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Kowarik M, Wetter M, Haeuptle MA, Braun M, Steffen M, Kemmler S, Ravenscroft N, De Benedetto G, Zuppiger M, Sirena D, Cescutti P, Wacker M
The development and characterization of an E. coli O25B bioconjugate vaccine
Glycoconjugate Journal 38(4) (2021)
421-435
|
a-L-Rhap-(1-3)-+
|
-4)-a-D-Glcp-(1-3)-a-L-Rhap2Ac-(1-3)-b-D-GlcpNAc-(1-
|
b-D-Glcp-(1-6)-+ |
Show graphically |
Escherichia coli O25B UPEC138
(Ancestor NCBI TaxID 1095709,
species name lookup)
Escherichia coli O25B-EPA
(Ancestor NCBI TaxID 1095709,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: meningitis [ICD11:
1D01 
];
urinary tract infections (UTI) [ICD11:
GC08 ];
infection due to Escherichia coli [ICD11:
XN6P4 ]
The structure was elucidated in this paperNCBI PubMed ID: 33730261Publication DOI: 10.1007/s10719-021-09985-9Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: michael.kowarik
lmtbio.com
Institutions: GlycoVaxyn AG, Grabenstrasse 3, 8952, Schlieren, Switzerland, Department of Chemistry, University of Cape Town, Rondebosch, 7701, South Africa, LimmaTech Biologics AG, Grabenstrasse 3, 8952, Schlieren, Switzerland, Institute of Microbiology, ETH Zurich, Vladimir-Prelog-Weg 1-5/10, 8093, Zurich, Switzerland, Molecular Partners AG, Wagistrasse 14, 8952, Schlieren, Switzerland, Numab Therapeutics AG, Einsiedlerstrasse 34, 8820, Wadenswil, Switzerland, Dip. di Scienze della Vita, University di Trieste, 34127, Trieste, Italy, National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Hertfordshire, EN6 3QG, UK, Wacker Biotech Consulting AG, Heuelstrasse 22, 8800, Thalwil, Switzerland
Extraintestinal pathogenic Escherichia coli (ExPEC) cause a wide range of clinical diseases such as bacteremia and urinary tract infections. The increase of multidrug resistant ExPEC strains is becoming a major concern for the treatment of these infections and E. coli has been identified as a critical priority pathogen by the WHO. Therefore, the development of vaccines has become increasingly important, with the surface lipopolysaccharide constituting a promising vaccine target. This study presents genetic and structural analysis of clinical urine isolates from Switzerland belonging to the serotype O25. Approximately 75% of these isolates were shown to correspond to the substructure O25B only recently described in an emerging clone of E. coli sequence type 131. To address the high occurrence of O25B in clinical isolates, an O25B glycoconjugate vaccine was prepared using an E. coli glycosylation system. The O antigen cluster was integrated into the genome of E. coli W3110, thereby generating an E. coli strain able to synthesize the O25B polysaccharide on a carrier lipid. The polysaccharide was enzymatically conjugated to specific asparagine side chains of the carrier protein exotoxin A (EPA) of Pseudomonas aeruginosa by the PglB oligosaccharyltransferase from Campylobacter jejuni. Detailed characterization of the O25B-EPA conjugate by use of physicochemical methods including NMR and GC-MS confirmed the O25B polysaccharide structure in the conjugate, opening up the possibility to develop a multivalent E. coli conjugate vaccine containing O25B-EPA.
Escherichia coli, physicochemical characterization, bioconjugate vaccine, serotype O25B, ST131
Structure type: polymer chemical repeating unit
Location inside paper: p. 426, Fig. 1b, table 1, p. 432, O25B
Compound class: O-antigen
Contained glycoepitopes: IEDB_130422,IEDB_135813,IEDB_136105,IEDB_137340,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_158539,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, NMR-2D, GC-MS, SDS-PAGE, sugar analysis, GC, de-O-acetylation, genetic methods, immunoblotting, RP-HPLC, MALDI-MS/MS, bioconjugation, HPAEC-CD
Comments, role: recombinant E. coli W3110 (ΔgtrABS; ΔrfbW3110::rfbO25B; ΔwaaL; p970 (pglB) and p1076 (EPA)) were used for O25B-EPA.
