Glycans‐by‐design: Engineering bacteria for the biosynthesis of complex glycans and glycoconjugates
Identifieur interne : 000690 ( Main/Exploration ); précédent : 000689; suivant : 000691Glycans‐by‐design: Engineering bacteria for the biosynthesis of complex glycans and glycoconjugates
Auteurs : Judith H. Merritt [États-Unis] ; Anne A. Ollis [États-Unis] ; Adam C. Fisher [États-Unis] ; Matthew P. Delisa [États-Unis]Source :
- Biotechnology and Bioengineering [ 0006-3592 ] ; 2013-06.
Descripteurs français
- Wicri :
- topic : Biotechnologie, Glucose, Vaccin.
English descriptors
- KwdEn :
- Acceptor, Acceptor site, Acidic residue, Acra, Aebi, Amino, Amino acid, Asparagine residues, Bacteria, Bacterial glycoengineering, Bacterial glycolipids, Bacterial glycosylation, Bacterial oligosaccharyltransferase, Bacteriol, Bioengineering, Biol, Biosynthesis, Biotechnology, Campylobacter, Campylobacter jejuni, Carbohydrate, Cell surface, Chem, Colanic, Coli, Conjugation, Core oligosaccharide, Core saccharide, Engineering glycans, Enterica, Escherichia, Escherichia coli, Eukaryote, Eukaryotic, Eukaryotic glycoproteins, Faridmoayer, Feldman, Glucose, Glycan, Glycan synthesis, Glycans, Glycobiology, Glycoengineered, Glycoengineered bacteria, Glycoengineering, Glycolipids, Glycoprotein, Glycosylation, Glycosyltransferases, Hmw1c homolog, Ihssen, Inner membrane, Jejuni, Jejuni pglb, June, Lari pglb, Lgta, Lgtb, Lgte, Lipid, Lipid carrier, Lipopolysaccharide, Lizak, Microbiol, Monosaccharide, Neisseria, Nothaft, Nucleotide, Nucleotide sugar transporters, Nucleotide sugars, Oligosaccharide, Oligosaccharyltransferase, Osts, Pathway, Paton, Periplasm, Pglb, Polysaccharide, Priem, Proc natl acad, Protein glycosylation, Recent review, Recombinant, Saccharide, Samain, Schwarz, Small number, Subunit, Szymanski, Target proteins, Therapeutic glycoproteins, Transporter, Typhimurium, Vaccine, Wacker, Yavuz.
- Teeft :
- Acceptor, Acceptor site, Acidic residue, Acra, Aebi, Amino, Amino acid, Asparagine residues, Bacteria, Bacterial glycoengineering, Bacterial glycolipids, Bacterial glycosylation, Bacterial oligosaccharyltransferase, Bacteriol, Bioengineering, Biol, Biosynthesis, Biotechnology, Campylobacter, Campylobacter jejuni, Carbohydrate, Cell surface, Chem, Colanic, Coli, Conjugation, Core oligosaccharide, Core saccharide, Engineering glycans, Enterica, Escherichia, Escherichia coli, Eukaryote, Eukaryotic, Eukaryotic glycoproteins, Faridmoayer, Feldman, Glucose, Glycan, Glycan synthesis, Glycans, Glycobiology, Glycoengineered, Glycoengineered bacteria, Glycoengineering, Glycolipids, Glycoprotein, Glycosylation, Glycosyltransferases, Hmw1c homolog, Ihssen, Inner membrane, Jejuni, Jejuni pglb, June, Lari pglb, Lgta, Lgtb, Lgte, Lipid, Lipid carrier, Lipopolysaccharide, Lizak, Microbiol, Monosaccharide, Neisseria, Nothaft, Nucleotide, Nucleotide sugar transporters, Nucleotide sugars, Oligosaccharide, Oligosaccharyltransferase, Osts, Pathway, Paton, Periplasm, Pglb, Polysaccharide, Priem, Proc natl acad, Protein glycosylation, Recent review, Recombinant, Saccharide, Samain, Schwarz, Small number, Subunit, Szymanski, Target proteins, Therapeutic glycoproteins, Transporter, Typhimurium, Vaccine, Wacker, Yavuz.
Abstract
There is an urgent need for new tools that enable better understanding of the structure, recognition, metabolism, and biosynthesis of glycans as well as the production of biologically important glycans and glycoconjugates. With the discovery of glycoprotein synthesis in bacteria and functional transfer of glycosylation pathways between species, Escherichia coli cells have become a tractable host for both understanding glycosylation and the underlying glycan code of living cells as well as for expressing glycoprotein therapeutics and vaccines. Here, we review recent efforts to harness natural biological pathways and engineer synthetic designer pathways in bacteria for making complex glycans and conjugating these to lipids and proteins. The result of these efforts has been a veritable transformation of bacteria into living factories for scalable, bottom‐up production of complex glycoconjugates by design. Biotechnol. Bioeng. 2013; 110: 1550–1564. © 2013 Wiley Periodicals, Inc.
