Bacterial Glycoengineering as a Biosynthetic Route to Customized Glycomolecules.

Adv Biochem Eng Biotechnol

School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA.

Published: July 2021

Bacteria have garnered increased interest in recent years as a platform for the biosynthesis of a variety of glycomolecules such as soluble oligosaccharides, surface-exposed carbohydrates, and glycoproteins. The ability to engineer commonly used laboratory species such as Escherichia coli to efficiently synthesize non-native sugar structures by recombinant expression of enzymes from various carbohydrate biosynthesis pathways has allowed for the facile generation of important products such as conjugate vaccines, glycosylated outer membrane vesicles, and a variety of other research reagents for studying and understanding the role of glycans in living systems. This chapter highlights some of the key discoveries and technologies for equipping bacteria with the requisite biosynthetic machinery to generate such products. As the bacterial glyco-toolbox continues to grow, these technologies are expected to expand the range of glycomolecules produced recombinantly in bacterial systems, thereby opening up this platform to an even larger number of applications.

Download full-text PDF

Source
http://dx.doi.org/10.1007/10_2018_72DOI Listing

Publication Analysis

Top Keywords

bacterial glycoengineering
4
glycoengineering biosynthetic
4
biosynthetic route
4
route customized
4
customized glycomolecules
4
glycomolecules bacteria
4
bacteria garnered
4
garnered increased
4
increased interest
4
interest years
4

Similar Publications

Advances in bacterial glycoprotein engineering: A critical review of current technologies, emerging challenges, and future directions.

Biotechnol Adv

January 2025

TEDA Institute of Biological Sciences and Biotechnology, Nankai University, Tianjin, China; Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, Nankai University, Tianjin, China; Nankai International Advanced Research Institute, Nankai University, Shenzhen, China. Electronic address:

Protein glycosylation, which involves the addition of carbohydrate chains to amino acid side chains, imparts essential properties to proteins, offering immense potential in synthetic biology applications. Despite its importance, natural glycosylation pathways present several limitations, highlighting the need for new tools to better understand glycan structures, recognition, metabolism, and biosynthesis, and to facilitate the production of biologically relevant glycoproteins. The field of bacterial glycoengineering has gained significant attention due to the ongoing discovery and study of bacterial glycosylation systems.

View Article and Find Full Text PDF

Sugar Auxiliary Group Assisted Diversity-Oriented Enzymatic Modular Synthesis of 0-Series Ganglioside Glycans.

Angew Chem Int Ed Engl

December 2024

Key Laboratory of Marine Drugs of Ministry of Education, Shandong Key Laboratory of Glycoscience and Glycotherapeutics, School of Medicine and Pharmacy, Ocean University of China, Qingdao, 266003, China.

Owing to the inaccessibility of β1-4-N-acetylgalactosaminyltransferase for direct glycan chain elongation, the enzymatic synthesis of 0-series gangliosides with extended backbones has not been explored. In this study, sialic acid was enzymatically introduced as an auxiliary group to overcome the limitation of substrate specificity of Campylobacter jejuni β1-4-N-acetylgalactosaminyltransferase (CjCgtA) to achieve the synthesis of desired extended 0-series ganglioside core structures, and the sialic acid auxiliary group could be removed by sialidase at appropriate stages. A bacterial α2-6-sialyltransferase from Photobacterium damselae (Pd2,6ST) exhibited unexpected acceptor substrate specificity for 0-series ganglioside core structures, providing ready access to complex gangliosides bearing the sialyl N-acetylgalactosamine unit.

View Article and Find Full Text PDF

Rational design of N-glycosyltransferases from Aggregatibacter aphrophilus to synthesize Gal-modified glycoconjugates targeting hepatocellular carcinoma cells.

Int J Biol Macromol

December 2024

State Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong University, Qingdao 266237, China. Electronic address:

Hepatocellular carcinoma (HCC) significantly impacts human health due to its tendency to develop multi-drug resistance. Regarding the treatment of HCC, galactosylated conjugates can target drug delivery. Bacterial N-glycosyltransferases (NGTs) catalyze glucosylation or galactosylation of the Asn residue motif Asn-X-Ser/Thr (X ≠ P).

View Article and Find Full Text PDF

Diabetic wounds have become a global healthcare burden owing to impaired angiogenesis and persistent infections. Extracellular vesicles (EVs) can improve diabetic wounds, though their targeting ability is limited. In this study, we investigated the performance of a novel hydrogel dressing comprised of gelatin methacryloyl, glycoengineered EVs, and polylysine in treating infected diabetic wounds.

View Article and Find Full Text PDF

Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1.

Microorganisms

November 2024

National Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, NMPA Key Laboratory for Quality Research and Evaluation of Carbohydrate-Based Medicine, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.

Relatively little is known about enzymes with broad substrate spectra, leading to limited applications and progress. Herein, we elucidate Aly16-1 of sp. strain CB16 as a novel multifunctional member of the eighth polysaccharide lyase (PL8) family, although it shared few sequence identities with the characterized enzymes.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!