DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Election/Restrictions
Applicant’s election without traverse of Group I in the reply filed on 9/30/25 is acknowledged.
Claim Status
Claims 1-15 are pending.
Claim 15 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 9/30/25.
Claims 1-14 are currently under consideration for patentability under 37 CFR 1.104.
Information Disclosure Statement
The information disclosure statements filed on 9/12/22, 11/15/24, and 12/19/25 have been considered. Signed copies are enclosed.
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Notably, the disclosure statement filed lists a Search Report. The listing of the references cited in a Search Report itself is not considered to be an information disclosure statement (IDS) complying with 37 CFR 1.98. 37 CFR 1.98(a)(2) requires a legible copy of: (1) each foreign patent; (2) each publication or that portion which caused it to be listed; (3) for each cited pending U.S. application, the application specification including claims, and any drawing of the application, or that portion of the application which caused it to be listed including any claims directed to that portion, unless the cited pending U.S. application is stored in the Image File Wrapper (IFW) system; and (4) all other information, or that portion which caused it to be listed. In addition, each IDS must include a list of all patents, publications, applications, or other information submitted for consideration by the Office (see 37 CFR 1.98(a)(1) and (b)), and MPEP § 609.04(a), subsection I. states, "the list ... must be submitted on a separate paper." Therefore, the references cited in the Search Report have not been considered. Applicant is advised that the date of submission of any item of information or any missing element(s) will be the date of submission for purposes of determining compliance with the requirements based on the time of filing the IDS, including all "statement" requirements of 37 CFR 1.97(e). See MPEP § 609.05(a).
Note: If copies of the individual references cited on the Search Report are also cited separately on the IDS (and these references have not been lined-through) they have been considered.
Specification
Trademarks
The use of the terms CAPTO, MABSELECT, PROSEP, SuRe, AMSPHERE, NUVIA, cPRIME, POROS, TRIZMA, SEPHAROSE, FRACTOGEL, ESHMUNO, and OSPHERE, which are trade names or marks used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Claim Objections
Claim 1 is objected to because of the following informalities: the claim subparts are designated with a period. Each claim begins with a capital letter and ends with a period. Periods may not be used elsewhere in the claims except for abbreviations. See Fressola v. Manbeck, 36 USPQ2d 1211 (D.D.C. 1995). It is recommended that the claim subparts be designated with parentheses, such as “(a)” or “a)”. Appropriate correction is required.
Claim 10 is objected to because of the following informalities: the term “anti-IL17c” contains an acronym and/or abbreviation that should be spelled out upon first occurrence. Appropriate correction is required.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 3-4 and 9-12 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 3 and 4 recite the term “about”. The term “about” is not defined in the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention.
Claim 4 recites adjusting the sample to a pH about 5.2 to about 5.6, but the base claim requires adjusting the pH to a range of 6.5-7.5. It is impossible to have two completely different pH values at the same time.
Regarding claim 4, the phrase "preferably" renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Claim 9 recites the limitation "wherein the monoclonal antibody". There is insufficient antecedent basis for this limitation in the claim.
Claim 9 recites “wherein the monoclonal antibody to be purified is a monoclonal antibody”. The phrase is redundant and it is unclear what limitations are required other than a monoclonal antibody.
Claims depending from the rejected claims do not remedy the deficiency and therefore are also rejected.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 4 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 4 recites adjusting the sample to a pH about 5.2 to about 5.6, but the base claim requires adjusting the pH to a range of 6.5-7.5. Claim 4 therefore is not properly dependent from claim 1.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claim(s) 1-6, 8-9, and 13 is/are rejected under 35 U.S.C. 102(a)(1) and 35 U.S.C. 102(a)(2) as being anticipated by Althouse et al (WO 2015/070068 A1; filed 11/7/14; published 5/14/15).
Claim 1 is directed to a method for increasing the yield of an antibody in the flow through of ion exchange chromatography during antibody purification comprising the steps of: providing a sample comprising an antibody; adjusting the conductivity of the sample; processing the adjusted sample by ion exchange chromatography in flow-through mode and collecting the flow-through comprising the antibody, wherein the conductivity of the sample is adjusted with Tris to at least 10 mS/cm and wherein the pH after adjusting the conductivity is in the range of pH 6.5 to 7.5.
Claim 2 is directed to the method according to claim 1, wherein the sample comprising an antibody is an affinity chromatography eluate.
Claim 3 is directed to the method according claim 2, wherein the affinity chromatography eluate is a Protein A chromatography eluate with a pH of about 3 to about 4.
Claim 4 is directed to the method according to claim 3, wherein the pH of about 3 to about 4 of the sample is adjusted to a pH of about 5.2 to about 5.6, preferably to a pH of 5.5.
Claim 5 is directed to the method according to claim 1, wherein the conductivity of the sample is adjusted to a conductivity between 10 and 50 mS/cm.
Claim 6 is directed to the method according to claim 5, wherein the conductivity is adjusted to the range of 13 to 30 mS/cm.
