JSR Corp. v. Cytiva Bioprocess R&D AB

• Decision Date: 18 May 2023
• Docket Number: IPR2022-00042,IPR2022-00045,Patent 10,875,007 B2
• Parties: JSR CORPORATION and JSR LIFE SCIENCES, LLC, Petitioner, v. CYTIVA BIOPROCESS R&D AB, Patent Owner. Claim(s) Challenged 35 U.S.C. § Reference(s)/Basis Claim(s) Challenged 35 U.S.C. § Reference(s)/Basis Claim(s) 35 U.S.C. § Reference(s)/Basis Claim(s) Shown Unpatentable Claim(s) Not shown Unpatentable Claim(s) 35 U.S.C. § Reference(s)/Basis Claim(s) Shown Unpatentable Claim(s) Not shown Unpatentable
• Court: Patent Trial and Appeal Board

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JSR CORPORATION and JSR LIFE SCIENCES, LLC, Petitioner, v. CYTIVA BIOPROCESS R&D AB, Patent Owner.

Nos. IPR2022-00042, IPR2022-00045

Patent 10,875,007 B2

United States Patent and Trademark Office, Patent Trial and Appeal Board

May 18, 2023

FOR PETITIONER: Naveen Modi Eric Dittmann Isaac Ashkenazi Phillip Citroen PAUL HASTINGS LLP

FOR PATENT OWNER: David Krinsky David Berl WILLIAMS &CONNOLLY LLP

Before ULRIKE W. JENKS, SHERIDAN K. SNEDDEN, and SUSAN L. C MITCHELL, Administrative Patent Judges.

JUDGMENT FINAL WRITTEN DECISION DETERMINING SOME CHALLENGED CLAIMS UNPATENTABLE 35 U.S.C. § 318

SNEDDEN, Administrative Patent Judge.

I. INTRODUCTION

This is a Final Written Decision in an inter partes review of claims 114, 16-32, and 34-37 ("the challenged claims) of U.S. Patent No. 10,875,007 B2 (Ex. 1001, "the '007 patent"). We have jurisdiction under 35 U.S.C. § 6, and enter this Final Written Decision pursuant to 35 U.S.C. § 318(a) and 37 C.F.R. § 42.73. For the reasons set forth below, we determine that JSR Corporation and JSR Life Sciences, LLC (collectively, "Petitioner") has shown, by a preponderance of the evidence, that some of the challenged claims are unpatentable. See 35 U.S.C. § 316(e).

A. Consolidated Proceedings

The two captioned proceedings (IPR2022-00042 and IPR2022-00045 (or "the '045 IPR")) involve the '007 patent and challenge the same set of claims. The asserted grounds and prior art contentions are different in each proceeding. Consolidation is appropriate where, as here, the Board can more efficiently handle the common issues and evidence, and also remain consistent across proceedings. Under 35 U.S.C. § 315(d), the Director may determine the manner in which these pending proceedings may proceed, including "providing for stay, transfer, consolidation, or termination of any such matter or proceeding." See also 37 C.F.R. § 42.4(a) ("The Board institutes the trial on behalf of the Director."). There is no specific Board rule that governs consolidation of cases. But 37 C.F.R. § 42.5(a) allows the Board to determine a proper course of conduct in a proceeding for any situation not specifically covered by the rules and to enter non-final orders to administer the proceeding. Therefore, on behalf of the Director under § 315(d), and for a more efficient administration of these proceedings, we consolidate IPR2022-00042 and IPR2022-00045 for purposes of rendering this Final Written Decision.

B. Evidence

Petitioner relies upon information that includes the following:

Ex. 1004, M. Linhult, et al., Improving the Tolerance of a Protein A Analogue to Repeated Alkaline Exposures Using a Bypass Mutagenesis Approach, 55 PROTEINS: STRUCTURE, Function, and Bioinf., 407-16 (2004) ("Linhult").

Ex. 1005, L. Abrahmsen, et al., U.S. Patent No. 5,143,844 (issued Sept. 1, 1992) ("Abrahmsen").

Ex. 1006, S. Hober, PCT Publication No. Wo 03/080655 A1 (published oct. 2, 2003) ("Hober").

Ex. 1018, H. Berg., U.S. Patent Application Publication No. 2006/0134805 (published June 22, 2006) ("Berg").

C. Procedural History

Petitioner filed a Petition for an inter partes review of the challenged claims under 35 U.S.C. § 311. Paper 1^[1]("Pet."). Petitioner supported the Petition with the Declaration of Dr. Steven M. Cramer. Ex. 1002. Cytiva Bioprocess R&D AB ("Patent owner") filed a Patent owner Preliminary Response to the Petition. Paper 8.

On May 19, 2022, pursuant to 35 U.S.C. § 314(a), we instituted trial ("Decision" or "Dec." (Paper 10)) to determine whether any challenged claim of the '007 patent is unpatentable.

