ArticleSmall (Weinheim an der Bergstrasse, Germany)2008
Recombinant glycans on an S-layer self-assembly protein: a new dimension for nanopatterned biomaterials.
Article in Small (Weinheim an der Bergstrasse, Germany), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
16 citing papers in PubMed, 27 citations in OpenAlex.
- Synthetic glycoscapes: addressing the structural and functional complexity of the glycocalyx.Interface focus · 2019Review
- Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei.Nature communications · 2018Article
- Nanoscale materials for probing the biological functions of the glycocalyx.Glycobiology · 2016Review
- Relevance of glycosylation of S-layer proteins for cell surface properties.Acta biomaterialia · 2015Article
- S-layers: principles and applications.FEMS microbiology reviews · 2014Article
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- Protein O-glucosylation in Lactobacillus buchneri.Glycoconjugate journal · 2014Article
- Multivalent glycoconjugates as anti-pathogenic agents.Chemical Society reviews · 2013Review
- Bacterial cell-envelope glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2013Review
- Description of a Putative Oligosaccharyl:S-Layer Protein Transferase from the TyrosineAdvances in microbiology · 2012Article
- A fusion tag to fold on: the S-layer protein SgsE confers improved folding kinetics to translationally fused enhanced green fluorescent protein.Journal of microbiology and biotechnology · 2012Article
- Protein glycosylation in bacteria: sweeter than ever.Nature reviews. Microbiology · 2010Review
- Structural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilus.Journal of molecular biology · 2010Article
- Construction of a gene knockout system for application in Paenibacillus alvei CCM 2051T, exemplified by the S-layer glycan biosynthesis initiation enzyme WsfP.Applied and environmental microbiology · 2009Article
- Purification, crystallization and preliminary crystallographic analysis of WsaF, an essential rhamnosyltransferase from Geobacillus stearothermophilus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- Molecular basis of S-layer glycoprotein glycan biosynthesis in Geobacillus stearothermophilus.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Crucial biological phenomena are mediated through carbohydrates that are displayed in a defined manner and interact with molecular scale precision. We lay the groundwork for the integration of recombinant carbohydrates into a "biomolecular construction kit" for the design of new biomaterials, by utilizing the self-assembly system of the crystalline cell surface (S)-layer protein SgsE of Geobacillus stearothermophilus NRS 2004/3a. SgsE is a naturally O-glycosylated protein, with intrinsic properties that allow it to function as a nanopatterned matrix for the periodic display of glycans. By using a combined carbohydrate/protein engineering approach, two types of S-layer neoglycoproteins are produced in Escherichia coli. Based on the identification of a suitable periplasmic targeting system for the SgsE self-assembly protein as a cellular prerequisite for protein glycosylation, and on engineering of one of the natural protein O-glycosylation sites into a target for N-glycosylation, the heptasaccharide from the AcrA protein of Campylobacter jejuni and the O7 polysaccharide of E. coli are co- or post-translationally transferred to the S-layer protein by the action of the oligosaccharyltransferase PglB. The degree of glycosylation of the S-layer neoglycoproteins after purification from the periplasmic fraction reaches completeness. Electron microscopy reveals that recombinant glycosylation is fully compatible with the S-layer protein self-assembly system. Tailor-made ("functional") nanopatterned, self-assembling neoglycoproteins may open up new strategies for influencing and controlling complex biological systems with potential applications in the areas of biomimetics, drug targeting, vaccine design, or diagnostics.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.