuo Endo1, Satoshi Koizumi, Kazuhiko Tabata2 and Akio Ozaki2

Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., 3–6–6, Asahi-machi, Machida-shi, Tokyo 194–8533, Japan

Helicobacter pylori, which is a human pathogen associated with gastric and duodenal ulcer, has been shown to express human oncofetal antigens Lewis X and Lewis Y. Although the mammalian glycosyltransferases that synthesize these structures are well characterized, little is known about the corresponding bacterial enzymes. We report that a novel ß1,4-galactosyltransferase gene (HpgalT) involved in the biosynthesis of lipopolysaccharides in H.pylori has been cloned and expressed in Escherichia coli. The deduced amino acid sequence of the protein (HpGal-T) encoded by HpgalT consists of 274 residues with the calculated molecular mass of 31,731 Da, which does not show significant similarity to those of ß1,4-galactosyltransferases from mammalian sources and Neisseria. It was confirmed that HpGal-T catalyzed the introduction of galactose from UDP-Gal in a ß1,4 linkage to accepting N-acetylglucosamine (GlcNAc) residues by means of high-performance anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD). When the E.coli cells which overexpressed HpgalT was coupled with the UDP-Gal production system, which consisted of recombinant E.coli cells overexpressing its UDP-Gal biosynthetic genes and Corynebacterium ammoniagenes, N-acetyllactosamine, a core structure of lipopolysaccharide of H.pylori, was efficiently produced from orotic acid, galactose, and GlcNAc.

1 To whom correspondence should be addressed

2 Present address: Technical Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., 1–1 Kyowa-cho, Hofu-shi, Yamaguchi 747–8522, Japan


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 GlycobiologyHome page
E. Yavuz, S. Drouillard, E. Samain, I. Roberts, and B. Priem
Glucuronylation in Escherichia coli for the bacterial synthesis of the carbohydrate moiety of nonsulfated HNK-1
Glycobiology, February 1, 2008; 18(2): 152 - 157.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
K. Hiratsuka, S. M. Logan, J. W. Conlan, V. Chandan, A. Aubry, N. Smirnova, H. Ulrichsen, K. H. N. Chan, D. W. Griffith, B. A. Harrison, et al.
Identification of a D-glycero-D-manno-Heptosyltransferase Gene from Helicobacter pylori
J. Bacteriol., August 1, 2005; 187(15): 5156 - 5165.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
S. M. Logan, E. Altman, O. Mykytczuk, J.-R. Brisson, V. Chandan, F. St. Michael, A. Masson, S. Leclerc, K. Hiratsuka, N. Smirnova, et al.
Novel biosynthetic functions of lipopolysaccharide rfaJ homologs from Helicobacter pylori
Glycobiology, July 1, 2005; 15(7): 721 - 733.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
Z. Liu, Y. Lu, J. Zhang, K. Pardee, and P. G. Wang
P1 Trisaccharide (Gal{alpha}1,4Gal{beta}1,4GlcNAc) Synthesis by Enzyme Glycosylation Reactions Using Recombinant Escherichia coli
Appl. Envir. Microbiol., April 1, 2003; 69(4): 2110 - 2115.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
M. V. Tullius, N. J. Phillips, N. K. Scheffler, N. M. Samuels, R. S. Munson Jr., E. J. Hansen, M. Stevens-Riley, A. A. Campagnari, and B. W. Gibson
The lbgAB Gene Cluster of Haemophilus ducreyi Encodes a {beta}-1,4-Galactosyltransferase and an {alpha}-1,6-DD-Heptosyltransferase Involved in Lipooligosaccharide Biosynthesis
Infect. Immun., June 1, 2002; 70(6): 2853 - 2861.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.