In IPR2022-00042, Petitioner asserts the following grounds of unpatentability (Pet. 4):

Claim(s) Challenged 35 U.S.C. §^[2] Reference(s)/Basis

1-11, 20-29

103(a)

Linhult, Abrahmsén

1-14, 16-32, 34-37

103(a)

Linhult, Hober

1-14, 16-32, 34-37

103(a)

Linhult, Abrahmsén, Hober

1-14, 16-32, 34-37

103(a)

Abrahmsén, Hober

In IPR2022-00045, Petitioner asserts the following grounds of unpatentability ('045 IPR Pet. 4):

Claim(s) Challenged 35 U.S.C. § Reference(s)/Basis

1-14, 16-18, 20-32, 34-36

103(a)

Berg, Linhult

4-8, 10, 19, 22-26, 28, 37

103(a)

Berg, Linhult, Hober

1-3, 9, 10, 12-14, 16-18, 20, 21, 27, 28, 30-32, 34-36

103(a)

Berg, Abrahmsén

4-8, 10, 11, 19, 22, 26, 28, 29, 37

103(a)

Berg, Abrahmsén, Hober

Patent Owner filed a Patent Owner Response to the Petition. Paper 15 ("PO Resp."). Patent Owner supported the Response with the Declaration of Dr. Daniel Bracewell (Ex. 2025). See PO Resp., iv (Exhibit List). Petitioner filed a Reply to the Patent Owner Response. Paper 28 ("Reply"). Petitioner supported the Reply with a Reply Declaration from Dr. Steven M. Cramer. Ex. 1061. Patent Owner filed a Sur-reply to Petitioner's Reply. Paper 34 ("Sur-reply").

On February 16, 2023, the parties presented arguments at an oral hearing. Paper 35. The hearing transcript has been entered in the record. Paper 39 ("Tr.").

For the reasons set forth below, we determine that Petitioner has shown by a preponderance of the evidence that claims 1-10, 12-14, 16-28, 30-32, and 34-37 of the '007 patent are unpatentable, but find that Petitioner has not shown by a preponderance of the evidence that claims 11 and 29 are unpatentable.

D. Related Matters

The '007 patent is at issue in Cytiva Bioprocess R&D et al. v. JSR Corp. et al., Case No. 21-310-RGA (D. Del.). Pet. 2; Paper 5, 1.

In addition to the '007 patent, Petitioner filed Petitions for inter partes review of related U.S. patents as follows: U.S. Patent No. 10,343,142 B2 ("the '142 patent") in IPR2022-00041 and IPR2022-00044; and U.S. Patent No. 10,213,765 B2 ("the '765 patent") in IPR2022-00036 and IPR2022-00043. Pet. 2-3; Paper 5, 1-2. The '007 patent is a continuation of the '142 patent which is a continuation of the '765 patent. Ex. 1001, code (60).

E. Subject matter background

Antibodies (also called immunoglobulins) are glycoproteins, which specifically recognize foreign molecules. These recognized foreign molecules are called antigens. Ex. 2001, 1. A schematic representation of the structure of a conventional IgG and fragments is shown below:

(Image Omitted)

The figure (Ex. 2001, 2 (Fig. 1)), reproduced above, shows

the structure of a conventional IgG and fragments that can be generated thereof. The constant heavy-chain domains CH1, CH2 and CH3 are shown in yellow, the constant light-chain domain (CL) in green and the variable heavy-chain (VH) or light-chain (VL) domains in red and orange, respectively. The antigen binding domains of a conventional antibody are Fabs and Fv fragments. Fab fragments can be generated by papain digestion. Fvs are the smallest fragments with an intact antigen-binding domain. They can be generated by enzymatic approaches or expression of the relevant gene fragments (the recombinant version). In the recombinant single-chain Fv fragment, the variable domains are joined by a peptide linker. Both possible configurations of the variable domains are shown, i.e. the carboxyl terminus of VH fused to the N-terminus of VL and vice versa.

Ex. 2001, 2; see also PO Resp. 5.

Below is a generic, exemplary schematic that shows how affinity purification typically works:

(Image Omitted)

The figure shows the schematic of the loading, contact, and adsorbing step onto a column, followed by the wash step, and finally the elution and collection of the target compound. Ex. 1002 ¶ 24 (citing Ex. 1014 §§ 1.1, 4.2.); see also PO Resp. 7 ("In a typical process, the composition containing the desired antibody then is loaded onto (i.e., pumped or injected into) the column."); Pet. 6; see generally Ex. 1014.

F. The '007 patent (Ex. 1001)

The '007 patent discloses an affinity ligand useful for isolating antibodies or antibody fragments. See Ex. 1001, Abstr., 1:43-49. Affinity ligands were previously used to capture antibodies (immunoglobulin proteins) in chromatography matrices. See id. at 2:1-19. After each use, chromatography matrices are cleaned using an alkaline protocol "known as Cleaning In Place (CIP)." See id. at 2:20-54. CIP damages protein-based affinity ligands through deamidation and cleavage of peptides. Id. at 2:3554.

The '007 discloses prior efforts to genetically engineer protein-based affinity ligands to improve stability to alkaline cleaning, e.g., CIP. See id. at 2:53-54; 3:3-55. Specifically, the '007 patent describes a modified affinity ligand based on Staphylococcus protein A ("SpA"). SpA was "widely used" as an affinity chromatography ligand due to its ability to bind to antibodies without affecting the antibodies' ability to bind to antigens. Id. at 2:55-68. However, the '007 patent discloses that unmodified SpA required milder cleaning conditions than conventional CIP to prevent damaging the SpA ligand. Id. at 3:18-25. Accordingly, the '007 patent describes a need for modifying SpA to improve alkaline resistance while maintaining binding selectivity. Id. at 3:25-28.

The '007 patent describes prior efforts to modify SpA through its constituent domains. See id. at 3:42-55. SpA is composed of five domains, designated as domains E, D, A, B, and C, which are able to bind to antibodies at the antibodies' fragment crystallizable ("Fc") region. Id. at 2:60-65. The '007 patent describes a known modified SpA B-domain with "increased chemical stability at pH-values of up to about 13-14." Id. at 3:42-55 (citing WO 03/080655). The increased stability results from mutating "at least one asparagine residue . . . to an amino acid other than glutamine or aspartic acid," as it was known that asparagine and glutamine residues were sensitive to deamidation and cleavage in alkaline conditions. See id. at 2:42-47; 3:42-55.

Against this background, the '007 patent discloses an affinity ligand based on...