IP Library Granted Patent US 11,136,359
Granted Patent B2
US 11,136,359 · App. 15/900,419 · Granted Oct 5, 2021

Mutated immunoglobulin-binding polypeptides

Inventors: Gustav Rodrigo (Uppsala, SE); Mats Ander (Uppsala, SE); Tomas Bjorkman (Uppsala, SE); Goran Bauren (Uppsala, SE)
Assignee: Cytiva BioProcess R&D AB
C07K14/31B01D15/3809B01J20/286B01J20/3204B01J20/3212B01J20/3219B01J20/3274C07K1/22C07K14/745C07K16/00
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Quick Facts
Patent No.
US 11,136,359
App. No.
15/900,419
Granted
Oct 5, 2021
Kind
B2
Abstract

The invention discloses a polypeptide with improved alkaline stability, which polypeptide comprises a mutant of a B or C domain of Staphylococcus Protein A (SpA), as specified by SEQ ID NO 1 or SEQ ID NO 2, or of Protein Z, as specified by SEQ ID NO 3, wherein at least the glutamine residue at position 9 has been mutated to an amino acid other than asparagine. The invention also discloses multimers of said polypeptide, as well as separation matrices comprising the multimers or polypeptides.

Claims (15)

1. An immunoglobulin-binding polypeptide comprising a mutant B-domain or C-domain of Staphylococcus Protein A (SpA), as specified by SEQ ID NO:4, wherein the glutamine residue at position 9 has been mutated to an alanine residue or a threonine residue, or wherein the glutamine residue at position 9 has been mutated to an alanine residue or a threonine residue with further mutations in at least one of E15 mutated to a lysine residue, D36 mutated to a threonine residue or an alanine residue, and E47 mutated to a threonine residue; and wherein the polypeptide binds the kappa light chain of an antibody or fragment thereof and has improved alkaline stability compared to a non-mutated B-domain or C-domain of SpA.

2. The polypeptide of claim 1 , wherein in the further mutations the original amino acid residue is substituted at E15 with lysine.

3. The polypeptide of claim 1 , wherein in the further mutations the original amino acid residue is substituted at D36 with threonine.

4. The polypeptide of claim 1 , wherein in the further mutations the original amino acid residue is substituted at D36 with alanine.

5. The polypeptide of claim 1 , wherein in the further mutations the original amino acid residue is substituted at E47 with threonine.

6. The polypeptide of claim 1 , wherein the amino acid residue at position 9 is alanine.

7. The polypeptide of claim 1 , wherein the amino acid residue at position 9 is threonine.

8. The polypeptide or multimer according to claim 1 , further comprising at the C-terminal or N-terminal one or more coupling elements, selected from the group consisting of a cysteine residue, a plurality of lysine residues and a plurality of histidine residues.

9. A nucleic acid or a vector encoding a polypeptide or multimer according to claim 1 .

10. A separation matrix, wherein a plurality of polypeptides or multimers according to claim 1 have been coupled to a solid support.

11. A method of isolating an immunoglobulin, wherein a separation matrix according to claim 10 is used.

12. The method of claim 11 , comprising the steps of:

contacting a liquid sample comprising an immunoglobulin with the separation matrix,

washing said separation matrix with a washing liquid,

eluting the immunoglobulin from the separation matrix with an elution liquid, and cleaning the separation matrix with a cleaning liquid.

Assignments (3)
CHANGE OF NAME Recorded Oct 5, 2020
From: GE HEALTHCARE BIOPROCESS R&D AB
To: CYTIVA BIOPROCESS R&D AB
Reel/Frame 054299/0349 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 20, 2018
From: RODRIGO, GUSTAV; ANDER, MATS; BJORKMAN, TOMAS; BAUREN, GORAN
To: GE HEALTHCARE BIO-SCIENCES AB
Reel/Frame 044981/0812 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 20, 2018
From: GE HEALTHCARE BIO-SCIENCES AB
To: GE HEALTHCARE BIOPROCESS R&D AB
Reel/Frame 045381/0001 →
Priority Claims (2)
SE 1350859-3 · Jul 10, 2013 · national
SE 1350860-1 · Jul 10, 2013 · national
Continuity (2)
Continuation 14903837
Related Publication 20180244729A1 · Aug 30, 2018
Cited By (2)
US 12,221,492 US 12,448,411