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Urbach C, Halila S, Guerreiro C, Driguez H, Mulard LA, Armand S
CGTase-catalysed cis-glucosylation of L-rhamnosides for the preparation of Shigella flexneri 2a and 3a haptens
Chembiochem: a European Journal of Chemical Biology 15(2) (2014)
293-300
|
/Variants 0/-+ a-D-Glcp-(1-4)-+
| |
-2)-a-L-Rhap-(1-2)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-GlcpNAc6(%)Ac-(1-
/Variants 0/ is:
?%Ac-4)-
OR (exclusively)
?%Ac-3)- |
Show graphically |
Shigella flexneri 2a
(NCBI TaxID 42897,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: bacillary dysentery [ICD11:
1A02 
, ICD11:
XN7HG ];
infection due to Shigella flexneri [ICD11:
XN7Y2 ]
NCBI PubMed ID: 24376024Publication DOI: 10.1002/cbic.201300597Journal NLM ID: 100937360Publisher: Weinheim, Germany: Wiley Interscience
Correspondence: Sylvie.Armand
cermav.cnrs.fr
Institutions: Centre de Recherches sur les Macromolécules Végétales (CERMAV-CNRS), Affiliated with Grenoble University and the Institut de Chimie Moléculaire de Grenoble, Domaine Universitaire de Grenoble, 601 rue de la Chimie, B.P. 53, 38041 Grenoble cedex 9, France, Institut Pasteur, Unité de Chimie des Biomolécules, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France, NRS UMR 3523, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France
We report the enzymatic synthesis of α-D-glucopyranosyl-(1→4)-α-L-rhamnopyranoside and α-D-glucopyranosyl-(1→3)-α-L-rhamnopyranoside by using a wild-type transglucosidase in combination with glucoamylase and glucose oxidase. It was shown that Bacillus circulans 251 cyclodextrin glucanotransferase (CGTase, EC 2.1.4.19) can efficiently couple an α-L-rhamnosyl acceptor to a maltodextrin molecule with an α-(1→4) linkage, albeit in mixture with the α-(1→3) regioisomer, thus giving two glucosylated acceptors in a single reaction. Optimisation of the CGTase coupling reaction with β-cyclodextrin as the donor substrate and methyl or allyl α-L-rhamnopyranoside as acceptors resulted in good conversion yields (42-70 %) with adjustable glycosylation regioselectivity. Moreover, the efficient chemical conversion of the products of CGTase-mediated cis-glucosylation into protected building blocks (previously used in the synthesis of O-antigen fragments of several Shigella flexneri serotypes) was substantiated. These novel chemoenzymatic strategies towards useful, convenient intermediates in the synthesis of S. flexneri serotypes 2a and 3a oligosaccharides might find applications in developments towards synthetic carbohydrate-based vaccine candidates against bacillary dysentery.
carbohydrates, Shigella flexneri, biocatalysis, cis-glycosylation, cyclodextrin glucanotransferase
Structure type: polymer chemical repeating unit
Location inside paper: p.293, A), SF2a
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_125613,IEDB_125614,IEDB_127514,IEDB_130687,IEDB_133752,IEDB_133753,IEDB_133754,IEDB_135806,IEDB_135807,IEDB_135808,IEDB_135809,IEDB_135813,IEDB_135817,IEDB_135849,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_141815,IEDB_141816,IEDB_142488,IEDB_143253,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_153213,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, TLC, chemical methods, MS, biochemical methods, enzymatic synthesis, cis-glycosylation
Biological activity: kinetic study of the coupling activity
Synthetic data: enzymatic and chemoenzymatic
Related record ID(s): 30520, 30521, 30522
NCBI Taxonomy refs (TaxIDs): 42897
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There is only one chemically distinct structure:
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Urbach C, Halila S, Guerreiro C, Driguez H, Mulard LA, Armand S
CGTase-catalysed cis-glucosylation of L-rhamnosides for the preparation of Shigella flexneri 2a and 3a haptens
Chembiochem: a European Journal of Chemical Biology 15(2) (2014)
293-300
|
a-D-Glcp-(1-3)-+
|
-2)-a-L-Rhap-(1-2)-a-L-Rhap-(1-3)-a-L-Rhap2Ac-(1-3)-b-D-GlcpNAc6(%)Ac-(1- |
Show graphically |
Shigella flexneri 3a
(NCBI TaxID 424717,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: bacillary dysentery [ICD11:
1A02 , ICD11:
XN7HG ];
infection due to Shigella flexneri [ICD11:
XN7Y2 ]
NCBI PubMed ID: 24376024Publication DOI: 10.1002/cbic.201300597Journal NLM ID: 100937360Publisher: Weinheim, Germany: Wiley Interscience
Correspondence: Sylvie.Armand
cermav.cnrs.fr
Institutions: Centre de Recherches sur les Macromolécules Végétales (CERMAV-CNRS), Affiliated with Grenoble University and the Institut de Chimie Moléculaire de Grenoble, Domaine Universitaire de Grenoble, 601 rue de la Chimie, B.P. 53, 38041 Grenoble cedex 9, France, Institut Pasteur, Unité de Chimie des Biomolécules, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France, NRS UMR 3523, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France