Claim 7 is directed to the method according to claim 5, wherein the conductivity is adjusted to 15 mS/cm.
Claim 8 is directed to the method according to any-of the preceding claimsclaim1, wherein the ion exchange chromatography is multimodal anion exchange chromatography.
Claim 9 is directed to the method according to claim 1, wherein the monoclonal antibody to be purified is a monoclonal antibody.
Claim 10 is directed to the method according to claim 9, wherein the monoclonal antibody to be purified is an anti-IL17c antibody.
Claim 11 is directed to the method according to claim 10, wherein the monoclonal anti-IL17C antibody to be purified comprises a VH of SEQ ID NO: 8 and a VL of SEQ ID NO: 7.
Claim 12 is directed to the method according to claim 11, wherein the monoclonal anti-IL17C antibody to be purified consists of a heavy chain of SEQ ID NO:10 and a light chain of SEQ ID NO: 9.
Claim 13 is directed to the method according to claim 1, wherein the yield of the purified antibody in the flow-through is more than 75%.
Claim 14 is directed to the method according to claim 1, wherein the conductivity of the sample in step b) is adjusted with Tris in the absence of NaCl.
Regarding the limitations of instant claim 1, Althouse teaches a purification process for pharmaceutical grade monoclonal antibodies (see e.g. paragraphs [0002]-[0003]). The process can include a Protein A affinity chromatography step followed by a mixed-mode step comprising cation or anion exchange comprising a one-step or two-step process (see e.g. paragraph [0007]). The affinity eluate can be adjusted to a pH of about 5-7 and a conductivity of 3-15 mS/cm (see e.g. paragraph [0008]). In one example, a Protein A eluate was adjusted to pH 7 and 16.6 mS/cm, then polished using a Capto MMC IMPRES column in a flow through method (see e.g. Example, including paragraphs [0119]-[0120]). The ion exchange chromatography can be conducted as a flow-through mode (see e.g. paragraph [0008]). A suitable buffer for the polishing step is a Tris/NaCl buffer (see e.g. paragraph [0008]).
Regarding the limitations of instant claim 2, Althouse teaches that Protein A chromatography is affinity chromatography (see e.g. paragraph [0004]), therefore the method of Example 2 in Althouse meets the limitations of the claim.
Regarding the limitations of instant claim 3, the elution buffer for the affinity chromatography step can have a pH around 3.5 (see e.g. paragraph [0006]).
Regarding the limitations of instant claim 4, the affinity eluate can be adjusted to a pH of about 5-7 and a conductivity of 3-15 mS/cm (see e.g. paragraph [0008]). Table 2 indicates that the conductivity can be adjusted to 5 and 13 mS/cm (see e.g. page 34). Further, Althouse specifically discusses adjusting the pH to 5.0 (see e.g. paragraph [0066]).
Regarding the limitations of instant claim 5 and 6, In one example, a Protein A eluate was adjusted to pH 7 and 16.6 mS/cm, then polished using a Capto MMC IMPRES column in a flow through method (see e.g. Example, including paragraphs [0119]-[0120]). The ion exchange chromatography can be conducted as a flow-through mode (see e.g. paragraph [0008]). A suitable buffer for the polishing step is a Tris/NaCl buffer (see e.g. paragraph [0008]).
Regarding the limitations of instant claim 8, the mixed mode step can comprise an anion exchange chromatography step (see e.g. paragraph [0007]).
Regarding the limitations of instant claim 9, Althouse teaches a purification process for pharmaceutical grade monoclonal antibodies (see e.g. paragraphs [0002]-[0003]).
Regarding the limitations of instant claim 13, Table 2 of Althouse shows yields from the process of above 75% (see e.g. page 34).
Claim(s) 1-10 and 13-14 is/are rejected under 35 U.S.C. 102(a)(1) and 35 U.S.C. 102(a)(2) as being anticipated by Giese et al (WO 2017/218977 A2; filed 6/16/17; published 12/21/17).
Claim 1 is directed to a method for increasing the yield of an antibody in the flow through of ion exchange chromatography during antibody purification comprising the steps of: providing a sample comprising an antibody; adjusting the conductivity of the sample; processing the adjusted sample by ion exchange chromatography in flow-through mode and collecting the flow-through comprising the antibody, wherein the conductivity of the sample is adjusted with Tris to at least 10 mS/cm and wherein the pH after adjusting the conductivity is in the range of pH 6.5 to 7.5.
Claim 2 is directed to the method according to claim 1, wherein the sample comprising an antibody is an affinity chromatography eluate.
Claim 3 is directed to the method according claim 2, wherein the affinity chromatography eluate is a Protein A chromatography eluate with a pH of about 3 to about 4.
Claim 4 is directed to the method according to claim 3, wherein the pH of about 3 to about 4 of the sample is adjusted to a pH of about 5.2 to about 5.6, preferably to a pH of 5.5.
Claim 5 is directed to the method according to claim 1, wherein the conductivity of the sample is adjusted to a conductivity between 10 and 50 mS/cm.
Claim 6 is directed to the method according to claim 5, wherein the conductivity is adjusted to the range of 13 to 30 mS/cm.
Claim 7 is directed to the method according to claim 5, wherein the conductivity is adjusted to 15 mS/cm.
Claim 8 is directed to the method according to any-of the preceding claimsclaim1, wherein the ion exchange chromatography is multimodal anion exchange chromatography.
Claim 9 is directed to the method according to claim 1, wherein the monoclonal antibody to be purified is a monoclonal antibody.
Claim 10 is directed to the method according to claim 9, wherein the monoclonal antibody to be purified is an anti-IL17c antibody.
Claim 11 is directed to the method according to claim 10, wherein the monoclonal anti-IL17C antibody to be purified comprises a VH of SEQ ID NO: 8 and a VL of SEQ ID NO: 7.
Claim 12 is directed to the method according to claim 11, wherein the monoclonal anti-IL17C antibody to be purified consists of a heavy chain of SEQ ID NO:10 and a light chain of SEQ ID NO: 9.
Claim 13 is directed to the method according to claim 1, wherein the yield of the purified antibody in the flow-through is more than 75%.
Claim 14 is directed to the method according to claim 1, wherein the conductivity of the sample in step b) is adjusted with Tris in the absence of NaCl.
Regarding the limitations of instant claim 1, Giese teaches purification of multispecific antibodies that involves affinity chromatography using Protein A, followed by multimodal anion exchange chromatography in flow through mode (see e.g. Figure 1, and Abstract, see e.g. claim 88-89). Giese teaches that the desired pH and conductivity of the buffer can be adjusted as needed in the loading buffer or other buffers (see e.g. paragraph [0153]). Loading buffer is the buffer used to load the composition (see e.g. paragraph [0154]). The loading buffer can have a conductivity of greater than 10 mS/cm (see e.g. paragraph [0166]). The pH of the loading buffer can be 6.5, 7, or 7.5 (see e.g. paragraph [0175]). The buffer can comprise Tris HCL or Tris acetate (see e.g. paragraph [0153], [0165]). The chromatography can be carried out in flow-through mode (see e.g. paragraph [0012], [0013], [0223], claim 92).
Regarding the limitations of instant claim 2, the capture chromatography can be affinity chromatography, such as Protein A chromatography (see e.g. paragraph [0010]).
Regarding the limitations of instant claim 3, the protein A elution buffer can comprise about 150 mM acetic acid at about pH 2.9, which would fall within the “about 3” of the instant claims (see e.g. paragraph [0016]). In another example, the antibody can be eluted at a pH of 3.2 (see e.g. paragraph [0482]).
Regarding the limitations of instant claim 4, Giese teaches that the eluate from the Protein A column can have a pH adjusted to around 5.0 (see e.g. paragraph [0432]).
Regarding the limitations of instant claims 5-6, Giese teaches that the conductivity can be adjusted to 10 or 20 mS/cm (see e.g. paragraph [0166])).
Regarding the limitations of instant claim 7, Giese teaches that the conductivity can be adjusted to 15 mS/cm (see e.g. paragraph [0168]).
Regarding the limitations of instant claim 8, Giese teaches purification of multispecific antibodies that involves affinity chromatography using Protein A, followed by multimodal anion exchange chromatography in flow through mode (see e.g. Figure 1, and Abstract, see e.g. claim 88-89).
Regarding the limitations of instant claim 9, Giese teaches that the antibody can be a monoclonal antibody (see e.g. paragraph [0245]).
Regarding the limitations of instant claim 10, Giese teaches that the purified antibody can bind to IL-17c (see e.g. paragraph [0397]).
Regarding the limitations of instant claim 13, Giese teaches yields of 89% using the CAPTO Adhere column (see e.g. Table 15).
Regarding the limitations of instant claim 14, the reference describes buffer as having “sodium chloride, Tris HCL, Tris acetate…or a mixture thereof” (see e.g. paragraph [0153]). This indicates that buffers both with and without sodium chloride are anticipated.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 1-13 is/are rejected under 35 U.S.C. 103 as being unpatentable over Haas et al (WO 2017/140831 A1; filed 2/17/17; published 8/24/17) in view of Althouse et al (WO 2015/070068 A1; filed 11/7/14; published 5/14/15).
Claim 1 is directed to a method for increasing the yield of an antibody in the flow through of ion exchange chromatography during antibody purification comprising the steps of: providing a sample comprising an antibody; adjusting the conductivity of the sample; processing the adjusted sample by ion exchange chromatography in flow-through mode and collecting the flow-through comprising the antibody, wherein the conductivity of the sample is adjusted with Tris to at least 10 mS/cm and wherein the pH after adjusting the conductivity is in the range of pH 6.5 to 7.5.
Claim 2 is directed to the method according to claim 1, wherein the sample comprising an antibody is an affinity chromatography eluate.
Claim 3 is directed to the method according claim 2, wherein the affinity chromatography eluate is a Protein A chromatography eluate with a pH of about 3 to about 4.
