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 .
DETAILED ACTION
Continued Examination Under 37 CFR 1.114
1. A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 4/20/2026 has been entered.
Status of the Claims
2. Claims 1-23 are the original claims filed on 4/22/2022. In the Preliminary Amendment of 12/15/2022, claims 1-6 and 8-23 are amended and claim 7 is canceled. In the Response of 11/26/2025, Claims 1, 10, 14, 18, and 20-23 are amended, and Claims 17 and 19 are canceled. IN the Response of 4/20/2026, Claims 9-10 and 23 are amended.
Claims 1-6, 8-16, 18, and 20-23 are all the claims.
The Office Action contains new grounds for objection and rejection.
Priority
3. USAN 17/755,196, filed 04/22/2022, and having 1 RCE-type filing therein, is a National Stage entry of PCT/NL2020/050656, International Filing Date: 10/23/2020, claims foreign priority to NL 2024097, filed 10/24/2019.
Information Disclosure Statement
4. As of 5/4/2026, a total of three (3) IDS are filed: 4/22/2022; 12/15/2022; and 9/18/2024. The corresponding initialed and dated 1449 form is considered and of record.
Withdrawal of Rejections
Claim Rejections - 35 USC § 112(b)
5. The rejection of Claims 9-10 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite is withdrawn. Claim 9 is amended to the broad recitation “a lung cancer”, and while the recitation “non-small cell lung cancer (NSCLC)” which is the narrower statement of the range/limitation is deleted. Claim 10 is amended to NSCLC species of lung cancer.
Double Patenting
6. The rejection of Claims 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 1-17 of U.S. Patent No. 11279770 is withdrawn.
Applicants allege the arguments presented in reliance on the specification are improper in an ODP analysis under General Foods Corp.
Response to Arguments
The decision under General Foods Corp. is dispositive to Applicants allegations when read in full. MPEP 804(II)(B)(1) stating in part [underlined text]:
When considering whether the invention defined in a claim of an application would have been anticipated by or is an obvious variation of the invention defined in the claim of a patent or copending application, no part of the reference patent or application may be used as if it were prior art. General Foods Corp. v. Studiengesellschaft Kohle mbH, 972 F.2d 1272, 1281, 23 USPQ2d 1839, 1846 (Fed. Cir. 1992) (“Our precedent makes clear that the disclosure of a patent cited in support of a double patenting rejection cannot be used as though it were prior art, even where the disclosure is found in the claims”). This does not mean that one is precluded from all use of the reference patent or application disclosure to understand the meaning of the reference claims.
Here is the case where the claims are drawn to methods of treatment in a patient using a particular compound where under the same provision in the MPEP at 804(II)(B)(1) states in part:
In AbbVie Inc. v. Kennedy Institute of Rheumatology Trust, 764 F.3d 1366, 112 USPQ2d 1001 (Fed. Cir. 2014), the court explained that it is also proper to look at the disclosed utility in the reference disclosure to determine the overall question of obviousness in a nonstatutory double patenting context. See Sun Pharm. Indus., Ltd. V. Eli Lilly & Co., 611 F.3d 1381, 95 USPQ2d 1797 (Fed. Cir. 2010); Pfizer, Inc. v. Teva Pharm. USA, Inc., 518 F.3d 1353, 86 USPQ2d 1001 (Fed. Cir. 2008); Geneva Pharmaceuticals Inc. v. GlaxoSmithKline PLC, 349 F3d 1373, 1385-86, 68 USPQ2d 1865, 1875 (Fed. Cir. 2003).
To avoid improperly treating what is disclosed in a reference patent or copending application as if it were prior art in the context of a nonstatutory double patenting analysis, the examiner must first properly construe the scope of the reference claims. The portion of the specification of the reference that describes subject matter that falls within the scope of a reference claim may be relied upon to properly construe the scope of that claim. In particular, when ascertaining the scope of the reference’s claim(s) to a compound, the examiner should consider the reference’s specification, including all of the compound’s uses that are disclosed. See Sun Pharm. Indus., 611 F.3d at 1386-88, 95 USPQ2d at 1801-02.
Here is the case where the reference teaches a soluble human Recombinant Human NRG1-beta 1/HRG1-beta 1 EGF Domain: (396-HB-050 RND). Human NRG1-beta 1/HRGI-beta 1 EGF Domain will hereinafter be referred to as HRG at (97) but does not teach or suggest an NRG1 fusion gene expressed by the cancer in the subject of the method invention.
