M
Michael Wacker
Researcher at ETH Zurich
Publications - 19
Citations - 2177
Michael Wacker is an academic researcher from ETH Zurich. The author has contributed to research in topics: Glycosylation & Oligosaccharyltransferase. The author has an hindex of 14, co-authored 19 publications receiving 2063 citations. Previous affiliations of Michael Wacker include GlaxoSmithKline & École Polytechnique Fédérale de Lausanne.
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Journal ArticleDOI
N-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli
Michael Wacker,Dennis Linton,Paul G. Hitchen,Mihai Nita-Lazar,Stuart M. Haslam,Simon J. North,Maria Panico,Howard R. Morris,Anne Dell,Brendan W. Wren,Markus Aebi +10 more
TL;DR: It is demonstrated that a functional N-linked glycosylation pathway could be transferred into Escherichia coli and opened up the possibility of engineering permutations of recombinant glycan structures for research and industrial applications.
Journal ArticleDOI
Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli.
Mario F. Feldman,Michael Wacker,Marcela Hernandez,Paul G. Hitchen,Cristina L. Marolda,Michael Kowarik,Howard R. Morris,Anne Dell,Miguel A. Valvano,Markus Aebi +9 more
TL;DR: E. coli cells are engineered in a way that two different pathways, protein N-glycosylation and lipopolysaccharide (LPS) biosynthesis, converge at the step in which PglB, the key enzyme of the C. jejuni N-gresylation system, transfers O polysaccharides from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein.
Journal ArticleDOI
Definition of the bacterial N-glycosylation site consensus sequence.
Michael Kowarik,N. Martin Young,Shin Numao,Benjamin L. Schulz,Isabelle Hug,Nico Callewaert,Dominic C Mills,David C. Watson,Marcela Hernandez,John F. Kelly,Michael Wacker,Markus Aebi +11 more
TL;DR: Bacterial N‐glycosylation site selection is more specific than the eukaryotic equivalent with respect to the polypeptide acceptor sequence.
Journal ArticleDOI
Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems
Michael Wacker,Mario F. Feldman,Nico Callewaert,Michael Kowarik,Bradley R. Clarke,Nicola L. B. Pohl,Marcela Hernandez,Enrique D. Vinés,Miguel A. Valvano,Chris Whitfield,Markus Aebi +10 more
TL;DR: The elucidation of the mechanism of action and the substrate specificity of PglB represents the foundation for engineering glycoproteins that will have an impact on biotechnology.
Journal ArticleDOI
The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation
TL;DR: The data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes.