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1. (CSDB ID: 10870) | report error |
| -4)-b-D-Quip3NAc-(1-3)-b-D-Ribf-(1-4)-b-D-Galp-(1-3)-a-D-GalpNAc-(1- | Show graphically |
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Escherichia coli O5
(NCBI TaxID 1010795,
species name lookup)
]
nankai.edu.cn; fenglu63nankai.edu.cnExtraintestinal pathogenic Escherichia coli (ExPEC) has presented a major clinical infection emerged in the past decades. O-polysaccharide (OPS)-based glycoconjugate vaccines produced using the bacterial glycosylation machinery can be utilized to confer protection against such infection. However, constructing a low-cost microbial cell factory for high-efficient production of OPS-based glycoconjugate vaccines remains challenging. Here, we engineered a glyco-optimized chassis strain by reprogramming metabolic network. The yield was enhanced to 38.6 mg L-1, the highest level reported so far. MS analysis showed that designed glycosylation sequon was modified by target polysaccharide with high glycosylation efficiency of 90.7 % and 76.7 % for CTB-O5 and CTB-O7, respectively. The glycoconjugate vaccines purified from this biosystem elicited a marked increase in protection against ExPEC infection in mouse model, compared to a non-optimized system. The glyco-optimized platform established here is broadly suitable for polysaccharide-based conjugate production against ExPEC and other surface-polysaccharide-producing pathogens.
O-polysaccharide, glycoconjugate vaccine, ExPEC, glyco-optimized chassis strain, glycosylation efficiency, sugar to protein ratio
Structure type: suggested polymer biological repeating unit|
2. (CSDB ID: 10871) | report error |
| a-L-Rhap-(1-3)-+ | -3)-b-D-Quip4NAc-(1-2)-a-D-Manp-(1-4)-b-D-Galp-(1-3)-a-D-GlcpNAc-(1- | Show graphically |
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Escherichia coli O7
(NCBI TaxID 2162916,
species name lookup)
]nankai.edu.cn; fenglu63nankai.edu.cnExtraintestinal pathogenic Escherichia coli (ExPEC) has presented a major clinical infection emerged in the past decades. O-polysaccharide (OPS)-based glycoconjugate vaccines produced using the bacterial glycosylation machinery can be utilized to confer protection against such infection. However, constructing a low-cost microbial cell factory for high-efficient production of OPS-based glycoconjugate vaccines remains challenging. Here, we engineered a glyco-optimized chassis strain by reprogramming metabolic network. The yield was enhanced to 38.6 mg L-1, the highest level reported so far. MS analysis showed that designed glycosylation sequon was modified by target polysaccharide with high glycosylation efficiency of 90.7 % and 76.7 % for CTB-O5 and CTB-O7, respectively. The glycoconjugate vaccines purified from this biosystem elicited a marked increase in protection against ExPEC infection in mouse model, compared to a non-optimized system. The glyco-optimized platform established here is broadly suitable for polysaccharide-based conjugate production against ExPEC and other surface-polysaccharide-producing pathogens.
O-polysaccharide, glycoconjugate vaccine, ExPEC, glyco-optimized chassis strain, glycosylation efficiency, sugar to protein ratio
Structure type: suggested polymer biological repeating unit|
3. (CSDB ID: 22333) | report error |
| b-D-GlcpNAc-(1-2)-+ | b-D-Galp-(1-4)-+ | | | -3)-b-D-Galp-(1-4)-b-D-Glcp-(1-3)-b-D-GalpNAc-(1- | Show graphically |
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Escherichia coli MGD12
(Ancestor NCBI TaxID 562,
species name lookup)
Escherichia coli O21
(NCBI TaxID 2162911,
species name lookup)
]nankai.edu.cn>; B. Liu <liubin1981nankai.edu.cn>Glycoproteins, in which polysaccharides are usually attached to proteins, are an important class of biomolecules that are widely used as therapeutic agents in clinical treatments for decades. Uropathogenic Escherichia coli (UPEC) O21 has been identified as a serogroup that induces urinary tract infections, with a global increasing number among women and young children. Therefore, there is an urgent need to establish protective vaccines against UPEC infection. Herein, we engineered non-pathogenic E. coli MG1655 to achieve robust, cost-effective de novo biosynthesis of O21 O-antigen polysaccharide-based glycoprotein against UPEC O21. Specifically, this glycoengineered E. coli MG1655 was manipulated for high-efficient glucose-glycerol co-utilization and for the gene cluster installation and O-glycosylation machinery assembly. The key pathways of UDP-sugar precursors were also strengthened to enforce more carbon flux towards the glycosyl donors, which enhanced the glycoprotein titer by 5.6-fold. Further optimization of culture conditions yielded glycoproteins of up to 35.34 mg/L. Glycopeptide MS confirmed the preciset biosynthesis of glycoprotein. This glycoprotein elicited antigen-specific IgG immune responses and significantly reduced kidney and bladder colonization. This bacterial cell-based glyco-platform and optimized strategies can provide a guideline for the biosynthesis of other value-added glycoproteins.
polysaccharides, glycoprotein, protein glycosylation, O21 O-antigen gene cluster, UDP-sugar precursors, Urinary tract infections (UTI)
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