7. The rejection of Claims 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 12195551 is withdrawn. See the legal analysis under section 6.
Here is the case where the reference teaches neither NRG1 fusion gene nor a prior treatment.
8. The rejection of Claims 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 12139548 is withdrawn. See the legal analysis under section 6.
Here is the case where the reference teaches a soluble human Recombinant Human NRG1-beta 1/HRG1-beta 1 EGF Domain: (396-HB-050 RND). Human NRG1-beta 1/HRGI-beta 1 EGF Domain will hereinafter be referred to as HRG at (96) but does not teach or suggest an NRG1 fusion gene expressed by the cancer in the subject of the method invention.
9. The provisional rejection of claims 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 66-91 of copending Application No. 16/499,144 (reference application US 20210206875) is withdrawn. See the legal analysis under section 6.
Here is the case where the reference claims (claim 78) an Erb-B2 therapy resistant phenotype in the subject of the method but does not teach or suggest an NRG1 fusion gene expressed by the cancer in the subject of the method invention.
10. The provisional rejection of Claims 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 58-78 of copending Application No. 18/419,492 (reference application US 20240158531) is withdrawn. See the legal analysis under section 6.
Here is the case where the reference application teaches neither a NRG1 fusion gene nor a prior treatment.
11. The provisional rejection of Claims 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 58-73 of copending Application No. 18/419,527 (reference application US 20240158532) is withdrawn. See the legal analysis under section 6.
Here is the case where the reference teaches a soluble human Recombinant Human NRG1-beta 1/HRG1-beta 1 EGF Domain: (396-HB-050 RND). Human NRG1-beta 1/HRGI-beta 1 EGF Domain will hereinafter be referred to as HRG at [0257] but does not teach or suggest an NRG1 fusion gene expressed by the cancer in the subject of the method invention.
12. The provisional rejection of Claims 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 2, 4-11, 13, 16-18, 21-22, 28 and 32 of copending Application No. 18/251,832 (reference application US 20240026029) is withdrawn. See the legal analysis under section 6.
Here is the case where the reference teaches a subject having a prior treatment (claim 22) but does not teach or suggest an NRG1 fusion gene expressed by the cancer in the subject of the method invention.
Rejections Maintained
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Written Description
13. The rejection of Claims 1-6, 8-16, 18, 20 and 22-23 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement maintained for the pending claims.
The rejection of Claim 21 is withdrawn.
a) Applicants allege [0130,131 and 133] of the specification provide support for pairing the VH for MF3958 and the VH for MF3178 with any light chain, such as a common light chain, without affecting its binding specificity to ErbB-2 and ErbB-3, respectively.
Response to Arguments
Applicants’ arguments do not address the breadth and scope for the instant claimed method of treatment inventions, i.e., Claims 1 and 23.
Notably, generic claims 1 and 23 do not even require a LC much less a VL being paired with either the first and/or second antigen binding sites of the bispecific antibody. The instant claims encompass single VH domains (or a single domain comprising VH CDR1-3) for the first and second antigen binding sites for which there is no support in the application as filed.
The method invention of claim 1 requires the structure/function correlation for the instant claimed single VH domains for the bispecific antibody possessing all of the following properties:
i) a first antigen-binding site that comprises the CDR1, CDR2 and CDR3 sequences of MF3958 (SEQ ID NO:82) and that binds an extracellular part of ErbB-2 and a second antigen-binding site that comprises the CDR1, CDR2 and CDR3 sequences of MF3178 (SEQ ID NO:97) and that binds an extracellular part of ErbB-3 to the subject;
ii) the first and second antigen-binding sites bind a generic NRG1 fusion-gene, ErbB2+, ErbB3+ cancer cell, respectively, in a subject, in vivo;
iii) binding is treatment effective for the subject has progressed after having received a prior treatment with a monospecific bivalent antibody comprising antigen-binding sites that bind an extracellular part of ErbB-2 or an extracellular part of ErbB-3, or a prior treatment with a tyrosine kinase inhibitor (TKI) of ErbB-2 or chemotherapy or with a combination thereof;
iv) the first antigen-binding site binds domain I of ErbB-2 and the second antigen-binding site binds domain III of ErbB-3, wherein the affinity of the first antigen-binding site for ErbB-2 is lower than the affinity of the second antigen- binding site for ErbB-3; and
The method invention of claim 23 requires the structure/function correlation for the instant claimed single VH domains for the bispecific antibody possessing all of the following properties:
i) a first antigen-binding site that comprises the CDR1, CDR2 and CDR3 sequences of MF3958 (SEQ ID NO:82) and that binds an extracellular part of ErbB-2 and a second antigen-binding site that comprises the CDR1, CDR2 and CDR3 sequences of MF3178 (SEQ ID NO:97) and that binds an extracellular part of ErbB-3 to the subject;
ii) the first and second antigen-binding sites bind a generic NRG1 fusion-gene, ErbB2+, ErbB3+ cancer cell, respectively, in a subject, in vivo; and
iii) binding is treatment effective for the pretreatment cancer subject that had previously received an ErbB-2 or ErbB-3 targeted tumor treatment.
