Utilizing the O-antigen lipopolysaccharide biosynthesis pathway in Escherichia coli to interrogate the substrate specificities of exogenous glycosyltransferase genes in a combinatorial approach.
Identifieur interne : 000099 ( PubMed/Checkpoint ); précédent : 000098; suivant : 000100Utilizing the O-antigen lipopolysaccharide biosynthesis pathway in Escherichia coli to interrogate the substrate specificities of exogenous glycosyltransferase genes in a combinatorial approach.
Auteurs : Eric B. Johansen [États-Unis] ; Francis C. Szoka ; Anthony Zaleski ; Michael A. Apicella ; Bradford W. GibsonSource :
- Glycobiology [ 1460-2423 ] ; 2010.
Descripteurs français
- KwdFr :
- Antigènes O (), Antigènes O (biosynthèse), Antigènes O (génétique), Conformation des glucides, Escherichia coli (métabolisme), Glycosyltransferase (génétique), Glycosyltransferase (métabolisme), Haemophilus influenzae (enzymologie), Haemophilus influenzae (génétique), Spécificité du substrat, Séquence glucidique, Test ELISA, Vecteurs génétiques (génétique).
- MESH :
- biosynthèse : Antigènes O.
- enzymologie : Haemophilus influenzae.
- génétique : Antigènes O, Glycosyltransferase, Haemophilus influenzae, Vecteurs génétiques.
- métabolisme : Escherichia coli, Glycosyltransferase.
- Antigènes O, Conformation des glucides, Spécificité du substrat, Séquence glucidique, Test ELISA.
English descriptors
- KwdEn :
- Carbohydrate Conformation, Carbohydrate Sequence, Enzyme-Linked Immunosorbent Assay, Escherichia coli (metabolism), Genetic Vectors (genetics), Glycosyltransferases (genetics), Glycosyltransferases (metabolism), Haemophilus influenzae (enzymology), Haemophilus influenzae (genetics), O Antigens (biosynthesis), O Antigens (chemistry), O Antigens (genetics), Substrate Specificity.
- MESH :
- chemical , biosynthesis : O Antigens.
- chemical , chemistry : O Antigens.
- chemical , genetics : Glycosyltransferases, O Antigens.
- enzymology : Haemophilus influenzae.
- genetics : Genetic Vectors, Haemophilus influenzae.
- metabolism : Escherichia coli, Glycosyltransferases.
- Carbohydrate Conformation, Carbohydrate Sequence, Enzyme-Linked Immunosorbent Assay, Substrate Specificity.
Abstract
In previous work, our laboratory generated novel chimeric lipopolysaccharides (LPS) in Escherichia coli transformed with a plasmid containing exogenous lipooligosaccharide synthesis genes (lsg) from Haemophilus influenzae. Analysis of these novel oligosaccharide-LPS chimeras allowed characterization of the carbohydrate structures generated by several putative glycosyltransferase genes within the lsg locus. Here, we adapted this strategy to construct a modular approach to study the synthetic properties of individual glycosyltransferases expressed alone and in combinations. To this end, a set of expression vectors containing one to four putative glycosyltransferase genes from the lsg locus, lsgC-F, were transformed into E. coli K12 (XL-1) which is defective in LPS O-antigen biosynthesis. This strategy relied on the inclusion of the H. influenzae gene product lsgG in every plasmid construct, which partially rescues the E. coli LPS biosynthesis defect by priming uridine diphosphate-undecaprenyl in the WecA-dependent O-antigen synthetic pathway with N-acetyl-glucosamine (GlcNAc). This GlcNAc-undecaprenyl then served as an acceptor substrate for further carbohydrate extension by transformed glycosyltransferases. The resultant LPS-linked chimeric glycans were isolated from their E. coli constructs and characterized by mass spectrometry, methylation analysis and enzyme-linked immunosorbent assays. These structural data allowed the specificity of various glycosyltransferases to be unambiguously assigned to individual genes. LsgF was found to transfer a galactose (Gal) to terminal GlcNAc. LsgE was found to transfer GlcNAc to Gal-GlcNAc, and both LsgF and LsgD were found to transfer Gal to GlcNAc-Gal-GlcNAc but with differing linkage specificities. This method can be generalized and readily adapted to study the substrate specificity of other putative or uncharacterized glycosyltransferases.