Claim 4 is directed to the method according to claim 3, wherein the pH of about 3 to about 4 of the sample is adjusted to a pH of about 5.2 to about 5.6, preferably to a pH of 5.5.
Claim 5 is directed to the method according to claim 1, wherein the conductivity of the sample is adjusted to a conductivity between 10 and 50 mS/cm.
Claim 6 is directed to the method according to claim 5, wherein the conductivity is adjusted to the range of 13 to 30 mS/cm.
Claim 7 is directed to the method according to claim 5, wherein the conductivity is adjusted to 15 mS/cm.
Claim 8 is directed to the method according to any-of the preceding claimsclaim1, wherein the ion exchange chromatography is multimodal anion exchange chromatography.
Claim 9 is directed to the method according to claim 1, wherein the monoclonal antibody to be purified is a monoclonal antibody.
Claim 10 is directed to the method according to claim 9, wherein the monoclonal antibody to be purified is an anti-IL17c antibody.
Claim 11 is directed to the method according to claim 10, wherein the monoclonal anti-IL17C antibody to be purified comprises a VH of SEQ ID NO: 8 and a VL of SEQ ID NO: 7.
Claim 12 is directed to the method according to claim 11, wherein the monoclonal anti-IL17C antibody to be purified consists of a heavy chain of SEQ ID NO:10 and a light chain of SEQ ID NO: 9.
Claim 13 is directed to the method according to claim 1, wherein the yield of the purified antibody in the flow-through is more than 75%.
Claim 14 is directed to the method according to claim 1, wherein the conductivity of the sample in step b) is adjusted with Tris in the absence of NaCl.
Haas et al teaches an anti-IL-17C antibody (see e.g. abstract). The antibody can comprise SEQ ID NO: 42 and 43, which set forth identical sequences to instant SEQ ID NO:9 and 10, respectively (see Haas, Table 1, especially page 35). Haas teaches that the antibody can be isolated, although a specific preferred isolation method is not identified for pharmaceutical compositions (see e.g. page 24).
Haas et al does not teach the method of instant claim 1 requiring ion exchange chromatography comprising the steps of: providing a sample comprising an antibody; adjusting the conductivity of the sample; processing the adjusted sample by ion exchange chromatography in flow-through mode and collecting the flow-through comprising the antibody, wherein the conductivity of the sample is adjusted with Tris to at least 10 mS/cm and wherein the pH after adjusting the conductivity is in the range of pH 6.5 to 7.5. Haas does not teach the dependent claim limitations for the method steps.
Althouse teaches a purification process for pharmaceutical grade monoclonal antibodies (see e.g. paragraphs [0002]-[0003]). The process can include a Protein A affinity chromatography step followed by a mixed-mode step comprising cation or anion exchange comprising a one-step or two-step process (see e.g. paragraph [0007]). The affinity eluate can be adjusted to a pH of about 5-7 and a conductivity of 3-15 mS/cm (see e.g. paragraph [0008]). In one example, a Protein A eluate was adjusted to pH 7 and 16.6 mS/cm, then polished using a Capto MMC IMPRES column in a flow through method (see e.g. Example, including paragraphs [0119]-[0120]). The ion exchange chromatography can be conducted as a flow-through mode (see e.g. paragraph [0008]). A suitable buffer for the polishing step is a Tris/NaCl buffer (see e.g. paragraph [0008]). Althouse teaches that Protein A chromatography is affinity chromatography (see e.g. paragraph [0004]), therefore the method of Example 2 in Althouse meets the limitations of the claim. Althouse teaches that the elution buffer for the affinity chromatography step can have a pH around 3.5 (see e.g. paragraph [0006]). Althouse teaches that the affinity eluate can be adjusted to a pH of about 5-7 and a conductivity of 3-15 mS/cm (see e.g. paragraph [0008]). Table 2 indicates that the conductivity can be adjusted to 5 and 13 mS/cm (see e.g. page 34). Further, Althouse specifically discusses adjusting the pH to 5.0 (see e.g. paragraph [0066]). Althouse teaches that in one example, a Protein A eluate was adjusted to pH 7 and 16.6 mS/cm, then polished using a Capto MMC IMPRES column in a flow through method (see e.g. Example, including paragraphs [0119]-[0120]). The ion exchange chromatography can be conducted as a flow-through mode (see e.g. paragraph [0008]). A suitable buffer for the polishing step is a Tris/NaCl buffer (see e.g. paragraph [0008]). Althouse teaches that the mixed mode step can comprise an anion exchange chromatography step (see e.g. paragraph [0007]). Althouse teaches a purification process for pharmaceutical grade monoclonal antibodies (see e.g. paragraphs [0002]-[0003]). Table 2 of Althouse shows yields from the process of above 75% (see e.g. page 34).
