Glycoarrays—tools for determining protein–carbohydrate interactions and glycoenzyme specificity

Laurent, Nicolas; Voglmeir, Josef; Flitsch, Sabine L.

doi:10.1039/b806983m

Cited by 134 publications

(103 citation statements)

References 144 publications

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“…A review of glycoarrays for qualitative and quantitative analysis of carbohydrate binding has been published (Laurent, Voglmeir, & Flitsch, 2008a) and König (2008) has discussed the use of bioaffinity target plates in general. Mrksich (2008) has reviewed recent work on mass spectrometry, particularly MALDI, as a method for developing and characterizing a broad range of chemical reactions of molecules attached to selfassembled monolayers of alkanethiolates on gold, a technique termed SAMDI-TOF mass spectrometry.…”

Section: Glycan Arraysmentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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This review is the fifth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2008. The first section of the review covers fundamental studies, fragmentation of carbohydrate ions, use of derivatives and new software developments for analysis of carbohydrate spectra. Among newer areas of method development are glycan arrays, MALDI imaging and the use of ion mobility spectrometry. The second section of the review discusses applications of MALDI MS to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, biopharmaceuticals, glycated proteins, glycolipids, glycosides and various other natural products. There is a short section on the use of MALDI mass spectrometry for the study of enzymes involved in glycan processing and a section on the use of MALDI MS to monitor products of the chemical synthesis of carbohydrates with emphasis on carbohydrate-protein complexes and glycodendrimers. Corresponding analyses by electrospray ionization now appear to outnumber those performed by MALDI and the amount of literature makes a comprehensive review on this technique impractical. However, most of the work relating to sample preparation and glycan synthesis is equally relevant to electrospray and, consequently, those proposing analyses by electrospray should also find material in this review of interest.

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Section: Glycan Arraysmentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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“…For example, the GT could be used to express and isolate carrier proteins that are hyper-glycosylated with a multiplicity of homogeneous glycans. Such hyper-glycosylated proteins could then be used as features on carbohydrate microarrays (so-called glycoarrays), which are currently very challenging to fabricate due in large part to difficulties associated with the synthesis and isolation of sufficient quantities of naturally occurring oligosaccharides (38). Glycan diversity could be "genetically encoded" by expression of different glycosyltransferases to control the specific glycoform, and covalent transfer onto target proteins could be achieved using PglB, which is relatively promiscuous in its choice of both oligosaccharide (16) and protein (Fig.…”

Section: Discussionmentioning

confidence: 99%

Production of Secretory and Extracellular N-Linked Glycoproteins inEscherichia coli

Fisher

Haitjema

Guarino

et al. 2011

Appl Environ Microbiol

118

108

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The Campylobacter jejuni pgl gene cluster encodes a complete N-linked protein glycosylation pathway that can be functionally transferred into Escherichia coli. In this system, we analyzed the interplay between N-linked glycosylation, membrane translocation and folding of acceptor proteins in bacteria. We developed a recombinant N-glycan acceptor peptide tag that permits N-linked glycosylation of diverse recombinant proteins expressed in the periplasm of glycosylation-competent E. coli cells. With this "glycosylation tag," a clear difference was observed in the glycosylation patterns found on periplasmic proteins depending on their mode of inner membrane translocation (i.e., Sec, signal recognition particle [SRP], or twin-arginine translocation [Tat] export), indicating that the mode of protein export can influence N-glycosylation efficiency. We also established that engineered substrate proteins targeted to environments beyond the periplasm, such as the outer membrane, the membrane vesicles, and the extracellular medium, could serve as substrates for N-linked glycosylation. Taken together, our results demonstrate that the C. jejuni N-glycosylation machinery is compatible with distinct secretory mechanisms in E. coli, effectively expanding the N-linked glycome of recombinant E. coli. Moreover, this simple glycosylation tag strategy expands the glycoengineering toolbox and opens the door to bacterial synthesis of a wide array of recombinant glycoprotein conjugates.

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“…In this context, carbohydrates, one of the most common compounds in living systems, are of increased interest for a large number of medical and pharmalogical-related applications, like vaccines and anticancer drugs 11 , fabrication of glycoarrays for antibody recognition and cell adhesion 12 , antibiofilm and antimicrobial formulations 13 , just to cite some. Even if carbohydrates alone are a source of nutrition to microorganisms rather than biocidal compounds, some reports relate the antimicrobial effects of sugar-containing molecules, such as bacterial exopolysaccharides, extracted from Escherichia coli, 14 and few glycoconjugates, carbohydrates covalently linked to an organic moiety (from simple alkyl chain to more complex structures), of both synthetic and natural origins.…”

Section: Introductionmentioning

confidence: 99%

Biocidal Properties of a Glycosylated Surface: Sophorolipids on Au(111)

Valotteau

Calers

Casale

et al. 2015

ACS Appl. Mater. Interfaces

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Classical antibacterial surfaces usually involve antiadhesive and/or biocidal strategies. Glycosylated surfaces are usually used to prevent biofilm formation via antiadhesive mechanisms. We report here the first example of a glycosylated surface with biocidal properties created by the covalent grafting of sophorolipids (a sophorose unit linked by a glycosidic bond to an oleic acid) through a self-assembled monolayer (SAM) of short aminothiols on gold (111) surfaces. The biocidal effect of such surfaces on Gram+ bacteria was assessed by a wide combination of techniques including microscopy observations, fluorescent staining and bacterial growth tests. About 50% of the bacteria are killed via alteration of the cell envelope. In addition, the role of the sophorose unit and aliphatic chain configuration are highlighted by the lack of activity of substrates modified respectively with sophorose-free oleic acid and sophorolipid-derivative having a saturated aliphatic chain. This system 2 demonstrates thus the direct implication of a carbohydrate in the destabilization and disruption of the bacterial cell envelope.3

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Glycoarrays—tools for determining protein–carbohydrate interactions and glycoenzyme specificity

Cited by 134 publications

References 144 publications

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Production of Secretory and Extracellular N-Linked Glycoproteins inEscherichia coli

Biocidal Properties of a Glycosylated Surface: Sophorolipids on Au(111)

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