Related record ID(s): 9661, 10889
NCBI Taxonomy refs (TaxIDs): 1095709Reference(s) to other database(s): GTC:G56482HV
Show glycosyltransferases
NMR conditions: in D2O at 303 K
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6
3,3,3 aLRhap 101.4 70.9 70.8 72.9 69.4 17.4
3,3,6 bDGlcp 102.7 73.7 77.1 70.8 77.1 61.7
3,3 aDGlcp 96.8 73.3 76.8 73.2 70.4 67.5
3,2 Ac 173.6 21.0
3 aLRhap 99.4 69.0 73.3 70.9 69.4 17.1
2 Ac 175.1 22.8
bDGlcpN 100.5 56.3 81.5 69.5 77.0 61.9
1H NMR data:
Linkage Residue H1 H2 H3 H4 H5 H6
3,3,3 aLRhap 5.24 4.04 3.88 3.45 4.44 1.31
3,3,6 bDGlcp 4.53 3.30 3.48 3.38 3.45 3.74-3.94
3,3 aDGlcp 4.95 3.67 3.95 3.87 4.17 3.76-4.15
3,2 Ac - 2.13
3 aLRhap 4.93 5.21 3.93 3.60 4.07 1.26
2 Ac - 2.02
bDGlcpN 4.59 3.83 3.63 3.45 3.44 3.79
1H/13C HSQC data:
Linkage Residue C1/H1 C2/H2 C3/H3 C4/H4 C5/H5 C6/H6
3,3,3 aLRhap 101.4/5.24 70.9/4.04 70.8/3.88 72.9/3.45 69.4/4.44 17.4/1.31
3,3,6 bDGlcp 102.7/4.53 73.7/3.30 77.1/3.48 70.8/3.38 77.1/3.45 61.7/3.74-3.94
3,3 aDGlcp 96.8/4.95 73.3/3.67 76.8/3.95 73.2/3.87 70.4/4.17 67.5/3.76-4.15
3,2 Ac 21.0/2.13
3 aLRhap 99.4/4.93 69.0/5.21 73.3/3.93 70.9/3.60 69.4/4.07 17.1/1.26
2 Ac 22.8/2.02
bDGlcpN 100.5/4.59 56.3/3.83 81.5/3.63 69.5/3.45 77.0/3.44 61.9/3.79
1H NMR data:
| Linkage | Residue | H1 | H2 | H3 | H4 | H5 | H6 |
|---|
| 3,3,3 | aLRhap | 5.24 | 4.04 | 3.88 | 3.45 | 4.44 | 1.31 |
| 3,3,6 | bDGlcp | 4.53 | 3.30 | 3.48 | 3.38 | 3.45 | 3.74
3.94 |
| 3,3 | aDGlcp | 4.95 | 3.67 | 3.95 | 3.87 | 4.17 | 3.76
4.15 |
| 3,2 | Ac |
| 2.13 | |
| 3 | aLRhap | 4.93 | 5.21 | 3.93 | 3.60 | 4.07 | 1.26 |
| 2 | Ac |
| 2.02 | |
| | bDGlcpN | 4.59 | 3.83 | 3.63 | 3.45 | 3.44 | 3.79 |
|
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 |
|---|
| 3,3,3 | aLRhap | 101.4 | 70.9 | 70.8 | 72.9 | 69.4 | 17.4 |
| 3,3,6 | bDGlcp | 102.7 | 73.7 | 77.1 | 70.8 | 77.1 | 61.7 |
| 3,3 | aDGlcp | 96.8 | 73.3 | 76.8 | 73.2 | 70.4 | 67.5 |
| 3,2 | Ac | 173.6 | 21.0 | |
| 3 | aLRhap | 99.4 | 69.0 | 73.3 | 70.9 | 69.4 | 17.1 |
| 2 | Ac | 175.1 | 22.8 | |
| | bDGlcpN | 100.5 | 56.3 | 81.5 | 69.5 | 77.0 | 61.9 |
|
There is only one chemically distinct structure:
Expand this record
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Kowarik M, Wetter M, Haeuptle MA, Braun M, Steffen M, Kemmler S, Ravenscroft N, De Benedetto G, Zuppiger M, Sirena D, Cescutti P, Wacker M
The development and characterization of an E. coli O25B bioconjugate vaccine
Glycoconjugate Journal 38(4) (2021)
421-435
|
a-L-Rhap-(1-3)-+
|
-4)-a-D-Glcp-(1-3)-a-L-Rhap-(1-3)-b-D-GlcpNAc-(1-
|
b-D-Glcp-(1-6)-+ |
Show graphically |
Escherichia coli O25B UPEC138
(Ancestor NCBI TaxID 1095709,
species name lookup)
Escherichia coli O25B-EPA
(Ancestor NCBI TaxID 1095709,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: meningitis [ICD11:
1D01 ];
urinary tract infections (UTI) [ICD11:
GC08 ];
infection due to Escherichia coli [ICD11:
XN6P4 ]
The structure was elucidated in this paperNCBI PubMed ID: 33730261Publication DOI: 10.1007/s10719-021-09985-9Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: michael.kowarik