b) Applicants allege the specification itself exemplified such common light chains, including CDRs according to SEQ ID NOs: 1-3.
Response to Arguments
Claim 21 is withdrawn from the rejection. However, as regards the remaining claims, it is well-known in art that where structure and function are predictable (such as the genetic code correlating a specific nucleic acid sequence to amino acids), describing the function may be enough to show possession. However, simply claiming a genus of antibodies by their function (e.g., binding to an antigen) without disclosing the specific structural characteristics or amino acid sequences generally fails to meet the written description requirement unless a clear, art-recognized correlation between the antigen and the antibody's structure is demonstrated. See Smalley et al (jdsupra.com/legalnews/ pp. 1-9; March 26, 2018).
See MPEP 2163 II(A)(3)(a)(ii)
The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure “indicates that the patentee has invented species sufficient to constitute the gen[us].” See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) (“[A] patentee of a biotechnological invention cannot necessarily claim a genus after only describing a limited number of species because there may be unpredictability in the results obtained from species other than those specifically enumerated.”). “A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.”
The unpredictability for the making and using common LC/VL antibodies is established on the record but which Applicants have not yet addressed. The outstanding grounds for rejection set forth in the Office Action of 5/28/2025 are again incorporated in full herein below. The amendments to the claims and the comments in the response do not even address the outstanding matters concerning whether and/or what light chain is paired with the VH CDR1-3 for MF3958 and the VH CDR1-3 for MF3178 and the demonstrated use thereof for the breadth cancer treatment.
From the Office Action of 5/28/2025:
“Claim construction/ interpretation
The invention relates to a treatment using a bispecific antibody that comprises a first antigen-binding site that binds an extracellular part of ErbB-2 and a second antigen-binding site that binds an extracellular part of ErbB-3 for subjects that have a ErbB-2+/ErbB-3+ NRG1 fusion gene-associated cancer that has progressed after receiving a prior treatment. The prior treatment comprises a chemotherapy, a monospecific bivalent antibody & comprising antigen-binding sites that bind an extracellular part of ErbB-2 or an extracellular part of ErbB-3, or a prior treatment with Na tyrosine kinase inhibitor (TKI) of ErbB-2 or with a combination thereof.
“antigen-binding site”: the specification is unequivocal that the binding site can be single domain such as a VVH or VL from an antibody.
[0122] In one embodiment an antibody variable domain comprises a heavy chain variable region (VH) and a light chain variable region (VL). The antigen-binding site can be present in the combined VH/VL variable domain, or in only the VH region or only the VL region. When the antigen-binding site is present in only one of the two regions of the variable domain, the counterpart variable region can contribute to the folding and/or stability of the binding variable region, but does not significantly contribute to the binding of the antigen itself.
“treatment” or “treating”: the specification supports the prevention of progression or recurrence of extant cancer growth but does not imply that the bispecific antibody is cancer preventative in a naïve subject:
[0118] The term “therapeutic amount” or “effective amount” refers to an amount of an agent or combination of agents that provides the desired biological, therapeutic, and/or prophylactic result. That result can be reduction, amelioration, palliation, lessening, delaying, and/or alleviation of one or more of the signs, symptoms, or causes of a disease, or any other desired alteration of a biological system. In some embodiments, a therapeutic amount is an amount sufficient to delay tumor development. In some embodiments, a therapeutic amount is an amount sufficient to prevent or delay tumor recurrence.