DOI: 10.1093/glycob/cwq033
PubMed: 20208062
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:20208062Le document en format XML
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Gibson</name></author></analytic><series><title level="j">Glycobiology</title><idno type="eISSN">1460-2423</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carbohydrate Conformation</term><term>Carbohydrate Sequence</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Escherichia coli (metabolism)</term><term>Genetic Vectors (genetics)</term><term>Glycosyltransferases (genetics)</term><term>Glycosyltransferases (metabolism)</term><term>Haemophilus influenzae (enzymology)</term><term>Haemophilus influenzae (genetics)</term><term>O Antigens (biosynthesis)</term><term>O Antigens (chemistry)</term><term>O Antigens (genetics)</term><term>Substrate Specificity</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antigènes O ()</term><term>Antigènes O (biosynthèse)</term><term>Antigènes O (génétique)</term><term>Conformation des glucides</term><term>Escherichia coli (métabolisme)</term><term>Glycosyltransferase (génétique)</term><term>Glycosyltransferase (métabolisme)</term><term>Haemophilus influenzae (enzymologie)</term><term>Haemophilus influenzae (génétique)</term><term>Spécificité du substrat</term><term>Séquence glucidique</term><term>Test ELISA</term><term>Vecteurs génétiques (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>O Antigens</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>O Antigens</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glycosyltransferases</term><term>O Antigens</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Antigènes O</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Haemophilus influenzae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Haemophilus influenzae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Genetic Vectors</term><term>Haemophilus influenzae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Antigènes O</term><term>Glycosyltransferase</term><term>Haemophilus influenzae</term><term>Vecteurs génétiques</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Glycosyltransferases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Glycosyltransferase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Carbohydrate Conformation</term><term>Carbohydrate Sequence</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Antigènes O</term><term>Conformation des glucides</term><term>Spécificité du substrat</term><term>Séquence glucidique</term><term>Test ELISA</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In previous work, our laboratory generated novel chimeric lipopolysaccharides (LPS) in Escherichia coli transformed with a plasmid containing exogenous lipooligosaccharide synthesis genes (lsg) from Haemophilus influenzae. Analysis of these novel oligosaccharide-LPS chimeras allowed characterization of the carbohydrate structures generated by several putative glycosyltransferase genes within the lsg locus. Here, we adapted this strategy to construct a modular approach to study the synthetic properties of individual glycosyltransferases expressed alone and in combinations. To this end, a set of expression vectors containing one to four putative glycosyltransferase genes from the lsg locus, lsgC-F, were transformed into E. coli K12 (XL-1) which is defective in LPS O-antigen biosynthesis. This strategy relied on the inclusion of the H. influenzae gene product lsgG in every plasmid construct, which partially rescues the E. coli LPS biosynthesis defect by priming uridine diphosphate-undecaprenyl in the WecA-dependent O-antigen synthetic pathway with N-acetyl-glucosamine (GlcNAc). This GlcNAc-undecaprenyl then served as an acceptor substrate for further carbohydrate extension by transformed glycosyltransferases. The resultant LPS-linked chimeric glycans were isolated from their E. coli constructs and characterized by mass spectrometry, methylation analysis and enzyme-linked immunosorbent assays. These structural data allowed the specificity of various glycosyltransferases to be unambiguously assigned to individual genes. LsgF was found to transfer a galactose (Gal) to terminal GlcNAc. LsgE was found to transfer GlcNAc to Gal-GlcNAc, and both LsgF and LsgD were found to transfer Gal to GlcNAc-Gal-GlcNAc but with differing linkage specificities. This method can be generalized and readily adapted to study the substrate specificity of other putative or uncharacterized glycosyltransferases.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">20208062</PMID><DateCreated><Year>2010</Year><Month>05</Month><Day>14</Day></DateCreated><DateCompleted><Year>2010</Year><Month>09</Month><Day>16</Day></DateCompleted><DateRevised><Year>2014</Year><Month>12</Month><Day>04</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2423</ISSN><JournalIssue CitedMedium="Internet"><Volume>20</Volume><Issue>6</Issue><PubDate><Year>2010</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Glycobiology</Title><ISOAbbreviation>Glycobiology</ISOAbbreviation></Journal><ArticleTitle>Utilizing the O-antigen lipopolysaccharide biosynthesis pathway in Escherichia coli to interrogate the substrate specificities of exogenous glycosyltransferase genes in a combinatorial approach.