Chaperonin 10 variants
AssigneeCBio Limited
InventorsDean Jason Naylor, Richard James Brown, Christopher Bruce Howard, Christopher John De Bakker, Jeanette Elizabeth Stok, Andrew Leigh James, Daniel Scott Lambert, Kylie Jane Ralston, Walter Rene Antonius Van Heumen, Linda Allison Ward
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Abstract
The invention relates generally to chaperonin 10 N-terminal variants. More specifically, the invention relates to chaperonin 10 N-terminal variants with enhanced immunomodulatory capacity and/or enhanced binding affinity for pathogen-associated molecular patterns (PAMPs) and/or damage-associated molecular patterns (DAMPs).
Claims16
An isolated chaperonin 10 (Cpn10) variant polypeptide derived from human Cpn10 sharing at least 90% sequence identity with a wild-type human Cpn10 polypeptide and comprising an N-terminus extended by two to five additional amino acid residues compared to said wild-type polypeptide, wherein the polypeptide has increased binding affinity for a pathogen-associated molecular pattern (PAMP) compared to the binding affinity of Ala-Cpn10 (SEQ ID NO:
- 3) for said PAMP, wherein the isolated Cpn10 polypeptide possesses a conserved core antiparallel β-barrel flanked by a β-hairpin roof loop region and a mobile loop region.
An isolated chaperonin 10 (Cpn10) variant polypeptide sharing at least 90% sequence identity with a wild-type Cpn10 polypeptide and comprising an N-terminus extended by at least two additional amino acid residues compared to said wild-type polypeptide, wherein the polypeptide has increased binding affinity for a pathogen-associated molecular pattern (PAMP) compared to the binding affinity of Ala-Cpn10 (SEQ ID NO:
- 3) for said PAMP, wherein the N-terminus of said variant polypeptide commences with a methionine residue, and wherein said methionine residue precedes an amino acid residue selected from the group consisting of arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, tyrosine, and valine, wherein said polypeptide comprises the amino acid sequence as set forth in SEQ ID NOs:
- 29.
An isolated human chaperonin 10 (Cpn10) variant polypeptide sharing at least 80% sequence identity with a wild-type human Cpn10 polypeptide and comprising an N-terminus extended by one additional amino acid residue compared to said wild-type human polypeptide, wherein said additional amino acid residue is a serine or proline residue, and wherein said variant polypeptide has increased immunomodulatory function compared to human Ala-Cpn10, wherein the isolated Cpn10 polypeptide possesses a conserved core antiparallel β-barrel flanked by a β-hairpin roof loop region and a mobile loop region.
An isolated human Cpn10 variant polypeptide sharing at least 80% sequence identity with a wild-type human Cpn10 polypeptide and comprising an N-terminus extended by one additional amino acid residue compared to said wild-type human polypeptide, wherein said additional amino acid residue is a serine or proline residue, and wherein said variant polypeptide has increased immunomodulatory function compared to human Ala-Cpn10, wherein the isolated Cpn10 polypeptide possesses a core antiparallel β-barrel flanked by a β-hairpin roof loop region and a mobile loop region, wherein said polypeptide comprises the amino acid sequence as set forth in SEQ ID NO:
- 21 or 35.
Dependencies are inferred from the claim text.