lmtbio.com
Institutions: GlycoVaxyn AG, Grabenstrasse 3, 8952, Schlieren, Switzerland, Department of Chemistry, University of Cape Town, Rondebosch, 7701, South Africa, LimmaTech Biologics AG, Grabenstrasse 3, 8952, Schlieren, Switzerland, Institute of Microbiology, ETH Zurich, Vladimir-Prelog-Weg 1-5/10, 8093, Zurich, Switzerland, Molecular Partners AG, Wagistrasse 14, 8952, Schlieren, Switzerland, Numab Therapeutics AG, Einsiedlerstrasse 34, 8820, Wadenswil, Switzerland, Dip. di Scienze della Vita, University di Trieste, 34127, Trieste, Italy, National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Hertfordshire, EN6 3QG, UK, Wacker Biotech Consulting AG, Heuelstrasse 22, 8800, Thalwil, Switzerland
Extraintestinal pathogenic Escherichia coli (ExPEC) cause a wide range of clinical diseases such as bacteremia and urinary tract infections. The increase of multidrug resistant ExPEC strains is becoming a major concern for the treatment of these infections and E. coli has been identified as a critical priority pathogen by the WHO. Therefore, the development of vaccines has become increasingly important, with the surface lipopolysaccharide constituting a promising vaccine target. This study presents genetic and structural analysis of clinical urine isolates from Switzerland belonging to the serotype O25. Approximately 75% of these isolates were shown to correspond to the substructure O25B only recently described in an emerging clone of E. coli sequence type 131. To address the high occurrence of O25B in clinical isolates, an O25B glycoconjugate vaccine was prepared using an E. coli glycosylation system. The O antigen cluster was integrated into the genome of E. coli W3110, thereby generating an E. coli strain able to synthesize the O25B polysaccharide on a carrier lipid. The polysaccharide was enzymatically conjugated to specific asparagine side chains of the carrier protein exotoxin A (EPA) of Pseudomonas aeruginosa by the PglB oligosaccharyltransferase from Campylobacter jejuni. Detailed characterization of the O25B-EPA conjugate by use of physicochemical methods including NMR and GC-MS confirmed the O25B polysaccharide structure in the conjugate, opening up the possibility to develop a multivalent E. coli conjugate vaccine containing O25B-EPA.
Escherichia coli, physicochemical characterization, bioconjugate vaccine, serotype O25B, ST131
Structure type: polymer chemical repeating unit
Location inside paper: p. 426, Fig. 1b, table 1, p. 432, O25B
Compound class: O-antigen
Contained glycoepitopes: IEDB_135813,IEDB_136105,IEDB_137340,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_158539,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, NMR-2D, GC-MS, SDS-PAGE, sugar analysis, GC, de-O-acetylation, genetic methods, immunoblotting, RP-HPLC, MALDI-MS/MS, bioconjugation, HPAEC-CD
Comments, role: O-deacetylated polysaccharide; recombinant E. coli W3110 (ΔgtrABS; ΔrfbW3110::rfbO25B; ΔwaaL; p970 (pglB) and p1076 (EPA)) were used for O25B-EPA.