It would have been prima facie obvious to one of ordinary skill in the art at the time of the invention to purify the antibodies of Haas as described by Althouse to produce a pharmaceutically acceptable purity for the isolated antibody product. Haas teaches the antibody of the instant claims, but fails to provide a method for purification that would produce a pharmaceutical-grade antibody product. Althouse teaches that even standard purification processes for monoclonal antibodies often do not result in the antibody compositions of sufficient purity for use in pharmaceutical contexts (see e.g. Althouse, paragraph [0003]). Althouse remedies this by providing methods that produce an antibody composition is substantially free of process- and product-related impurities including host cell proteins ("HCPs"), leached Protein A, aggregates, and fragments (see e.g. paragraph [0005]). It would be expected, absent evidence to the contrary, that applying the isolation process of Althouse to the antibody of Haas would produce an increase in purity of the Haas antibody that would allow it to be useful as a pharmaceutical grade product. The advantages of increased purity and production of a pharmaceutical quality product provide the motivation to purify the antibody of Haas, based on the teachings of Althouse, with a reasonable expectation of success.
Furthermore, one of ordinary skilled in the art would have been motivated to optimize the pH and conductivity of the composition at various points in the process, including to adjust conductivity, since “it is the normal desire of scientists or artisans to improve upon what is already generally known”. The MPEP states the following: Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller. 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (Claimed process which was performed at a temperature between 40°C and 80°C and an acid concentration between 25% and 70% was held to be prima facie obvious over a reference process which differed from the claims only in that the reference process was performed at a temperature of 100°C and an acid concentration of 10%.); see also Peterson. 315 F.3d at 1330, 65 USPQ2d at 1382 (“The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set of percentage ranges is the optimum combination of percentages.”); In re Hoeschele, 406 F.2d 1403, 160 USPQ 809 (CCPA 1969) (Claimed elastomeric polyurethanes which fell within the broad scope of the references were held to be unpatentable thereover because, among other reasons, there was no evidence of the criticality of the claimed ranges of molecular weight or molar proportions.). For more recent cases applying this principle, see Merck & Co. Inc, v. Biocraft Laboratories Inc.. 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir.), cert, denied, 493 U.S. 975 (1989); In re Kulling. 897 F.2d 1147, 14 USPQ2d 1056 (Fed. Cir. 1990); and In re Geisler. 116 F.3d 1465, 43 USPQ2d 1362 (Fed. Cir. 1997).
Additionally, KSR International Co. v. Teleflex Inc., 127 S. Ct. 1727, 1741 (2007), discloses that if a technique has been used to improve one method, and a person of ordinary skill would recognize that it would be used in similar methods in the same way, using the technique is obvious unless its application is beyond that person’s skill. It would be obvious to apply a known technique to a known product to be used in a known method that is ready for improvement to yield predictable results. Thus, the combination of prior art references as combined provided a prima facie case of obviousness, absent convincing evidence to the contrary.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
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Claim 1-10 and 13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of U.S. Patent No. 10,259,869 in view of Althouse et al (WO 2015/070068 A1; filed 11/7/14; published 5/14/15).
Although the claims at issue are not identical, they are not patentably distinct from each other.
Claim 1 is directed to a method for increasing the yield of an antibody in the flow through of ion exchange chromatography during antibody purification comprising the steps of: providing a sample comprising an antibody; adjusting the conductivity of the sample; processing the adjusted sample by ion exchange chromatography in flow-through mode and collecting the flow-through comprising the antibody, wherein the conductivity of the sample is adjusted with Tris to at least 10 mS/cm and wherein the pH after adjusting the conductivity is in the range of pH 6.5 to 7.5.
Claim 2 is directed to the method according to claim 1, wherein the sample comprising an antibody is an affinity chromatography eluate.
Claim 3 is directed to the method according claim 2, wherein the affinity chromatography eluate is a Protein A chromatography eluate with a pH of about 3 to about 4.
Claim 4 is directed to the method according to claim 3, wherein the pH of about 3 to about 4 of the sample is adjusted to a pH of about 5.2 to about 5.6, preferably to a pH of 5.5.
Claim 5 is directed to the method according to claim 1, wherein the conductivity of the sample is adjusted to a conductivity between 10 and 50 mS/cm.
Claim 6 is directed to the method according to claim 5, wherein the conductivity is adjusted to the range of 13 to 30 mS/cm.
Claim 7 is directed to the method according to claim 5, wherein the conductivity is adjusted to 15 mS/cm.
Claim 8 is directed to the method according to any-of the preceding claimsclaim1, wherein the ion exchange chromatography is multimodal anion exchange chromatography.
Claim 9 is directed to the method according to claim 1, wherein the monoclonal antibody to be purified is a monoclonal antibody.
Claim 10 is directed to the method according to claim 9, wherein the monoclonal antibody to be purified is an anti-IL17c antibody.
Claim 11 is directed to the method according to claim 10, wherein the monoclonal anti-IL17C antibody to be purified comprises a VH of SEQ ID NO: 8 and a VL of SEQ ID NO: 7.
