Ghent University Academic Bibliography

Advanced

Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides

C Alaimo, I Catrein, L Morf, CL Marolda, Nico Callewaert UGent, MA Valvano, MF Feldman and M Aebi (2006) EMBO JOURNAL. 25(5). p.967-976
abstract
Translocation of lipid-linked oligosaccharide (LLO) intermediates across membranes is an essential but poorly understood process in eukaryotic and bacterial glycosylation pathways. Membrane proteins defined as translocases or flippases are implicated to mediate the translocation reaction. The membrane protein Wzx has been proposed to mediate the translocation across the plasma membrane of lipopolysaccharide (LPS) O antigen subunits, which are assembled on an undecaprenyl pyrophosphate lipid carrier. Similarly, PglK (formerly WlaB) is a Campylobacter jejuni-encoded ABC-type transporter proposed to mediate the translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate involved in the recently identified bacterial N-linked protein glycosylation pathway. A combination of genetic and carbohydrate structural analyses defined and characterized flippase activities in the C. jejuni N-linked protein glycosylation and the Escherichia coli LPS O antigen biosynthesis. PglK displayed relaxed substrate specificity with respect to the oligosaccharide structure of the LLO intermediate and complemented a wzx deficiency in E. coli O-antigen biosynthesis. Our experiments provide strong genetic evidence that LLO translocation across membranes can be catalyzed by two distinct proteins that do not share any sequence similarity.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
ENTEROBACTERIAL COMMON ANTIGEN, O-SPECIFIC LIPOPOLYSACCHARIDE, ESCHERICHIA-COLI K-12, ENDOPLASMIC-RETICULUM, CAMPYLOBACTER-JEJUNI, P-GLYCOPROTEIN, GENE-CLUSTER, O7-SPECIFIC LIPOPOLYSACCHARIDE, PROTEIN GLYCOSYLATION, BIOSYNTHESIS REGION, ABC transporter, flippase, N-linked glycosylation, O antigen
journal title
EMBO JOURNAL
Embo J.
volume
25
issue
5
pages
967 - 976
Web of Science type
Article
Web of Science id
000236225400005
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
10.086 (2006)
JCR rank
16/259 (2006)
JCR quartile
1 (2006)
ISSN
0261-4189
DOI
10.1038/sj.emboj.7601024
language
English
UGent publication?
no
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1203342
handle
http://hdl.handle.net/1854/LU-1203342
date created
2011-04-06 12:11:03
date last changed
2016-12-19 15:45:49
@article{1203342,
  abstract     = {Translocation of lipid-linked oligosaccharide (LLO) intermediates across membranes is an essential but poorly understood process in eukaryotic and bacterial glycosylation pathways. Membrane proteins defined as translocases or flippases are implicated to mediate the translocation reaction. The membrane protein Wzx has been proposed to mediate the translocation across the plasma membrane of lipopolysaccharide (LPS) O antigen subunits, which are assembled on an undecaprenyl pyrophosphate lipid carrier. Similarly, PglK (formerly WlaB) is a Campylobacter jejuni-encoded ABC-type transporter proposed to mediate the translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate involved in the recently identified bacterial N-linked protein glycosylation pathway. A combination of genetic and carbohydrate structural analyses defined and characterized flippase activities in the C. jejuni N-linked protein glycosylation and the Escherichia coli LPS O antigen biosynthesis. PglK displayed relaxed substrate specificity with respect to the oligosaccharide structure of the LLO intermediate and complemented a wzx deficiency in E. coli O-antigen biosynthesis. Our experiments provide strong genetic evidence that LLO translocation across membranes can be catalyzed by two distinct proteins that do not share any sequence similarity.},
  author       = {Alaimo, C and Catrein, I and Morf, L and Marolda, CL and Callewaert, Nico and Valvano, MA and Feldman, MF and Aebi, M},
  issn         = {0261-4189},
  journal      = {EMBO JOURNAL},
  keyword      = {ENTEROBACTERIAL COMMON ANTIGEN,O-SPECIFIC LIPOPOLYSACCHARIDE,ESCHERICHIA-COLI K-12,ENDOPLASMIC-RETICULUM,CAMPYLOBACTER-JEJUNI,P-GLYCOPROTEIN,GENE-CLUSTER,O7-SPECIFIC LIPOPOLYSACCHARIDE,PROTEIN GLYCOSYLATION,BIOSYNTHESIS REGION,ABC transporter,flippase,N-linked glycosylation,O antigen},
  language     = {eng},
  number       = {5},
  pages        = {967--976},
  title        = {Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides},
  url          = {http://dx.doi.org/10.1038/sj.emboj.7601024},
  volume       = {25},
  year         = {2006},
}

Chicago
Alaimo, C, I Catrein, L Morf, CL Marolda, Nico Callewaert, MA Valvano, MF Feldman, and M Aebi. 2006. “Two Distinct but Interchangeable Mechanisms for Flipping of Lipid-linked Oligosaccharides.” Embo Journal 25 (5): 967–976.
APA
Alaimo, C., Catrein, I., Morf, L., Marolda, C., Callewaert, N., Valvano, M., Feldman, M., et al. (2006). Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides. EMBO JOURNAL, 25(5), 967–976.
Vancouver
1.
Alaimo C, Catrein I, Morf L, Marolda C, Callewaert N, Valvano M, et al. Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides. EMBO JOURNAL. 2006;25(5):967–76.
MLA
Alaimo, C, I Catrein, L Morf, et al. “Two Distinct but Interchangeable Mechanisms for Flipping of Lipid-linked Oligosaccharides.” EMBO JOURNAL 25.5 (2006): 967–976. Print.