Related record ID(s): 9660, 10889
NCBI Taxonomy refs (TaxIDs): 1095709
Show glycosyltransferases
NMR conditions: in D2O at 303 K
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6
3,3,3 aLRhap 101.4 70.9 70.8 72.9 69.4 17.4
3,3,6 bDGlcp 102.7 73.7 77.1 70.8 77.1 61.7
3,3 aDGlcp 96.8 73.3 76.8 73.2 70.4 67.5
3 aLRhap 101.8 68.6 76.9 70.9 69.6 17.2
2 Ac 175.1 22.8
bDGlcpN 100.5 56.3 81.5 69.5 77.0 61.9
1H NMR data:
Linkage Residue H1 H2 H3 H4 H5 H6
3,3,3 aLRhap 5.24 4.04 3.88 3.45 4.44 1.31
3,3,6 bDGlcp 4.53 3.30 3.48 3.38 3.45 3.74-3.94
3,3 aDGlcp 4.95 3.67 3.95 3.87 4.17 3.76-4.15
3 aLRhap 4.90 3.96 3.74 3.54 4.00 1.24
2 Ac - 2.02
bDGlcpN 4.59 3.83 3.63 3.45 3.44 3.79
1H/13C HSQC data:
Linkage Residue C1/H1 C2/H2 C3/H3 C4/H4 C5/H5 C6/H6
3,3,3 aLRhap 101.4/5.24 70.9/4.04 70.8/3.88 72.9/3.45 69.4/4.44 17.4/1.31
3,3,6 bDGlcp 102.7/4.53 73.7/3.30 77.1/3.48 70.8/3.38 77.1/3.45 61.7/3.74-3.94
3,3 aDGlcp 96.8/4.95 73.3/3.67 76.8/3.95 73.2/3.87 70.4/4.17 67.5/3.76-4.15
3 aLRhap 101.8/4.90 68.6/3.96 76.9/3.74 70.9/3.54 69.6/4.00 17.2/1.24
2 Ac 22.8/2.02
bDGlcpN 100.5/4.59 56.3/3.83 81.5/3.63 69.5/3.45 77.0/3.44 61.9/3.79
1H NMR data:
| Linkage | Residue | H1 | H2 | H3 | H4 | H5 | H6 |
|---|
| 3,3,3 | aLRhap | 5.24 | 4.04 | 3.88 | 3.45 | 4.44 | 1.31 |
| 3,3,6 | bDGlcp | 4.53 | 3.30 | 3.48 | 3.38 | 3.45 | 3.74
3.94 |
| 3,3 | aDGlcp | 4.95 | 3.67 | 3.95 | 3.87 | 4.17 | 3.76
4.15 |
| 3 | aLRhap | 4.90 | 3.96 | 3.74 | 3.54 | 4.00 | 1.24 |
| 2 | Ac |
| 2.02 | |
| | bDGlcpN | 4.59 | 3.83 | 3.63 | 3.45 | 3.44 | 3.79 |
|
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 |
|---|
| 3,3,3 | aLRhap | 101.4 | 70.9 | 70.8 | 72.9 | 69.4 | 17.4 |
| 3,3,6 | bDGlcp | 102.7 | 73.7 | 77.1 | 70.8 | 77.1 | 61.7 |
| 3,3 | aDGlcp | 96.8 | 73.3 | 76.8 | 73.2 | 70.4 | 67.5 |
| 3 | aLRhap | 101.8 | 68.6 | 76.9 | 70.9 | 69.6 | 17.2 |
| 2 | Ac | 175.1 | 22.8 | |
| | bDGlcpN | 100.5 | 56.3 | 81.5 | 69.5 | 77.0 | 61.9 |
|
There is only one chemically distinct structure:
Expand this record
Collapse this record
Kowarik M, Wetter M, Haeuptle MA, Braun M, Steffen M, Kemmler S, Ravenscroft N, De Benedetto G, Zuppiger M, Sirena D, Cescutti P, Wacker M
The development and characterization of an E. coli O25B bioconjugate vaccine
Glycoconjugate Journal 38(4) (2021)
421-435
|
a-L-Rhap-(1-3)-+
|
-4)-a-D-Glcp-(1-3)-a-L-FucpNAc-(1-3)-b-D-GlcpNAc-(1-
|
b-D-Glcp-(1-6)-+ |
Show graphically |
Escherichia coli O25A UPEC436
(Ancestor NCBI TaxID 1095709,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: meningitis [ICD11:
1D01 ];
urinary tract infections (UTI) [ICD11:
GC08 ];
infection due to Escherichia coli [ICD11:
XN6P4 ]
The structure was elucidated in this paperNCBI PubMed ID: 33730261Publication DOI: 10.1007/s10719-021-09985-9Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: michael.kowarik
lmtbio.com