Claim 12 is directed to the method according to claim 11, wherein the monoclonal anti-IL17C antibody to be purified consists of a heavy chain of SEQ ID NO:10 and a light chain of SEQ ID NO: 9.
Claim 13 is directed to the method according to claim 1, wherein the yield of the purified antibody in the flow-through is more than 75%.
Claim 14 is directed to the method according to claim 1, wherein the conductivity of the sample in step b) is adjusted with Tris in the absence of NaCl.
The ‘869 patent teaches an anti-IL-17C antibody comprising heavy and light chain of SEQ ID NO:17 and 16, or SEQ ID NO:30 and 29 (see e.g. claims 1 and 5-6).
The ‘869 patent et al does not teach the method of instant claim 1 requiring ion exchange chromatography comprising the steps of: providing a sample comprising an antibody; adjusting the conductivity of the sample; processing the adjusted sample by ion exchange chromatography in flow-through mode and collecting the flow-through comprising the antibody, wherein the conductivity of the sample is adjusted with Tris to at least 10 mS/cm and wherein the pH after adjusting the conductivity is in the range of pH 6.5 to 7.5. Haas does not teach the dependent claim limitations for the method steps.
Althouse teaches a purification process for pharmaceutical grade monoclonal antibodies (see e.g. paragraphs [0002]-[0003]). The process can include a Protein A affinity chromatography step followed by a mixed-mode step comprising cation or anion exchange comprising a one-step or two-step process (see e.g. paragraph [0007]). The affinity eluate can be adjusted to a pH of about 5-7 and a conductivity of 3-15 mS/cm (see e.g. paragraph [0008]). In one example, a Protein A eluate was adjusted to pH 7 and 16.6 mS/cm, then polished using a Capto MMC IMPRES column in a flow through method (see e.g. Example, including paragraphs [0119]-[0120]). The ion exchange chromatography can be conducted as a flow-through mode (see e.g. paragraph [0008]). A suitable buffer for the polishing step is a Tris/NaCl buffer (see e.g. paragraph [0008]). Althouse teaches that Protein A chromatography is affinity chromatography (see e.g. paragraph [0004]), therefore the method of Example 2 in Althouse meets the limitations of the claim. Althouse teaches that the elution buffer for the affinity chromatography step can have a pH around 3.5 (see e.g. paragraph [0006]). Althouse teaches that the affinity eluate can be adjusted to a pH of about 5-7 and a conductivity of 3-15 mS/cm (see e.g. paragraph [0008]). Table 2 indicates that the conductivity can be adjusted to 5 and 13 mS/cm (see e.g. page 34). Further, Althouse specifically discusses adjusting the pH to 5.0 (see e.g. paragraph [0066]). Althouse teaches that in one example, a Protein A eluate was adjusted to pH 7 and 16.6 mS/cm, then polished using a Capto MMC IMPRES column in a flow through method (see e.g. Example, including paragraphs [0119]-[0120]). The ion exchange chromatography can be conducted as a flow-through mode (see e.g. paragraph [0008]). A suitable buffer for the polishing step is a Tris/NaCl buffer (see e.g. paragraph [0008]). Althouse teaches that the mixed mode step can comprise an anion exchange chromatography step (see e.g. paragraph [0007]). Althouse teaches a purification process for pharmaceutical grade monoclonal antibodies (see e.g. paragraphs [0002]-[0003]). Table 2 of Althouse shows yields from the process of above 75% (see e.g. page 34).
It would have been prima facie obvious to one of ordinary skill in the art at the time of the invention to purify the antibodies of the ‘869 patent as described by Althouse to produce a pharmaceutically acceptable purity for the isolated antibody product. The ‘869 patent teaches the antibody of the instant claims, but fails to provide a method for purification that would produce a pharmaceutical-grade antibody product. Althouse teaches that even standard purification processes for monoclonal antibodies often do not result in the antibody compositions of sufficient purity for use in pharmaceutical contexts (see e.g. Althouse, paragraph [0003]). Althouse remedies this by providing methods that produce an antibody composition is substantially free of process- and product-related impurities including host cell proteins ("HCPs"), leached Protein A, aggregates, and fragments (see e.g. paragraph [0005]). It would be expected, absent evidence to the contrary, that applying the isolation process of Althouse to the antibody of Haas would produce an increase in purity of the Haas antibody that would allow it to be useful as a pharmaceutical grade product. The advantages of increased purity and production of a pharmaceutical quality product provide the motivation to purify the antibody of the ‘869 patent, based on the teachings of Althouse, with a reasonable expectation of success.
