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Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems

M Wacker, MF Feldman, Nico Callewaert UGent, M Kowarik, BR Clarke, NL Pohl, M Hernandez, ED Vines, MA Valvano, C Whitfield, et al. (2006) PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 103(18). p.7088-7093
abstract
The PgIB oligosaccharyltransferase (OTase) of Campylobacter jejuni can be functionally expressed in Escherichia coli, and its relaxed oligosaccharide substrate specificity allows the transfer of different glycans from the lipid carrier undecaprenyl pyrophosphate to an acceptor protein. To investigate the substrate specificity of PgIB, we tested the transfer of a set of lipid-linked polysaccharides in E. coli and Salmonella enterica serovar Typhimurium. A hexose linked to the C-6 of the monosaccharide at the reducing end did not inhibit the transfer of the O antigen to the acceptor protein. However, PgIB required an acetamido group at the C-2. A model for the mechanism of PgIB involving this functional group was proposed. Previous experiments have shown that eukaryotic OTases have the same requirement, suggesting that eukaryotic and prokaryotic OTases catalyze the transfer of oligosaccharides by a conserved mechanism. Moreover, we demonstrated the functional transfer of the C. jejuni glycosylation system into S. enterica. The elucidation of the mechanism of action and the substrate specificity of PgIB represents the foundation for engineering glycoproteins that will have an impact on biotechnology.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
BINDING CASSETTE TRANSPORTER, N-LINKED GLYCOSYLATION, COLI SEROTYPE K30, RFB GENE-CLUSTER, ESCHERICHIA-COLI, CAMPYLOBACTER-JEJUNI, O-ANTIGEN, ASSISTED CATALYSIS, CAPSULAR POLYSACCHARIDE, PROTEIN GLYCOSYLATION, glycoengineering, glycoproteins, LPS, PgIB, Stt3p
journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Proc. Natl. Acad. Sci. U. S. A.
volume
103
issue
18
pages
7088 - 7093
Web of Science type
Article
Web of Science id
000237399900055
JCR category
MULTIDISCIPLINARY SCIENCES
JCR impact factor
9.643 (2006)
JCR rank
3/50 (2006)
JCR quartile
1 (2006)
ISSN
0027-8424
DOI
10.1073/pnas.0509207103
language
English
UGent publication?
no
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1203379
handle
http://hdl.handle.net/1854/LU-1203379
date created
2011-04-06 12:17:17
date last changed
2016-12-19 15:45:14
@article{1203379,
  abstract     = {The PgIB oligosaccharyltransferase (OTase) of Campylobacter jejuni can be functionally expressed in Escherichia coli, and its relaxed oligosaccharide substrate specificity allows the transfer of different glycans from the lipid carrier undecaprenyl pyrophosphate to an acceptor protein. To investigate the substrate specificity of PgIB, we tested the transfer of a set of lipid-linked polysaccharides in E. coli and Salmonella enterica serovar Typhimurium. A hexose linked to the C-6 of the monosaccharide at the reducing end did not inhibit the transfer of the O antigen to the acceptor protein. However, PgIB required an acetamido group at the C-2. A model for the mechanism of PgIB involving this functional group was proposed. Previous experiments have shown that eukaryotic OTases have the same requirement, suggesting that eukaryotic and prokaryotic OTases catalyze the transfer of oligosaccharides by a conserved mechanism. Moreover, we demonstrated the functional transfer of the C. jejuni glycosylation system into S. enterica. The elucidation of the mechanism of action and the substrate specificity of PgIB represents the foundation for engineering glycoproteins that will have an impact on biotechnology.},
  author       = {Wacker, M and Feldman, MF and Callewaert, Nico and Kowarik, M and Clarke, BR and Pohl, NL and Hernandez, M and Vines, ED and Valvano, MA and Whitfield, C and Aebi, M},
  issn         = {0027-8424},
  journal      = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
  keyword      = {BINDING CASSETTE TRANSPORTER,N-LINKED GLYCOSYLATION,COLI SEROTYPE K30,RFB GENE-CLUSTER,ESCHERICHIA-COLI,CAMPYLOBACTER-JEJUNI,O-ANTIGEN,ASSISTED CATALYSIS,CAPSULAR POLYSACCHARIDE,PROTEIN GLYCOSYLATION,glycoengineering,glycoproteins,LPS,PgIB,Stt3p},
  language     = {eng},
  number       = {18},
  pages        = {7088--7093},
  title        = {Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems},
  url          = {http://dx.doi.org/10.1073/pnas.0509207103},
  volume       = {103},
  year         = {2006},
}

Chicago
Wacker, M, MF Feldman, Nico Callewaert, M Kowarik, BR Clarke, NL Pohl, M Hernandez, et al. 2006. “Substrate Specificity of Bacterial Oligosaccharyltransferase Suggests a Common Transfer Mechanism for the Bacterial and Eukaryotic Systems.” Proceedings of the National Academy of Sciences of the United States of America 103 (18): 7088–7093.
APA
Wacker, M., Feldman, M., Callewaert, N., Kowarik, M., Clarke, B., Pohl, N., Hernandez, M., et al. (2006). Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 103(18), 7088–7093.
Vancouver
1.
Wacker M, Feldman M, Callewaert N, Kowarik M, Clarke B, Pohl N, et al. Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2006;103(18):7088–93.
MLA
Wacker, M, MF Feldman, Nico Callewaert, et al. “Substrate Specificity of Bacterial Oligosaccharyltransferase Suggests a Common Transfer Mechanism for the Bacterial and Eukaryotic Systems.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 103.18 (2006): 7088–7093. Print.