Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 19, Pages 8030-8033Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja301334b
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Funding
- BBSRC
- EPSRC
- Glycoform Ltd
- VTU
- IAVI [UOXFORCOA1101]
- Glycobiology Institute
- Biotechnology and Biological Sciences Research Council [BB/C510824/1, BB/E004350/1, EGA17763] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/G026688/1, EP/D023335/1, GR/T26542/01, EP/I500200/1, EP/D023343/1, EP/E000614/1] Funding Source: researchfish
- BBSRC [BB/E004350/1] Funding Source: UKRI
- EPSRC [EP/G026688/1, EP/E000614/1, EP/I500200/1] Funding Source: UKRI
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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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