Advances in Bacterial Oligosaccharyltransferase Structure Elucidation and Potential Application to Glycoconjugate Vaccine Design
Glycosylation is one of the most common post-translational modifications of proteins across all kingdoms of life. Diverse monosaccharides and polysaccharides can be attached to a range of amino acid residues generating N-glycosylation, O-glycosylation, C-glycosylation, S-glycosylation, as well as P-...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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IMR Press
2023-11-01
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| Series: | Frontiers in Bioscience-Landmark |
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| Online Access: | https://www.imrpress.com/journal/FBL/28/11/10.31083/j.fbl2811305 |
| _version_ | 1797400708078632960 |
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| author | Riye Lu Pengwei Li Li Zhu Ming Xian Chang Songying Ouyang |
| author_facet | Riye Lu Pengwei Li Li Zhu Ming Xian Chang Songying Ouyang |
| author_sort | Riye Lu |
| collection | DOAJ |
| description | Glycosylation is one of the most common post-translational modifications of proteins across all kingdoms of life. Diverse monosaccharides and polysaccharides can be attached to a range of amino acid residues generating N-glycosylation, O-glycosylation, C-glycosylation, S-glycosylation, as well as P-glycosylation. The functions of the eukaryotic glycosylation system during protein folding in the endoplasmic reticulum (ER) and Golgi are well-studied. Increasing evidence in the recent decade has demonstrated the presence of oligosaccharyltransferases (OSTs) in bacteria and archaea. In particular, the oligosaccharyltransferase (PglB) of Campylobacter jejuni and oligosaccharyltransferase (PglL) enzyme of Neisseria meningitidis are the most characterized OSTs that catalyze bacterial N-linked glycosylation and O-linked glycosylation, respectively. Glycoprotein administered as glycoconjugate vaccines have been shown to be effective prophylactic to protect against numerous pathogenic bacteria. The chemical synthesis of glycoproteins is complex and expensive, which limits its application to the development of glycoconjugate vaccines. However, studies have demonstrated that the biosynthesis of glycoproteins is realizable by transferring PglB, a plasmid encoding a substrate protein, or PglL, a plasmid encoding genes for glycan synthesis to Escherichia coli. This strategy can be applied to the development of glycoconjugate vaccines using engineered host E. coli. This review summarizes the structure and mechanism of action of the bacterial OSTs, PglB and PglL, and discusses their potential application to glycoconjugate vaccine design. |
| first_indexed | 2024-03-09T01:59:24Z |
| format | Article |
| id | doaj.art-26098ce5ca66456cbf4d09d918ffcdbc |
| institution | Directory Open Access Journal |
| issn | 2768-6701 |
| language | English |
| last_indexed | 2024-03-09T01:59:24Z |
| publishDate | 2023-11-01 |
| publisher | IMR Press |
| record_format | Article |
| series | Frontiers in Bioscience-Landmark |
| spelling | doaj.art-26098ce5ca66456cbf4d09d918ffcdbc2023-12-08T07:49:20ZengIMR PressFrontiers in Bioscience-Landmark2768-67012023-11-01281130510.31083/j.fbl2811305S2768-6701(23)01015-8Advances in Bacterial Oligosaccharyltransferase Structure Elucidation and Potential Application to Glycoconjugate Vaccine DesignRiye Lu0Pengwei Li1Li Zhu2Ming Xian Chang3Songying Ouyang4Key Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University, Fuzhou, 350117, ChinaState Key Laboratory of Freshwater Ecology and Biotechnology, Key Laboratory of Aquaculture Disease Control, Institute of Hydrobiology, Chinese Academy of Sciences, 430072 Wuhan, Hubei, ChinaState Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Biotechnology, 100071 Beijing, ChinaState Key Laboratory of Freshwater Ecology and Biotechnology, Key Laboratory of Aquaculture Disease Control, Institute of Hydrobiology, Chinese Academy of Sciences, 430072 Wuhan, Hubei, ChinaKey Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University, Fuzhou, 350117, ChinaGlycosylation is one of the most common post-translational modifications of proteins across all kingdoms of life. Diverse monosaccharides and polysaccharides can be attached to a range of amino acid residues generating N-glycosylation, O-glycosylation, C-glycosylation, S-glycosylation, as well as P-glycosylation. The functions of the eukaryotic glycosylation system during protein folding in the endoplasmic reticulum (ER) and Golgi are well-studied. Increasing evidence in the recent decade has demonstrated the presence of oligosaccharyltransferases (OSTs) in bacteria and archaea. In particular, the oligosaccharyltransferase (PglB) of Campylobacter jejuni and oligosaccharyltransferase (PglL) enzyme of Neisseria meningitidis are the most characterized OSTs that catalyze bacterial N-linked glycosylation and O-linked glycosylation, respectively. Glycoprotein administered as glycoconjugate vaccines have been shown to be effective prophylactic to protect against numerous pathogenic bacteria. The chemical synthesis of glycoproteins is complex and expensive, which limits its application to the development of glycoconjugate vaccines. However, studies have demonstrated that the biosynthesis of glycoproteins is realizable by transferring PglB, a plasmid encoding a substrate protein, or PglL, a plasmid encoding genes for glycan synthesis to Escherichia coli. This strategy can be applied to the development of glycoconjugate vaccines using engineered host E. coli. This review summarizes the structure and mechanism of action of the bacterial OSTs, PglB and PglL, and discusses their potential application to glycoconjugate vaccine design.https://www.imrpress.com/journal/FBL/28/11/10.31083/j.fbl2811305oligosaccharyltransferasespglbpgllglycoconjugate vaccine |
| spellingShingle | Riye Lu Pengwei Li Li Zhu Ming Xian Chang Songying Ouyang Advances in Bacterial Oligosaccharyltransferase Structure Elucidation and Potential Application to Glycoconjugate Vaccine Design Frontiers in Bioscience-Landmark oligosaccharyltransferases pglb pgll glycoconjugate vaccine |
| title | Advances in Bacterial Oligosaccharyltransferase Structure Elucidation and Potential Application to Glycoconjugate Vaccine Design |
| title_full | Advances in Bacterial Oligosaccharyltransferase Structure Elucidation and Potential Application to Glycoconjugate Vaccine Design |
| title_fullStr | Advances in Bacterial Oligosaccharyltransferase Structure Elucidation and Potential Application to Glycoconjugate Vaccine Design |
| title_full_unstemmed | Advances in Bacterial Oligosaccharyltransferase Structure Elucidation and Potential Application to Glycoconjugate Vaccine Design |
| title_short | Advances in Bacterial Oligosaccharyltransferase Structure Elucidation and Potential Application to Glycoconjugate Vaccine Design |
| title_sort | advances in bacterial oligosaccharyltransferase structure elucidation and potential application to glycoconjugate vaccine design |
| topic | oligosaccharyltransferases pglb pgll glycoconjugate vaccine |
| url | https://www.imrpress.com/journal/FBL/28/11/10.31083/j.fbl2811305 |
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