Designer α 6-fucosidase mutants enable direct core fucosylation of intact N-glycopeptides and N-glycoproteins
US11193155B2 · kind B2 · utility
2Cited by
12References
11Claims
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Key dates
| Filing date | Aug 10, 2017 |
| Grant date | Dec 7, 2021 |
| Priority date | — |
| Expiry date | Aug 10, 2037 |
Classification
- Technology area (CPC C)Chemistry; Metallurgy
- CPC primaryC07K2319/50
- WIPO fieldBiotechnology
- WIPO sectorChemistry
Abstract
The present invention provides for novel fucosidase mutants that server as fuco-ligases for core fucosylation of a range of biological glycopeptides and glycoproteins including intact therapeutic antibodies. Several mutants with mutation at the general acid/base residue E274 of the Lactobacillus casei α1,6-fucosidase, including E274A, E274S, and E274G, were able to efficiently fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins. The site specific mutants enable the transfer of fucose to a core GlcNAc-Asn residue and useful for drug delivery and vaccine development.
Source: USPTO / EPO open patent data. Objective bibliographic and citation counts.