We report the enzymatic synthesis of α-D-glucopyranosyl-(1→4)-α-L-rhamnopyranoside and α-D-glucopyranosyl-(1→3)-α-L-rhamnopyranoside by using a wild-type transglucosidase in combination with glucoamylase and glucose oxidase. It was shown that Bacillus circulans 251 cyclodextrin glucanotransferase (CGTase, EC 2.1.4.19) can efficiently couple an α-L-rhamnosyl acceptor to a maltodextrin molecule with an α-(1→4) linkage, albeit in mixture with the α-(1→3) regioisomer, thus giving two glucosylated acceptors in a single reaction. Optimisation of the CGTase coupling reaction with β-cyclodextrin as the donor substrate and methyl or allyl α-L-rhamnopyranoside as acceptors resulted in good conversion yields (42-70 %) with adjustable glycosylation regioselectivity. Moreover, the efficient chemical conversion of the products of CGTase-mediated cis-glucosylation into protected building blocks (previously used in the synthesis of O-antigen fragments of several Shigella flexneri serotypes) was substantiated. These novel chemoenzymatic strategies towards useful, convenient intermediates in the synthesis of S. flexneri serotypes 2a and 3a oligosaccharides might find applications in developments towards synthetic carbohydrate-based vaccine candidates against bacillary dysentery.
carbohydrates, Shigella flexneri, biocatalysis, cis-glycosylation, cyclodextrin glucanotransferase
Structure type: polymer chemical repeating unit
Location inside paper: p.293, B), SF3a
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_125613,IEDB_125614,IEDB_127514,IEDB_130421,IEDB_130422,IEDB_133752,IEDB_133753,IEDB_133754,IEDB_135813,IEDB_135849,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_141815,IEDB_141816,IEDB_142488,IEDB_143253,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_153213,IEDB_158539,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, TLC, chemical methods, MS, biochemical methods, enzymatic synthesis, cis-glycosylation
Biological activity: kinetic study of the coupling activity
Synthetic data: enzymatic and chemoenzymatic
Related record ID(s): 30147, 30521, 30522
NCBI Taxonomy refs (TaxIDs): 424717Reference(s) to other database(s): GTC:G32503HR
Show glycosyltransferases
There is only one chemically distinct structure:
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Urbach C, Halila S, Guerreiro C, Driguez H, Mulard LA, Armand S
CGTase-catalysed cis-glucosylation of L-rhamnosides for the preparation of Shigella flexneri 2a and 3a haptens
Chembiochem: a European Journal of Chemical Biology 15(2) (2014)
293-300
|
/Variants 0/-+
|
a-D-Glcp-(1-4)-a-L-Rhap
/Variants 0/ is:
Me-1)-
OR (exclusively)
Allyl-1)- |
Show graphically |
Shigella flexneri 2a
(NCBI TaxID 42897,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: bacillary dysentery [ICD11:
1A02 , ICD11:
XN7HG ];
infection due to Shigella flexneri [ICD11:
XN7Y2 ]
The structure was elucidated in this paperNCBI PubMed ID: 24376024Publication DOI: 10.1002/cbic.201300597Journal NLM ID: 100937360Publisher: Weinheim, Germany: Wiley Interscience
Correspondence: Sylvie.Armand
cermav.cnrs.fr
Institutions: Centre de Recherches sur les Macromolécules Végétales (CERMAV-CNRS), Affiliated with Grenoble University and the Institut de Chimie Moléculaire de Grenoble, Domaine Universitaire de Grenoble, 601 rue de la Chimie, B.P. 53, 38041 Grenoble cedex 9, France, Institut Pasteur, Unité de Chimie des Biomolécules, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France, NRS UMR 3523, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France
We report the enzymatic synthesis of α-D-glucopyranosyl-(1→4)-α-L-rhamnopyranoside and α-D-glucopyranosyl-(1→3)-α-L-rhamnopyranoside by using a wild-type transglucosidase in combination with glucoamylase and glucose oxidase. It was shown that Bacillus circulans 251 cyclodextrin glucanotransferase (CGTase, EC 2.1.4.19) can efficiently couple an α-L-rhamnosyl acceptor to a maltodextrin molecule with an α-(1→4) linkage, albeit in mixture with the α-(1→3) regioisomer, thus giving two glucosylated acceptors in a single reaction. Optimisation of the CGTase coupling reaction with β-cyclodextrin as the donor substrate and methyl or allyl α-L-rhamnopyranoside as acceptors resulted in good conversion yields (42-70 %) with adjustable glycosylation regioselectivity. Moreover, the efficient chemical conversion of the products of CGTase-mediated cis-glucosylation into protected building blocks (previously used in the synthesis of O-antigen fragments of several Shigella flexneri serotypes) was substantiated. These novel chemoenzymatic strategies towards useful, convenient intermediates in the synthesis of S. flexneri serotypes 2a and 3a oligosaccharides might find applications in developments towards synthetic carbohydrate-based vaccine candidates against bacillary dysentery.
