An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling
An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling
Protein endoglycosidases are useful for biocatalytic alteration of glycans on protein surfaces, but the currently limited selectivity of endoglycosidases has prevented effective manipulation of certain N-linked glycans widely found in nature. Here we reveal that a bacterial endoglycosidase from Streptococcus pyogenes, EndoS, is complementary to other known endoglycosidases (EndoA, EndoH) used for current protein remodeling. It allows processing of complex-type N-linked glycans +/- core fucosylation but does not process oligomannose- or hybrid-type glycans. This biocatalytic activity now addresses previously refractory antibody glycoforms.
8030-8033
Goodfellow, Jonathan J.
4decae7e-d6b0-46d8-8780-bff2abb277bd
Baruah, Kavitha
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Yamamoto, Keisuke
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Bonomelli, Camille
51edb32c-85d0-45be-b050-b075cc3f6c28
Krishna, Benjamin
0783a6da-86b2-41f3-9a52-e753ef44adae
Harvey, David J.
8bb24417-3852-4b1f-827b-0d5d2c176744
Crispin, Matthew
cd980957-0943-4b89-b2b2-710f01f33bc9
Scanlan, Christopher N.
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Davis, Benjamin G.
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16 May 2012
Goodfellow, Jonathan J.
4decae7e-d6b0-46d8-8780-bff2abb277bd
Baruah, Kavitha
a02f59f3-5e0f-4735-9fdd-639bdbb8f563
Yamamoto, Keisuke
1eead3db-3aff-4bf3-aafd-f17f2663be90
Bonomelli, Camille
51edb32c-85d0-45be-b050-b075cc3f6c28
Krishna, Benjamin
0783a6da-86b2-41f3-9a52-e753ef44adae
Harvey, David J.
8bb24417-3852-4b1f-827b-0d5d2c176744
Crispin, Matthew
cd980957-0943-4b89-b2b2-710f01f33bc9
Scanlan, Christopher N.
04dd1b57-b6fc-414c-8595-08310dbb3d32
Davis, Benjamin G.
d9911bd8-7252-44f5-8dac-ea88efab500a
Goodfellow, Jonathan J., Baruah, Kavitha, Yamamoto, Keisuke, Bonomelli, Camille, Krishna, Benjamin, Harvey, David J., Crispin, Matthew, Scanlan, Christopher N. and Davis, Benjamin G.
(2012)
An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling.
Journal of the American Chemical Society, 134 (19), .
(doi:10.1021/ja301334b).
Abstract
Protein endoglycosidases are useful for biocatalytic alteration of glycans on protein surfaces, but the currently limited selectivity of endoglycosidases has prevented effective manipulation of certain N-linked glycans widely found in nature. Here we reveal that a bacterial endoglycosidase from Streptococcus pyogenes, EndoS, is complementary to other known endoglycosidases (EndoA, EndoH) used for current protein remodeling. It allows processing of complex-type N-linked glycans +/- core fucosylation but does not process oligomannose- or hybrid-type glycans. This biocatalytic activity now addresses previously refractory antibody glycoforms.
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Published date: 16 May 2012
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Local EPrints ID: 414412
URI: http://eprints.soton.ac.uk/id/eprint/414412
ISSN: 0002-7863
PURE UUID: d63c80d3-694d-4550-96f8-5950412746fe
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Date deposited: 28 Sep 2017 16:31
Last modified: 06 Jun 2024 01:59
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Author:
Jonathan J. Goodfellow
Author:
Kavitha Baruah
Author:
Keisuke Yamamoto
Author:
Camille Bonomelli
Author:
Benjamin Krishna
Author:
David J. Harvey
Author:
Christopher N. Scanlan
Author:
Benjamin G. Davis
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