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Shanks, R.M., Caiazza, N.C., Hinsa, S.M., Toutain, C.M. Universal Genetic Assay for Engineering Extracellular Protein Expression. Mechanism of bacterial oligosaccharyltransferase: in vitro quantification of sequon binding and catalysis. Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements. Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase. Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni. Linton, D., Allan, E., Karlyshev, A.V., Cronshaw, A.D. Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli. Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli. N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. Production of secretory and extracellular N-linked glycoproteins in Escherichia coli. Glycoengineering of host mimicking type-2 LacNAc polymers and Lewis X antigens on bacterial cell surfaces. An engineered eukaryotic protein glycosylation pathway in Escherichia coli. The Escherichia coli glycophage display system. A filamentous phage display system for N-linked glycoproteins. Çelik, E., Fisher, A.C., Guarino, C., Mansell, T.J. Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB. Inverse metabolic engineering to improve Escherichia coli as an N-glycosylation host. Definition of the bacterial N-glycosylation site consensus sequence. Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation. X-ray structure of a bacterial oligosaccharyltransferase. Lizak, C., Gerber, S., Numao, S., Aebi, M. STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Protein glycosylation in bacterial mucosal pathogens.
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Mechanisms and principles of N-linked protein glycosylation. Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea. N-glycan structures: recognition and processing in the ER. N-linked oligosaccharides as outfitters for glycoprotein folding, form and function.
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Biological roles of oligosaccharides: all of the theories are correct. Roles of N-linked glycans in the endoplasmic reticulum. Intracellular functions of N-linked glycans. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Zielinska, D.F., Gnad, F., Wisniewski, J.R. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. These results underscore the utility of glycoSNAP for shedding light on poorly understood aspects of N-linked glycosylation and for engineering designer N-linked glycosylation biocatalysts.Īpweiler, R., Hermjakob, H. jejuni PglB variants that could glycosylate an array of noncanonical acceptor sequences, including one in a eukaryotic N-glycoprotein.
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This involved creation of a genetic assay, glycosylation of secreted N-linked acceptor proteins (glycoSNAP), that facilitates high-throughput screening of glycophenotypes in E. Here we sought to identify sequence determinants in the oligosaccharyltransferase PglB that restrict its specificity to only those glycan acceptor sites containing a negatively charged residue at the −2 position relative to asparagine. This machinery has been functionally transferred into Escherichia coli, enabling convenient mechanistic dissection of the N-linked glycosylation process in this genetically tractable host. The Campylobacter jejuni protein glycosylation locus ( pgl) encodes machinery for asparagine-linked ( N-linked) glycosylation and serves as the archetype for bacterial N-linked glycosylation.