Url:
DOI: 10.1002/bit.24885
Affiliations:
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Merritt</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Glycobia, Inc., Ithaca</wicri:cityArea></affiliation></author><author><name sortKey="Ollis, Anne A" sort="Ollis, Anne A" uniqKey="Ollis A" first="Anne A." last="Ollis">Anne A. Ollis</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>School of Chemical and Biomolecular Engineering, Cornell University, 254 Olin Hall, Ithaca</wicri:cityArea></affiliation></author><author><name sortKey="Fisher, Adam C" sort="Fisher, Adam C" uniqKey="Fisher A" first="Adam C." last="Fisher">Adam C. 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Delisa</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>School of Chemical and Biomolecular Engineering, Cornell University, 254 Olin Hall, Ithaca</wicri:cityArea></affiliation><affiliation wicri:level="1"><country wicri:rule="url">États-Unis</country></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Correspondence address: School of Chemical and Biomolecular Engineering, Cornell University, 254 Olin Hall, Ithaca</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Biotechnology and Bioengineering</title><title level="j" type="alt">BIOTECHNOLOGY AND BIOENGINEERING</title><idno type="ISSN">0006-3592</idno><idno type="eISSN">1097-0290</idno><imprint><biblScope unit="vol">110</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1550">1550</biblScope><biblScope unit="page" to="1564">1564</biblScope><biblScope unit="page-count">15</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2013-06">2013-06</date></imprint><idno type="ISSN">0006-3592</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-3592</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acceptor</term><term>Acceptor site</term><term>Acidic residue</term><term>Acra</term><term>Aebi</term><term>Amino</term><term>Amino acid</term><term>Asparagine residues</term><term>Bacteria</term><term>Bacterial glycoengineering</term><term>Bacterial glycolipids</term><term>Bacterial glycosylation</term><term>Bacterial oligosaccharyltransferase</term><term>Bacteriol</term><term>Bioengineering</term><term>Biol</term><term>Biosynthesis</term><term>Biotechnology</term><term>Campylobacter</term><term>Campylobacter jejuni</term><term>Carbohydrate</term><term>Cell surface</term><term>Chem</term><term>Colanic</term><term>Coli</term><term>Conjugation</term><term>Core oligosaccharide</term><term>Core saccharide</term><term>Engineering glycans</term><term>Enterica</term><term>Escherichia</term><term>Escherichia coli</term><term>Eukaryote</term><term>Eukaryotic</term><term>Eukaryotic glycoproteins</term><term>Faridmoayer</term><term>Feldman</term><term>Glucose</term><term>Glycan</term><term>Glycan synthesis</term><term>Glycans</term><term>Glycobiology</term><term>Glycoengineered</term><term>Glycoengineered bacteria</term><term>Glycoengineering</term><term>Glycolipids</term><term>Glycoprotein</term><term>Glycosylation</term><term>Glycosyltransferases</term><term>Hmw1c homolog</term><term>Ihssen</term><term>Inner membrane</term><term>Jejuni</term><term>Jejuni pglb</term><term>June</term><term>Lari pglb</term><term>Lgta</term><term>Lgtb</term><term>Lgte</term><term>Lipid</term><term>Lipid carrier</term><term>Lipopolysaccharide</term><term>Lizak</term><term>Microbiol</term><term>Monosaccharide</term><term>Neisseria</term><term>Nothaft</term><term>Nucleotide</term><term>Nucleotide sugar transporters</term><term>Nucleotide sugars</term><term>Oligosaccharide</term><term>Oligosaccharyltransferase</term><term>Osts</term><term>Pathway</term><term>Paton</term><term>Periplasm</term><term>Pglb</term><term>Polysaccharide</term><term>Priem</term><term>Proc natl acad</term><term>Protein glycosylation</term><term>Recent review</term><term>Recombinant</term><term>Saccharide</term><term>Samain</term><term>Schwarz</term><term>Small number</term><term>Subunit</term><term>Szymanski</term><term>Target proteins</term><term>Therapeutic glycoproteins</term><term>Transporter</term><term>Typhimurium</term><term>Vaccine</term><term>Wacker</term><term>Yavuz</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Acceptor</term><term>Acceptor site</term><term>Acidic residue</term><term>Acra</term><term>Aebi</term><term>Amino</term><term>Amino acid</term><term>Asparagine