Furthermore, one of ordinary skilled in the art would have been motivated to optimize the pH and conductivity of the composition at various points in the process, including to adjust conductivity, since “it is the normal desire of scientists or artisans to improve upon what is already generally known”. The MPEP states the following: Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller. 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (Claimed process which was performed at a temperature between 40°C and 80°C and an acid concentration between 25% and 70% was held to be prima facie obvious over a reference process which differed from the claims only in that the reference process was performed at a temperature of 100°C and an acid concentration of 10%.); see also Peterson. 315 F.3d at 1330, 65 USPQ2d at 1382 (“The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set of percentage ranges is the optimum combination of percentages.”); In re Hoeschele, 406 F.2d 1403, 160 USPQ 809 (CCPA 1969) (Claimed elastomeric polyurethanes which fell within the broad scope of the references were held to be unpatentable thereover because, among other reasons, there was no evidence of the criticality of the claimed ranges of molecular weight or molar proportions.). For more recent cases applying this principle, see Merck & Co. Inc, v. Biocraft Laboratories Inc.. 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir.), cert, denied, 493 U.S. 975 (1989); In re Kulling. 897 F.2d 1147, 14 USPQ2d 1056 (Fed. Cir. 1990); and In re Geisler. 116 F.3d 1465, 43 USPQ2d 1362 (Fed. Cir. 1997).
Additionally, KSR International Co. v. Teleflex Inc., 127 S. Ct. 1727, 1741 (2007), discloses that if a technique has been used to improve one method, and a person of ordinary skill would recognize that it would be used in similar methods in the same way, using the technique is obvious unless its application is beyond that person’s skill. It would be obvious to apply a known technique to a known product to be used in a known method that is ready for improvement to yield predictable results. Thus, the combination of prior art references as combined provided a prima facie case of obviousness, absent convincing evidence to the contrary.
Claims 1-10 and 13-14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-10 and 12-26 of copending Application No. 19/363,767 (reference application) in view of Althouse et al (WO 2015/070068 A1; filed 11/7/14; published 5/14/15).
Although the claims at issue are not identical, they are not patentably distinct from each other.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claim 1 is directed to a method for increasing the yield of an antibody in the flow through of ion exchange chromatography during antibody purification comprising the steps of: providing a sample comprising an antibody; adjusting the conductivity of the sample; processing the adjusted sample by ion exchange chromatography in flow-through mode and collecting the flow-through comprising the antibody, wherein the conductivity of the sample is adjusted with Tris to at least 10 mS/cm and wherein the pH after adjusting the conductivity is in the range of pH 6.5 to 7.5.
Claim 2 is directed to the method according to claim 1, wherein the sample comprising an antibody is an affinity chromatography eluate.
Claim 3 is directed to the method according claim 2, wherein the affinity chromatography eluate is a Protein A chromatography eluate with a pH of about 3 to about 4.
Claim 4 is directed to the method according to claim 3, wherein the pH of about 3 to about 4 of the sample is adjusted to a pH of about 5.2 to about 5.6, preferably to a pH of 5.5.
Claim 5 is directed to the method according to claim 1, wherein the conductivity of the sample is adjusted to a conductivity between 10 and 50 mS/cm.
Claim 6 is directed to the method according to claim 5, wherein the conductivity is adjusted to the range of 13 to 30 mS/cm.
Claim 7 is directed to the method according to claim 5, wherein the conductivity is adjusted to 15 mS/cm.
Claim 8 is directed to the method according to any-of the preceding claimsclaim1, wherein the ion exchange chromatography is multimodal anion exchange chromatography.
Claim 9 is directed to the method according to claim 1, wherein the monoclonal antibody to be purified is a monoclonal antibody.
Claim 10 is directed to the method according to claim 9, wherein the monoclonal antibody to be purified is an anti-IL17c antibody.
Claim 11 is directed to the method according to claim 10, wherein the monoclonal anti-IL17C antibody to be purified comprises a VH of SEQ ID NO: 8 and a VL of SEQ ID NO: 7.
Claim 12 is directed to the method according to claim 11, wherein the monoclonal anti-IL17C antibody to be purified consists of a heavy chain of SEQ ID NO:10 and a light chain of SEQ ID NO: 9.
Claim 13 is directed to the method according to claim 1, wherein the yield of the purified antibody in the flow-through is more than 75%.
Claim 14 is directed to the method according to claim 1, wherein the conductivity of the sample in step b) is adjusted with Tris in the absence of NaCl.
The reference application teaches a method of producing an antibody composition comprising providing a sample with a first pH, adjusting the pH to a second pH, adjusting the conductivity of the sample and the second pH to a third pH, processing the adjusted sample by ion exchange chromatography and collecting the antibody in a composition (see e.g. reference claim 1). The pH and conductivity can be adjusted with Tris in the absence of salt (see e.g. reference claim 1). The yield from processing is at least 75% (see e.g. reference claim 5). The antibody can be a monoclonal antibody (see e.g. reference claim 8), and the antibody can be an anti-IL-17 antibody (see e.g. reference claim 9). The chromatography can be an anion exchange chromatography (see e.g. claim 10). The second pH is about 5.2 to about 5.6 (see e.g. reference claim 12).
The reference application does not teach the specific conductivity or pH of prior to loading onto the anion exchange column, and does not teach the specific conductivities, or that the anion exchange is multimodal or in flow-through mode.
