Antibodies against ox40 and uses thereof
US-2016347849-A1 · Dec 1, 2016 · US
US10894836B2 · US · B2
| Field | Value |
|---|---|
| Publication number | US-10894836-B2 |
| Application number | US-201816037304-A |
| Country | US |
| Kind code | B2 |
| Filing date | Jul 17, 2018 |
| Priority date | Nov 30, 2009 |
| Publication date | Jan 19, 2021 |
| Grant date | Jan 19, 2021 |
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Antibody and other Fc-containing molecules with variations in the Fc region with reduced binding to Fc gamma receptors and resulting activity and can be used in the treatment of various diseases and disorders.
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What is claimed: 1. An isolated polynucleotide encoding an Fc-containing molecule, comprising a mutated IgG1 Fc domain and having binding reduced by at least 800 fold or undetectable binding to a Fcγ receptor (FcγR), selected from the group consisting of FcγRI, FcγRIIa-H131 variant, FcγRIIa-R131 variant, FcγRIIb, and FcγRIII-V158 variant, as compared to an Fc-containing molecule with a wild type IgG1 Fc domain, wherein the mutated IgG1 Fc comprises the mutations L234A, L235A, G237A P238S, H268A, A330S, and P331S, wherein the binding is measured by conjugating the Fc-containing molecule and the FcγR to a donor and an acceptor beads and by measuring the energy transfer between the donor and the acceptor beads using ALPHASCREEN® assay. 2. The polynucleotide of claim 1 , wherein the polynucleotide encodes a molecule comprising is an antibody, an antibody fragment or an Fc region. 3. A vector comprising the polynucleotide of claim 1 or 2 . 4. An isolated host cell comprising the vector of claim 3 . 5. A method of making an Fc-containing molecule, comprising culturing the host cell of claim 4 under conditions wherein the Fc mutant-containing molecule is expressed, purifying the expressed Fc mutant-containing molecule, and measuring the reduced binding (by at least 800 fold) or undetectable binding of the Fc mutant-containing molecule to the Fcγ receptor (FcγR), selected from the group consisting of FcγRI, FcγRIIa-H131 variant, FcγRIIa-R131 variant, FcγRIIb, and FcγRIII-V158 variant, as compared to an Fc-containing molecule with a wild type IgG1 Fc domain.
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