residues</term><term>Bacteria</term><term>Bacterial glycoengineering</term><term>Bacterial glycolipids</term><term>Bacterial glycosylation</term><term>Bacterial oligosaccharyltransferase</term><term>Bacteriol</term><term>Bioengineering</term><term>Biol</term><term>Biosynthesis</term><term>Biotechnology</term><term>Campylobacter</term><term>Campylobacter jejuni</term><term>Carbohydrate</term><term>Cell surface</term><term>Chem</term><term>Colanic</term><term>Coli</term><term>Conjugation</term><term>Core oligosaccharide</term><term>Core saccharide</term><term>Engineering glycans</term><term>Enterica</term><term>Escherichia</term><term>Escherichia coli</term><term>Eukaryote</term><term>Eukaryotic</term><term>Eukaryotic glycoproteins</term><term>Faridmoayer</term><term>Feldman</term><term>Glucose</term><term>Glycan</term><term>Glycan synthesis</term><term>Glycans</term><term>Glycobiology</term><term>Glycoengineered</term><term>Glycoengineered bacteria</term><term>Glycoengineering</term><term>Glycolipids</term><term>Glycoprotein</term><term>Glycosylation</term><term>Glycosyltransferases</term><term>Hmw1c homolog</term><term>Ihssen</term><term>Inner membrane</term><term>Jejuni</term><term>Jejuni pglb</term><term>June</term><term>Lari pglb</term><term>Lgta</term><term>Lgtb</term><term>Lgte</term><term>Lipid</term><term>Lipid carrier</term><term>Lipopolysaccharide</term><term>Lizak</term><term>Microbiol</term><term>Monosaccharide</term><term>Neisseria</term><term>Nothaft</term><term>Nucleotide</term><term>Nucleotide sugar transporters</term><term>Nucleotide sugars</term><term>Oligosaccharide</term><term>Oligosaccharyltransferase</term><term>Osts</term><term>Pathway</term><term>Paton</term><term>Periplasm</term><term>Pglb</term><term>Polysaccharide</term><term>Priem</term><term>Proc natl acad</term><term>Protein glycosylation</term><term>Recent review</term><term>Recombinant</term><term>Saccharide</term><term>Samain</term><term>Schwarz</term><term>Small number</term><term>Subunit</term><term>Szymanski</term><term>Target proteins</term><term>Therapeutic glycoproteins</term><term>Transporter</term><term>Typhimurium</term><term>Vaccine</term><term>Wacker</term><term>Yavuz</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Biotechnologie</term><term>Glucose</term><term>Vaccin</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">There is an urgent need for new tools that enable better understanding of the structure, recognition, metabolism, and biosynthesis of glycans as well as the production of biologically important glycans and glycoconjugates. With the discovery of glycoprotein synthesis in bacteria and functional transfer of glycosylation pathways between species, Escherichia coli cells have become a tractable host for both understanding glycosylation and the underlying glycan code of living cells as well as for expressing glycoprotein therapeutics and vaccines. Here, we review recent efforts to harness natural biological pathways and engineer synthetic designer pathways in bacteria for making complex glycans and conjugating these to lipids and proteins. The result of these efforts has been a veritable transformation of bacteria into living factories for scalable, bottom‐up production of complex glycoconjugates by design. Biotechnol. Bioeng. 2013; 110: 1550–1564. © 2013 Wiley Periodicals, Inc.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><country name="États-Unis"><region name="État de New York"><name sortKey="Merritt, Judith H" sort="Merritt, Judith H" uniqKey="Merritt J" first="Judith H." last="Merritt">Judith H. Merritt</name></region><name sortKey="Delisa, Matthew P" sort="Delisa, Matthew P" uniqKey="Delisa M" first="Matthew P." last="Delisa">Matthew P. Delisa</name><name sortKey="Delisa, Matthew P" sort="Delisa, Matthew P" uniqKey="Delisa M" first="Matthew P." last="Delisa">Matthew P. Delisa</name><name sortKey="Delisa, Matthew P" sort="Delisa, Matthew P" uniqKey="Delisa M" first="Matthew P." last="Delisa">Matthew P. Delisa</name><name sortKey="Fisher, Adam C" sort="Fisher, Adam C" uniqKey="Fisher A" first="Adam C." last="Fisher">Adam C. Fisher</name><name sortKey="Ollis, Anne A" sort="Ollis, Anne A" uniqKey="Ollis A" first="Anne A." last="Ollis">Anne A. Ollis</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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