</ArticleTitle><Pagination><MedlinePgn>763-74</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/glycob/cwq033</ELocationID><Abstract><AbstractText>In previous work, our laboratory generated novel chimeric lipopolysaccharides (LPS) in Escherichia coli transformed with a plasmid containing exogenous lipooligosaccharide synthesis genes (lsg) from Haemophilus influenzae. Analysis of these novel oligosaccharide-LPS chimeras allowed characterization of the carbohydrate structures generated by several putative glycosyltransferase genes within the lsg locus. Here, we adapted this strategy to construct a modular approach to study the synthetic properties of individual glycosyltransferases expressed alone and in combinations. To this end, a set of expression vectors containing one to four putative glycosyltransferase genes from the lsg locus, lsgC-F, were transformed into E. coli K12 (XL-1) which is defective in LPS O-antigen biosynthesis. This strategy relied on the inclusion of the H. influenzae gene product lsgG in every plasmid construct, which partially rescues the E. coli LPS biosynthesis defect by priming uridine diphosphate-undecaprenyl in the WecA-dependent O-antigen synthetic pathway with N-acetyl-glucosamine (GlcNAc). This GlcNAc-undecaprenyl then served as an acceptor substrate for further carbohydrate extension by transformed glycosyltransferases. The resultant LPS-linked chimeric glycans were isolated from their E. coli constructs and characterized by mass spectrometry, methylation analysis and enzyme-linked immunosorbent assays. These structural data allowed the specificity of various glycosyltransferases to be unambiguously assigned to individual genes. LsgF was found to transfer a galactose (Gal) to terminal GlcNAc. LsgE was found to transfer GlcNAc to Gal-GlcNAc, and both LsgF and LsgD were found to transfer Gal to GlcNAc-Gal-GlcNAc but with differing linkage specificities. This method can be generalized and readily adapted to study the substrate specificity of other putative or uncharacterized glycosyltransferases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Johansen</LastName><ForeName>Eric B</ForeName><Initials>EB</Initials><AffiliationInfo><Affiliation>Department of Pharmaceutical Chemistry and Pharmaceutical Sciences, University of California, San Francisco, CA 94143, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Szoka</LastName><ForeName>Francis C</ForeName><Initials>FC</Initials></Author><Author ValidYN="Y"><LastName>Zaleski</LastName><ForeName>Anthony</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Apicella</LastName><ForeName>Michael A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Gibson</LastName><ForeName>Bradford W</ForeName><Initials>BW</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>AI024616</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM61851</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI024616</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI024616-21A1</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>03</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Glycobiology</MedlineTA><NlmUniqueID>9104124</NlmUniqueID><ISSNLinking>0959-6658</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019081">O Antigens</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.-</RegistryNumber><NameOfSubstance UI="D016695">Glycosyltransferases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2000 Feb 18;275(7):4747-58</RefSource><PMID Version="1">10671507</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Chem Commun (Camb). 2005 May 28;(20):2558-60</RefSource><PMID Version="1">15900325</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 2000 Oct 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Version="1">8894399</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Trends Biochem Sci. 2004 Dec;29(12):656-63</RefSource><PMID Version="1">15544952</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Microbiol. 2000 Jun;36(5):1059-70</RefSource><PMID Version="1">10844691</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N" UI="D002236">Carbohydrate Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D002240">Carbohydrate Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D004797">Enzyme-Linked Immunosorbent Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D004926">Escherichia coli</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D005822">Genetic Vectors</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000235">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D016695">Glycosyltransferases</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000235">genetics</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D006193">Haemophilus influenzae</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000201">enzymology</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000235">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D019081">O Antigens</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000096">biosynthesis</QualifierName><QualifierName MajorTopicYN="N" UI="Q000737">chemistry</QualifierName><QualifierName MajorTopicYN="N" UI="Q000235">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D013379">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC2900885</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="aheadofprint"><Year>2010</Year><Month>3</Month><Day>5</Day></PubMedPubDate><PubMedPubDate PubStatus="aheadofprint"><Year>2010</Year><Month>4</Month><Day>9</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>3</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>3</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>9</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pii">cwq033</ArticleId><ArticleId IdType="doi">10.1093/glycob/cwq033</ArticleId><ArticleId IdType="pubmed">20208062</ArticleId><ArticleId IdType="pmc">PMC2900885</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><noCountry><name sortKey="Apicella, Michael A" sort="Apicella, Michael A" uniqKey="Apicella M" first="Michael A" last="Apicella">Michael A. Apicella</name><name sortKey="Gibson, Bradford W" sort="Gibson, Bradford W" uniqKey="Gibson B" first="Bradford W" last="Gibson">Bradford W. Gibson</name><name sortKey="Szoka, Francis C" sort="Szoka, Francis C" uniqKey="Szoka F" first="Francis C" last="Szoka">Francis C. Szoka</name><name sortKey="Zaleski, Anthony" sort="Zaleski, Anthony" uniqKey="Zaleski A" first="Anthony" last="Zaleski">Anthony Zaleski</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Johansen, Eric B" sort="Johansen, Eric B" uniqKey="Johansen E" first="Eric B" last="Johansen">Eric B. Johansen</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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