Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on April 21, 2006
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
281/16/11186    most recent
M513772200v1
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 PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lewis, A. L.
Right arrow Articles by Nizet, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lewis, A. L.
Right arrow Articles by Nizet, V.
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?

Papers In Press, published online ahead of print February 20, 2006
J. Biol. Chem, 10.1074/jbc.M513772200
Submitted on December 27, 2005
Accepted on February 20, 2006

The group B Streptococcal sialic acid o-acetyltransferase is encoded by neuD, a conserved component of bacterial sialic acid biosynthetic gene clusters

Amanda L. Lewis, Mary E. Hensler, Ajit Varki, and Victor Nizet

Dept. of Pediatrics, University of California, San Diego School of Medicine, La Jolla, CA 92093-0687

Corresponding Author: vnizet{at}ucsd.edu

Nearly two-dozen microbial pathogens have surface polysaccharides or lipooligosaccharides that contain sialic acid (Sia), and several Sia-dependent virulence mechanisms are known to enhance bacterial survival or result in host tissue injury. Some pathogens are also known to O-acetylate their Sias, although the role of this modification in pathogenesis remains unclear. Here we report that neuD, a gene located within the Group B Streptococcus (GBS) Sia biosynthetic gene cluster, encodes a Sia O-acetyltransferase that is itself required for capsular polysaccharide (CPS) sialylation. Homology modeling and site-directed mutagenesis identified Lys123 as a critical residue for Sia O-acetyltransferase activity. Moreover, a single nucleotide polymorphism in neuD can determine whether GBS displays a “high” or “low” Sia O-acetylation phenotype. Complementation analysis revealed that Escherichia coli K1 NeuD also functions as a Sia O-acetyltransferase in GBS. In fact, NeuD homologs are commonly found within Sia biosynthetic gene clusters. A bioinformatic approach identified 18 bacterial species with a Sia biosynthetic gene cluster that included neuD. Included in this list are the sialylated human pathogens Legionella pneumophila, Vibrio parahaemolyticus, Pseudomonas aeruginosa, and Campylobacter jejuni, as well as an additional twelve bacterial species never before analyzed for Sia expression. Phylogenetic analysis shows that NeuD homologs of sialylated pathogens share a common evolutionary lineage distinct from the poly-Sia O-acetyltransferase of E. coli K1. These studies define a molecular genetic approach for the selective elimination of GBS Sia O-acetylation without concurrent loss of sialylation – a key to further studies addressing the role(s) of this modification in bacterial virulence.


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
 J. Biol. Chem.Home page
A. K. Bergfeld, H. Claus, N. K. Lorenzen, F. Spielmann, U. Vogel, and M. Muhlenhoff
The Polysialic Acid-specific O-Acetyltransferase OatC from Neisseria meningitidis Serogroup C Evolved Apart from Other Bacterial Sialate O-Acetyltransferases
J. Biol. Chem., January 2, 2009; 284(1): 6 - 16.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. B. Olivier and B. Imperiali
Crystal Structure and Catalytic Mechanism of PglD from Campylobacter jejuni
J. Biol. Chem., October 10, 2008; 283(41): 27937 - 27946.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. L. Lewis, H. Cao, S. K. Patel, S. Diaz, W. Ryan, A. F. Carlin, V. Thon, W. G. Lewis, A. Varki, X. Chen, et al.
NeuA Sialic Acid O-Acetylesterase Activity Modulates O-Acetylation of Capsular Polysaccharide in Group B Streptococcus
J. Biol. Chem., September 21, 2007; 282(38): 27562 - 27571.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
E. Severi, D. W. Hood, and G. H. Thomas
Sialic acid utilization by bacterial pathogens
Microbiology, September 1, 2007; 153(9): 2817 - 2822.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. K. Bergfeld, H. Claus, U. Vogel, and M. Muhlenhoff
Biochemical Characterization of Thepolysialic Acid-specific O-Acetyltransferase NeuO of Escherichia coli K1
J. Biol. Chem., July 27, 2007; 282(30): 22217 - 22227.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
J. R. Bishop and P. Gagneux
Evolution of carbohydrate antigens--microbial forces shaping host glycomes?
Glycobiology, May 1, 2007; 17(5): 23R - 34R.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
M. L. Warwas, J. N. Watson, A. J. Bennet, and M. M. Moore
Structure and role of sialic acids on the surface of Aspergillus fumigatus conidiospores
Glycobiology, April 1, 2007; 17(4): 401 - 410.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
A. F. Carlin, A. L. Lewis, A. Varki, and V. Nizet
Group B Streptococcal Capsular Sialic Acids Interact with Siglecs (Immunoglobulin-Like Lectins) on Human Leukocytes
J. Bacteriol., February 15, 2007; 189(4): 1231 - 1237.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
S. M. Steenbergen, Y.-C. Lee, W. F. Vann, J. Vionnet, L. F. Wright, and E. R. Vimr
Separate Pathways for O Acetylation of Polymeric and Monomeric Sialic Acids and Identification of Sialyl O-Acetyl Esterase in Escherichia coli K1.
J. Bacteriol., September 1, 2006; 188(17): 6195 - 6206.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement