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US 2021/0277052 A1Published application
Recombinant grp94 chaperones and methods of using the same to modulate glycosylation in fusion proteins
AssigneeHauptman-Woodward Medical Research Institute, Inc.
InventorsDaniel T. Gewirth, John D. Huck
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Abstract
Methods for glycosylation of Grp94 chaperone proteins, including Grp94 fragments, mutants, and fusion proteins, expressed in mammalian cells are presented. The method comprises altering a Pre-N domain of the Grp94 chaperone protein, wherein the alteration of the Pre-N domain of the Grp94 chaperone protein leads to glycosylation at available glycosylation sites downstream of the Pre-N domain of the Grp94 chaperone protein, when expressed in mammalian cells.
Claims20
A recombinant glucose-regulated protein 94 (Grp94) protein comprising:
- deletion of seven or more residues from a Pre-N domain of the recombinant Grp94;
- or
- substitution of five or more residues of the Pre-N domain with alanine,
- wherein the recombinant Grp94 is glycosylated at a minor glycosylation site.
1 more element
A method of glycosylating a protein comprising:
- expressing a recombinant fusion protein in a host cell,
- wherein the recombinant fusion protein comprises (i) a wild type glucose-regulated protein 94 (Grp94) or a recombinant Grp94 and (ii) the protein, wherein the protein fused to the C-terminus of the wild type or recombinant Grp94.
Dependencies are inferred from the claim text.