JBC Origene Your Gene Company

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M011293200 on January 23, 2001

J. Biol. Chem., Vol. 276, Issue 16, 12785-12790, April 20, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/16/12785    most recent
M011293200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wakarchuk, W. W.
Right arrow Articles by Gilbert, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wakarchuk, W. W.
Right arrow Articles by Gilbert, M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Dependence of the Bi-functional Nature of a Sialyltransferase from Neisseria meningitidis on a Single Amino Acid Substitution*

Warren W. WakarchukDagger , David Watson, Frank St. Michael, Jianjun Li, Yuyang Wu, Jean-Robert Brisson, N. Martin Young, and Michel Gilbert

From the Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada, K1A 0R6

The L1 immunotype strain 126E of Neisseria meningitidis has been shown to have an N-acetyl-neuraminic acid-containing lipooligosaccharide in which an alpha -linked galactose from a Pk epitope is substituted at the O6 position (Wakarchuk, W. W., Gilbert, M., Martin, A., Wu, Y., Brisson, J. R., Thibault, P., and Richards, J. C. (1998) Eur. J. Biochem. 254, 626-633). Using a synthetic Pk-epitope containing acceptor in glycosyltransferase reactions, we were able to show by NMR analysis of the reaction product that the 126E(L1)-derived sialyltransferase can make both alpha -2,3 and alpha -2,6 linkages to the terminal galactose. Gene disruption experiments showed that the lst gene in 126E(L1) was responsible for the in vivo addition of the alpha -2,6-linked N-acetyl-neuraminic acid residue. By site-directed mutagenesis it was possible to change the MC58(L3)-derived enzyme into a bifunctional enzyme with a single amino acid change at position 168, where a glycine was changed to an isoleucine. We performed a gene replacement experiment where the 126E(L1) alpha -2,3/6-sialyltransferase was replaced by allelic exchange with the monofunctional MC58(L3) alpha -2,3-sialyltransferase and with the mutant MC58(L3) allele G168I. We observed that the level of LOS sialylation with the G168I allele was very similar to that of the wild type 126E(L1), indicating that residue 168 is the critical residue for the alpha -2,6-sialyltransferase activity in vitro as well as in vivo.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Immunochemistry Program, Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario, Canada K1A 0R6. Fax: 613-941-1327; E-mail: warren.wakarchuk@nrc.ca.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 GlycobiologyHome page
L. M Willis, M. Gilbert, M.-F. Karwaski, M.-C. Blanchard, and W. W Wakarchuk
Characterization of the {alpha}-2,8-polysialyltransferase from Neisseria meningitidis with synthetic acceptors, and the development of a self-priming polysialyltransferase fusion enzyme
Glycobiology, February 1, 2008; 18(2): 177 - 186.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
H. Tsukamoto, Y. Takakura, T. Mine, and T. Yamamoto
Photobacterium sp. JT-ISH-224 Produces Two Sialyltransferases, {alpha}-/{beta}-Galactoside {alpha}2,3-Sialyltransferase and {beta}-Galactoside {alpha}2,6-Sialyltransferase
J. Biochem., February 1, 2008; 143(2): 187 - 197.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. L. Fox, A. D. Cox, M. Gilbert, W. W. Wakarchuk, J. Li, K. Makepeace, J. C. Richards, E. R. Moxon, and D. W. Hood
Identification of a Bifunctional Lipopolysaccharide Sialyltransferase in Haemophilus influenzae: INCORPORATION OF DISIALIC ACID
J. Biol. Chem., December 29, 2006; 281(52): 40024 - 40032.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. E. Deadman, S. L. Lundstrom, E. K. H. Schweda, E. R. Moxon, and D. W. Hood
Specific Amino Acids of the Glycosyltransferase LpsA Direct the Addition of Glucose or Galactose to the Terminal Inner Core Heptose of Haemophilus influenzae Lipopolysaccharide via Alternative Linkages
J. Biol. Chem., October 6, 2006; 281(40): 29455 - 29467.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
M. Packiam, D. M. Shell, S. V. Liu, Y.-B. Liu, D. J. McGee, R. Srivastava, S. Seal, and R. F. Rest
Differential Expression and Transcriptional Analysis of the {alpha}-2,3-Sialyltransferase Gene in Pathogenic Neisseria spp.
Infect. Immun., May 1, 2006; 74(5): 2637 - 2650.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
S. Gulati, A. Cox, L. A. Lewis, F. St. Michael, J. Li, R. Boden, S. Ram, and P. A. Rice
Enhanced Factor H Binding to Sialylated Gonococci Is Restricted to the Sialylated Lacto-N-Neotetraose Lipooligosaccharide Species: Implications for Serum Resistance and Evidence for a Bifunctional Lipooligosaccharide Sialyltransferase in Gonococci
Infect. Immun., November 1, 2005; 73(11): 7390 - 7397.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
A. Harduin-Lepers, R. Mollicone, P. Delannoy, and R. Oriol
The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach
Glycobiology, August 1, 2005; 15(8): 805 - 817.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
T. J. Inzana, G. Glindemann, A. D. Cox, W. Wakarchuk, and M. D. Howard
Incorporation of N-Acetylneuraminic Acid into Haemophilus somnus Lipooligosaccharide (LOS): Enhancement of Resistance to Serum and Reduction of LOS Antibody Binding
Infect. Immun., September 1, 2002; 70(9): 4870 - 4879.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Ouzzine, S. Gulberti, N. Levoin, P. Netter, J. Magdalou, and S. Fournel-Gigleux
The Donor Substrate Specificity of the Human beta 1,3-Glucuronosyltransferase I toward UDP-Glucuronic Acid Is Determined by Two Crucial Histidine and Arginine Residues
J. Biol. Chem., July 5, 2002; 277(28): 25439 - 25445.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
C.-M. Tsai, G. Kao, and P. Zhu
Influence of the Length of the Lipooligosaccharide {alpha} Chain on Its Sialylation in Neisseria meningitidis
Infect. Immun., January 1, 2002; 70(1): 407 - 411.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Toivonen, O. Aitio, and O. Renkonen
alpha 2,3-Sialylation of Terminal GalNAcbeta 1-3Gal Determinants by ST3Gal II Reveals the Multifunctionality of the Enzyme. THE RESULTING Neu5Acalpha 2-3GalNAc LINKAGE IS RESISTANT TO SIALIDASES FROM NEWCASTLE DISEASE VIRUS AND STREPTOCOCCUS PNEUMONIAE
J. Biol. Chem., September 28, 2001; 276(40): 37141 - 37148.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.