ArticleBiotechnology journal2015
Glycoarrays with engineered phages displaying structurally diverse oligosaccharides enable high-throughput detection of glycan-protein interactions.
Article in Biotechnology journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Measuring carbohydrate recognition profile of lectins on live cells using liquid glycan array (LiGA).Nature protocols · 2025Review
- Rapid biosynthesis of glycoprotein therapeutics and vaccines from freeze-dried bacterial cell lysates.Nature protocols · 2023Review
- A Low-Cost, Thermostable, Cell-Free Protein Synthesis Platform for On-Demand Production of Conjugate Vaccines.ACS synthetic biology · 2023Article
- A low-cost recombinant glycoconjugate vaccine confers immunogenicity and protection against enterotoxigenicFrontiers in molecular biosciences · 2023Article
- Genetically encoded multivalent liquid glycan array displayed on M13 bacteriophage.Nature chemical biology · 2021Article
- On-demand biomanufacturing of protective conjugate vaccines.Science advances · 2021Article
- Emergence and significance of carbohydrate-specific antibodies.Genes and immunity · 2020Review
- Microarray Strategies for Exploring Bacterial Surface Glycans and Their Interactions With Glycan-Binding Proteins.Frontiers in microbiology · 2019Review
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
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7 authors.
Funding
Abstract
Glycan microarrays have become a powerful platform to investigate the interactions of carbohydrates with a variety of biomolecules. However, the number and diversity of glycans available for use in such arrays represent a key bottleneck in glycan array fabrication. To address this challenge, we describe a novel glycan array platform based on surface patterning of engineered glycophages that display unique carbohydrate epitopes. Specifically, we show that glycophages are compatible with surface immobilization procedures and that phage-displayed oligosaccharides retain the ability to be recognized by different glycan-binding proteins (e.g. antibodies and lectins) after immobilization. A key advantage of glycophage arrays is that large quantities of glycophages can be produced biosynthetically from recombinant bacteria and isolated directly from bacterial supernatants without laborious purification steps. Taken together, the glycophage array technology described here should help to expand the diversity of glycan libraries and provide a complement to the existing toolkit for high-throughput analysis of glycan-protein interactions.
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Registered trials
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