Journal article

An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling.

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.

Publication status:: Published

Peer review status:: Peer reviewed

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APA Style

Goodfellow, J., Baruah, K., Yamamoto, K., Bonomelli, C., Krishna, B., Harvey, D., Crispin, M., Scanlan, C., & Davis, B. (2012). An endoglycosidase with alternative glycan specificity allows broadened glycoprotein remodelling. Journal of the American Chemical Society, 134(19), 8030–8033.

MLA Style

Goodfellow, J, et al. “An Endoglycosidase with Alternative Glycan Specificity Allows Broadened Glycoprotein Remodelling.” Journal of the American Chemical Society, vol. 134, no. 19, 2012, pp. 8030–33.

Chicago Style

Goodfellow, J, K Baruah, K Yamamoto, et al. 2012. “An Endoglycosidase with Alternative Glycan Specificity Allows Broadened Glycoprotein Remodelling.” Journal of the American Chemical Society 134 (19): 8030–33.
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Publisher copy:: 10.1021/ja301334b

Authors

+ Goodfellow, J More by this author

Institution:: University of Oxford
Department:: Department of Biochemistry
Role:: Author

+ Baruah, K More by this author

Institution:: University of Oxford
Division:: MPLS
Department:: Chemistry
Sub department:: Organic Chemistry
Role:: Author

+ Yamamoto, K More by this author

Institution:: University of Oxford
Division:: MPLS
Department:: Chemistry
Sub department:: Organic Chemistry
Role:: Author

+ Bonomelli, C More by this author

Institution:: University of Oxford
Department:: Department of Biochemistry
Role:: Author

+ Krishna, B More by this author

Institution:: University of Oxford
Department:: Department of Biochemistry
Role:: Author

More authors...

+ International Aids Vaccine Initiative More from this funder

Funding agency for:: Scanlan, C
Grant:: UOXFORCOA1101

+ VTU More from this funder

Funding agency for:: Yamamoto, K

+ Glycoform Ltd More from this funder

Funding agency for:: Goodfellow, J

+ Glycobiology Institute More from this funder

Funding agency for:: Bonomelli, C; Krishna, B

+ Biotechnology and Biological Sciences Research Council More from this funder

More funders...

Journal:: Journal of the American Chemical Society More from this journal
Volume:: 134
Issue:: 19
Pages:: 8030-8033
Publication date:: 2012-05-02
DOI:: 10.1021/ja301334b
EISSN:: 1520-5126
ISSN:: 0002-7863

Language:: English
Keywords:: Glycoproteins

Humans

Substrate Specificity

Protein Conformation

Streptococcus pyogenes

Models, Molecular

Polysaccharides

Glycoside Hydrolases

Immunoglobulin G
Pubs id:: pubs:329007
UUID:: uuid:cf92f6dc-e3d3-4eee-b0c3-188ce9feba49
Local pid:: pubs:329007
Source identifiers:: 329007
Deposit date:: 2012-12-19
ARK identifier:: ark:/29072/ora_cf92f6dce3d34eeeb0c3188ce9feba49

Terms of use

Copyright holder:: American Chemical Society
Copyright date:: 2012

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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