Althouse teaches a purification process for pharmaceutical grade monoclonal antibodies (see e.g. paragraphs [0002]-[0003]). The process can include a Protein A affinity chromatography step followed by a mixed-mode step comprising cation or anion exchange comprising a one-step or two-step process (see e.g. paragraph [0007]). The affinity eluate can be adjusted to a pH of about 5-7 and a conductivity of 3-15 mS/cm (see e.g. paragraph [0008]). In one example, a Protein A eluate was adjusted to pH 7 and 16.6 mS/cm, then polished using a Capto MMC IMPRES column in a flow through method (see e.g. Example, including paragraphs [0119]-[0120]). The ion exchange chromatography can be conducted as a flow-through mode (see e.g. paragraph [0008]). A suitable buffer for the polishing step is a Tris/NaCl buffer (see e.g. paragraph [0008]). Althouse teaches that Protein A chromatography is affinity chromatography (see e.g. paragraph [0004]), therefore the method of Example 2 in Althouse meets the limitations of the claim. Althouse teaches that the elution buffer for the affinity chromatography step can have a pH around 3.5 (see e.g. paragraph [0006]). Althouse teaches that the affinity eluate can be adjusted to a pH of about 5-7 and a conductivity of 3-15 mS/cm (see e.g. paragraph [0008]). Table 2 indicates that the conductivity can be adjusted to 5 and 13 mS/cm (see e.g. page 34). Further, Althouse specifically discusses adjusting the pH to 5.0 (see e.g. paragraph [0066]). Althouse teaches that in one example, a Protein A eluate was adjusted to pH 7 and 16.6 mS/cm, then polished using a Capto MMC IMPRES column in a flow through method (see e.g. Example, including paragraphs [0119]-[0120]). The ion exchange chromatography can be conducted as a flow-through mode (see e.g. paragraph [0008]). A suitable buffer for the polishing step is a Tris/NaCl buffer (see e.g. paragraph [0008]). Althouse teaches that the mixed mode step can comprise an anion exchange chromatography step (see e.g. paragraph [0007]). Althouse teaches a purification process for pharmaceutical grade monoclonal antibodies (see e.g. paragraphs [0002]-[0003]). Table 2 of Althouse shows yields from the process of above 75% (see e.g. page 34).
It would have been prima facie obvious to one of ordinary skill in the art at the time of the invention to modify the reference claimed method as described by Althouse to produce a pharmaceutically acceptable purity for the isolated antibody product. Althouse teaches that even standard purification processes for monoclonal antibodies often do not result in the antibody compositions of sufficient purity for use in pharmaceutical contexts (see e.g. Althouse, paragraph [0003]). Althouse remedies this by providing methods that produce an antibody composition is substantially free of process- and product-related impurities including host cell proteins ("HCPs"), leached Protein A, aggregates, and fragments (see e.g. paragraph [0005]). It would be expected, absent evidence to the contrary, that applying the isolation process of Althouse to the antibody of Haas would produce an increase in purity of the Haas antibody that would allow it to be useful as a pharmaceutical grade product. The advantages of increased purity and production of a pharmaceutical quality product provide the motivation to modify the purification method for an antibody according to the reference application, based on the teachings of Althouse, with a reasonable expectation of success.
Furthermore, one of ordinary skilled in the art would have been motivated to optimize the pH and conductivity of the composition at various points in the process, including to adjust conductivity, since “it is the normal desire of scientists or artisans to improve upon what is already generally known”. The MPEP states the following: Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller. 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (Claimed process which was performed at a temperature between 40°C and 80°C and an acid concentration between 25% and 70% was held to be prima facie obvious over a reference process which differed from the claims only in that the reference process was performed at a temperature of 100°C and an acid concentration of 10%.); see also Peterson. 315 F.3d at 1330, 65 USPQ2d at 1382 (“The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set of percentage ranges is the optimum combination of percentages.”); In re Hoeschele, 406 F.2d 1403, 160 USPQ 809 (CCPA 1969) (Claimed elastomeric polyurethanes which fell within the broad scope of the references were held to be unpatentable thereover because, among other reasons, there was no evidence of the criticality of the claimed ranges of molecular weight or molar proportions.). For more recent cases applying this principle, see Merck & Co. Inc, v. Biocraft Laboratories Inc.. 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir.), cert, denied, 493 U.S. 975 (1989); In re Kulling. 897 F.2d 1147, 14 USPQ2d 1056 (Fed. Cir. 1990); and In re Geisler. 116 F.3d 1465, 43 USPQ2d 1362 (Fed. Cir. 1997).
Additionally, KSR International Co. v. Teleflex Inc., 127 S. Ct. 1727, 1741 (2007), discloses that if a technique has been used to improve one method, and a person of ordinary skill would recognize that it would be used in similar methods in the same way, using the technique is obvious unless its application is beyond that person’s skill. It would be obvious to apply a known technique to a known product to be used in a known method that is ready for improvement to yield predictable results. Thus, the combination of prior art references as combined provided a prima facie case of obviousness, absent convincing evidence to the contrary.
Conclusion
No claim is allowed.
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