In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-L-fucosidases

Jianbing Jiang; Wouter W. Kallemeijn; Daniel W. Wright; Adrianus M C H Van Den Nieuwendijk; Veronica Coco Rohde; Elisa Colomina Folch; Hans Van Den Elst; Bogdan I. Florea; Saskia Scheij; Wilma E. Donker-Koopman; Marri Verhoek; Nan Li; Martin Schürmann; Daniel Mink; Rolf G. Boot; Jeroen D C Codée; Gijsbert A. Van Der Marel; Gideon J. Davies; Johannes M F G Aerts; Herman S. Overkleeft

doi:10.1039/c4sc03739a

In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-L-fucosidases

Jianbing Jiang, Wouter W. Kallemeijn, Daniel W. Wright, Adrianus M C H Van Den Nieuwendijk, Veronica Coco Rohde, Elisa Colomina Folch, Hans Van Den Elst, Bogdan I. Florea, Saskia Scheij, Wilma E. Donker-Koopman, Marri Verhoek, Nan Li, Martin Schürmann, Daniel Mink, Rolf G. Boot, Jeroen D C Codée, Gijsbert A. Van Der Marel, Gideon J. Davies, Johannes M F G Aerts^*, Herman S. Overkleeft

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

GH29 α-L-fucosidases catalyze the hydrolysis of α-L-fucosidic linkages. Deficiency in human lysosomal α-L-fucosidase (FUCA1) leads to the recessively inherited disorder, fucosidosis. Herein we describe the development of fucopyranose-configured cyclophellitol aziridines as activity-based probes (ABPs) for selective in vitro and in vivo labeling of GH29 α-L-fucosidases from bacteria, mice and man. Crystallographic analysis on bacterial α-L-fucosidase confirms that the ABPs act by covalent modification of the active site nucleophile. Competitive activity-based protein profiling identified l-fuconojirimycin as the single GH29 α-L-fucosidase inhibitor from eight configurational isomers.

Original language	English
Pages (from-to)	2782-2789
Number of pages	8
Journal	Chemical Science
Volume	6
Issue number	5
Early online date	9 Feb 2015
DOIs	https://doi.org/10.1039/c4sc03739a
Publication status	Published - 1 May 2015

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Jiang, J., Kallemeijn, W. W., Wright, D. W., Van Den Nieuwendijk, A. M. C. H., Rohde, V. C., Folch, E. C., Van Den Elst, H., Florea, B. I., Scheij, S., Donker-Koopman, W. E., Verhoek, M., Li, N., Schürmann, M., Mink, D., Boot, R. G., Codée, J. D. C., Van Der Marel, G. A., Davies, G. J., Aerts, J. M. F. G., & Overkleeft, H. S. (2015). In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-L-fucosidases. Chemical Science, 6(5), 2782-2789. https://doi.org/10.1039/c4sc03739a

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title = "In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-L-fucosidases",

abstract = "GH29 α-L-fucosidases catalyze the hydrolysis of α-L-fucosidic linkages. Deficiency in human lysosomal α-L-fucosidase (FUCA1) leads to the recessively inherited disorder, fucosidosis. Herein we describe the development of fucopyranose-configured cyclophellitol aziridines as activity-based probes (ABPs) for selective in vitro and in vivo labeling of GH29 α-L-fucosidases from bacteria, mice and man. Crystallographic analysis on bacterial α-L-fucosidase confirms that the ABPs act by covalent modification of the active site nucleophile. Competitive activity-based protein profiling identified l-fuconojirimycin as the single GH29 α-L-fucosidase inhibitor from eight configurational isomers.",

author = "Jianbing Jiang and Kallemeijn, {Wouter W.} and Wright, {Daniel W.} and {Van Den Nieuwendijk}, {Adrianus M C H} and Rohde, {Veronica Coco} and Folch, {Elisa Colomina} and {Van Den Elst}, Hans and Florea, {Bogdan I.} and Saskia Scheij and Donker-Koopman, {Wilma E.} and Marri Verhoek and Nan Li and Martin Sch{\"u}rmann and Daniel Mink and Boot, {Rolf G.} and Cod{\'e}e, {Jeroen D C} and {Van Der Marel}, {Gijsbert A.} and Davies, {Gideon J.} and Aerts, {Johannes M F G} and Overkleeft, {Herman S.}",

year = "2015",

month = may,

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doi = "10.1039/c4sc03739a",

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Jiang, J, Kallemeijn, WW, Wright, DW, Van Den Nieuwendijk, AMCH, Rohde, VC, Folch, EC, Van Den Elst, H, Florea, BI, Scheij, S, Donker-Koopman, WE, Verhoek, M, Li, N, Schürmann, M, Mink, D, Boot, RG, Codée, JDC, Van Der Marel, GA, Davies, GJ, Aerts, JMFG & Overkleeft, HS 2015, 'In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-L-fucosidases', Chemical Science, vol. 6, no. 5, pp. 2782-2789. https://doi.org/10.1039/c4sc03739a

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T1 - In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-L-fucosidases

AU - Jiang, Jianbing

AU - Kallemeijn, Wouter W.

AU - Wright, Daniel W.

AU - Van Den Nieuwendijk, Adrianus M C H

AU - Rohde, Veronica Coco

AU - Folch, Elisa Colomina

AU - Van Den Elst, Hans

AU - Florea, Bogdan I.

AU - Scheij, Saskia

AU - Donker-Koopman, Wilma E.

AU - Verhoek, Marri

AU - Li, Nan

AU - Schürmann, Martin

AU - Mink, Daniel

AU - Boot, Rolf G.

AU - Codée, Jeroen D C

AU - Van Der Marel, Gijsbert A.

AU - Davies, Gideon J.

AU - Aerts, Johannes M F G

AU - Overkleeft, Herman S.

PY - 2015/5/1

Y1 - 2015/5/1

N2 - GH29 α-L-fucosidases catalyze the hydrolysis of α-L-fucosidic linkages. Deficiency in human lysosomal α-L-fucosidase (FUCA1) leads to the recessively inherited disorder, fucosidosis. Herein we describe the development of fucopyranose-configured cyclophellitol aziridines as activity-based probes (ABPs) for selective in vitro and in vivo labeling of GH29 α-L-fucosidases from bacteria, mice and man. Crystallographic analysis on bacterial α-L-fucosidase confirms that the ABPs act by covalent modification of the active site nucleophile. Competitive activity-based protein profiling identified l-fuconojirimycin as the single GH29 α-L-fucosidase inhibitor from eight configurational isomers.

AB - GH29 α-L-fucosidases catalyze the hydrolysis of α-L-fucosidic linkages. Deficiency in human lysosomal α-L-fucosidase (FUCA1) leads to the recessively inherited disorder, fucosidosis. Herein we describe the development of fucopyranose-configured cyclophellitol aziridines as activity-based probes (ABPs) for selective in vitro and in vivo labeling of GH29 α-L-fucosidases from bacteria, mice and man. Crystallographic analysis on bacterial α-L-fucosidase confirms that the ABPs act by covalent modification of the active site nucleophile. Competitive activity-based protein profiling identified l-fuconojirimycin as the single GH29 α-L-fucosidase inhibitor from eight configurational isomers.

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SP - 2782

EP - 2789

JO - Chemical Science

JF - Chemical Science

IS - 5

ER -

In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-L-fucosidases

Abstract

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