Institutions: GlycoVaxyn AG, Grabenstrasse 3, 8952, Schlieren, Switzerland, Department of Chemistry, University of Cape Town, Rondebosch, 7701, South Africa, LimmaTech Biologics AG, Grabenstrasse 3, 8952, Schlieren, Switzerland, Institute of Microbiology, ETH Zurich, Vladimir-Prelog-Weg 1-5/10, 8093, Zurich, Switzerland, Molecular Partners AG, Wagistrasse 14, 8952, Schlieren, Switzerland, Numab Therapeutics AG, Einsiedlerstrasse 34, 8820, Wadenswil, Switzerland, Dip. di Scienze della Vita, University di Trieste, 34127, Trieste, Italy, National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Hertfordshire, EN6 3QG, UK, Wacker Biotech Consulting AG, Heuelstrasse 22, 8800, Thalwil, Switzerland
Extraintestinal pathogenic Escherichia coli (ExPEC) cause a wide range of clinical diseases such as bacteremia and urinary tract infections. The increase of multidrug resistant ExPEC strains is becoming a major concern for the treatment of these infections and E. coli has been identified as a critical priority pathogen by the WHO. Therefore, the development of vaccines has become increasingly important, with the surface lipopolysaccharide constituting a promising vaccine target. This study presents genetic and structural analysis of clinical urine isolates from Switzerland belonging to the serotype O25. Approximately 75% of these isolates were shown to correspond to the substructure O25B only recently described in an emerging clone of E. coli sequence type 131. To address the high occurrence of O25B in clinical isolates, an O25B glycoconjugate vaccine was prepared using an E. coli glycosylation system. The O antigen cluster was integrated into the genome of E. coli W3110, thereby generating an E. coli strain able to synthesize the O25B polysaccharide on a carrier lipid. The polysaccharide was enzymatically conjugated to specific asparagine side chains of the carrier protein exotoxin A (EPA) of Pseudomonas aeruginosa by the PglB oligosaccharyltransferase from Campylobacter jejuni. Detailed characterization of the O25B-EPA conjugate by use of physicochemical methods including NMR and GC-MS confirmed the O25B polysaccharide structure in the conjugate, opening up the possibility to develop a multivalent E. coli conjugate vaccine containing O25B-EPA.
Escherichia coli, physicochemical characterization, bioconjugate vaccine, serotype O25B, ST131
Structure type: polymer chemical repeating unit
Location inside paper: p. 426, Fig. 1b, O25A
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_135813,IEDB_136105,IEDB_137340,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, NMR-2D, GC-MS, SDS-PAGE, sugar analysis, GC, de-O-acetylation, genetic methods, immunoblotting, RP-HPLC, MALDI-MS/MS, bioconjugation, HPAEC-CD
Related record ID(s): 9660, 9661
NCBI Taxonomy refs (TaxIDs): 1095709Reference(s) to other database(s): GTC:G18223OD, GlycomeDB:
28106
Show glycosyltransferases
There is only one chemically distinct structure:
Expand this record
Collapse this record
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