carbohydrates, Shigella flexneri, biocatalysis, cis-glycosylation, cyclodextrin glucanotransferase
Structure type: oligomer
Location inside paper: p.294, scheme 2, compounds 4a and 4b EC-OR [<
>]aDGlcp(1-4)aLRhap
Contained glycoepitopes: IEDB_136105,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, TLC, chemical methods, MS, biochemical methods, enzymatic synthesis, cis-glycosylation
Biological activity: kinetic study of the coupling activity
Enzymes that release or process the structure: cyclodextrin glucanotransferase (CGTase, EC 2.1.4.19) from Bacillus circulans 251, glucoamylase, glucose oxidase, catalase
Synthetic data: enzymatic and chemoenzymatic
Comments, role: synthetic fragment of the O-antigen of S.flexneri 2a
Related record ID(s): 30147, 30520, 30522
NCBI Taxonomy refs (TaxIDs): 42897
Show glycosyltransferases
1H NMR data: present in publication
|
13C NMR data: present in publication
|
There is only one chemically distinct structure:
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Urbach C, Halila S, Guerreiro C, Driguez H, Mulard LA, Armand S
CGTase-catalysed cis-glucosylation of L-rhamnosides for the preparation of Shigella flexneri 2a and 3a haptens
Chembiochem: a European Journal of Chemical Biology 15(2) (2014)
293-300
|
/Variants 0/-+
|
a-D-Glcp-(1-3)-a-L-Rhap
/Variants 0/ is:
Me-1)-
OR (exclusively)
Allyl-1)- |
Show graphically |
Shigella flexneri 3a
(NCBI TaxID 424717,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: bacillary dysentery [ICD11:
1A02 , ICD11:
XN7HG ];
infection due to Shigella flexneri [ICD11:
XN7Y2 ]
The structure was elucidated in this paperNCBI PubMed ID: 24376024Publication DOI: 10.1002/cbic.201300597Journal NLM ID: 100937360Publisher: Weinheim, Germany: Wiley Interscience
Correspondence: Sylvie.Armand
cermav.cnrs.fr
Institutions: Centre de Recherches sur les Macromolécules Végétales (CERMAV-CNRS), Affiliated with Grenoble University and the Institut de Chimie Moléculaire de Grenoble, Domaine Universitaire de Grenoble, 601 rue de la Chimie, B.P. 53, 38041 Grenoble cedex 9, France, Institut Pasteur, Unité de Chimie des Biomolécules, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France, NRS UMR 3523, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France
We report the enzymatic synthesis of α-D-glucopyranosyl-(1→4)-α-L-rhamnopyranoside and α-D-glucopyranosyl-(1→3)-α-L-rhamnopyranoside by using a wild-type transglucosidase in combination with glucoamylase and glucose oxidase. It was shown that Bacillus circulans 251 cyclodextrin glucanotransferase (CGTase, EC 2.1.4.19) can efficiently couple an α-L-rhamnosyl acceptor to a maltodextrin molecule with an α-(1→4) linkage, albeit in mixture with the α-(1→3) regioisomer, thus giving two glucosylated acceptors in a single reaction. Optimisation of the CGTase coupling reaction with β-cyclodextrin as the donor substrate and methyl or allyl α-L-rhamnopyranoside as acceptors resulted in good conversion yields (42-70 %) with adjustable glycosylation regioselectivity. Moreover, the efficient chemical conversion of the products of CGTase-mediated cis-glucosylation into protected building blocks (previously used in the synthesis of O-antigen fragments of several Shigella flexneri serotypes) was substantiated. These novel chemoenzymatic strategies towards useful, convenient intermediates in the synthesis of S. flexneri serotypes 2a and 3a oligosaccharides might find applications in developments towards synthetic carbohydrate-based vaccine candidates against bacillary dysentery.
carbohydrates, Shigella flexneri, biocatalysis, cis-glycosylation, cyclodextrin glucanotransferase
Structure type: oligomer
Location inside paper: p.293, scheme 2, compounds 6a and 6b EA-OR
Contained glycoepitopes: IEDB_136105,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_158539,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, TLC, chemical methods, MS, biochemical methods, enzymatic synthesis, cis-glycosylation
Biological activity: kinetic study of the coupling activity
Enzymes that release or process the structure: cyclodextrin glucanotransferase (CGTase, EC 2.1.4.19) from Bacillus circulans 251, glucoamylase, glucose oxidase, catalase
Synthetic data: enzymatic and chemoenzymatic
Comments, role: synthetic fragment of the O-antigen of S.flexneri 3a
Related record ID(s): 30147, 30520, 30521
NCBI Taxonomy refs (TaxIDs): 424717
Show glycosyltransferases
1H NMR data: present in publication
|
13C NMR data: present in publication
|
There is only one chemically distinct structure:
Expand this record
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