The claimed method is interpreted as requiring the bispecific antibody not only overcome tolerance of the subject to the prior art therapies but is treatment effective, in vivo, for the NRG1 fusion-gene, ErbB2+, ErbB3+ cancer.
Status of single domain antibodies in the art
The current field of art for single domain antibodies (VH or VL dAb) recognizes the potential for these structures in numerous applications as well as the unpredictability of their binding absent some engineering of residues to maintain specificity or stability. See for example, Krah et al. (Immunopharmacology and Immunotoxicology, 38:1, 21-28 (2016)):
“In contrast to the naturally evolved equivalent in camelids and sharks, early studies
revealed that single human VH domains are prone to aggregation and exhibit poor solubility, which is caused by solvent exposure of hydrophobic patches in the absence of an interacting VL domain. The unfavorable properties were tackled in a variety of
mutational approaches and initial attempts aimed at the transfer of VHH key elements that attributed aggregation resistance and good solubility to camelid VHHs.”
“Nowadays, convenient generation of human dAbs with desired properties and specificities has been achieved using molecular evolution approaches (e.g. phage display) and repertoires of I or synthetic human VH or VL dAbs. However, most of the human dAb affinity reagents have been isolated from synthetic libraries that are
usually constructed with engineered single scaffolds and CDR-based diversities.”
Kim et al. (Biochimica et Biophysica Acta 1844 (2014) 1983–2001):
“Aggregation and denaturation is a concern in the manufacturability and efficacy of human diagnostic and therapeutic antibodies, as antibody aggregation has been implicated in reduced in vivo efficacy and increased immunogenicity [30–33]. Therapeutic antibodies must possess the ability to withstand physical and chemical stresses, and mechanical agitations, such as high protein concentrations, elevated temperature, extreme pH and ionic strength, freeze drying/filtration/centrifugation,
and exposure to detergents, organic solvents and proteases [34].”
“The physical stability of an antibody encompasses both colloidal [35,36] and conformational (thermodynamic) stabilities, which governs an antibody’s resistance to aggregation and unfolding. Inter- and intramolecular forces determine a protein’s propensity to aggregate — a complex process where proteins form non-native, but energetically favorable states [37]. This process can occur through multiple pathways
depending on the proteins’ biophysical properties.”
Applicants have not characterized a single example of the single domain VH or VL for the antigen-binding site in the application and use for a cancer treatment method of Claim 1 and 23, that bind the corresponding antigens much less provide the instant claimed outcome, i.e., overcoming tolerance and therapeutic effectiveness, in vivo. The ordinary artisan could reasonably conclude that Applicants were not in possession of the claimed method invention using the single domain VH or VL antibodies meeting all of the structural and functional properties required of the claims.
Status of Selecting Common Light Chains
Claims 17(i) and/or (ii), 18(i) and/or (ii) and 19 are drawn to specific VH domains that recognize the ErbB2 (i) and/or the ErbB3 (ii) antigens, respectively.
Claim 20 is drawn the light chain variable domain from the rearranged germline human kappa light chain.
Claim 21 is drawn to a light chain variable region comprising specific CDRs and that is common to/shared with both the VH for an ErbB-2 antigen and the VH for a ErbB-3 antigen in the bispecific antibody construct.
The art recognizes the unpredictability of pairing just any light chain with just any heavy chain to effectuate a common light chain being a structural/functional equivalent to the natural VL of the VH domain.
US 20150203591 (USAN 14/417,863) realizes the complexity in selecting just any common light chains as follows:
[000134] alludes to the possible difficulty (or difficulties) in selecting a light chain, or that one that interferes with binding of one or both of the heavy chains with its antigen, or fails to associate satisfactorily with one or both of the heavy chains:
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[000135] alludes to the fact that there exists a form of light chain considered to be universal and that it contains no more than four (4) somatic hypermutations so long as it allows binding and/or activation with respect to both epitopes in its association with the heavy chains:
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Finally, [000132-000133] allude to the importance of the selection means for the light chain portion by “surveying usage statistics” to identify the most frequent light chains employed in human antibodies:
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“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991). See also MPEP 2163.04.
Summary of species disclosed in the specification
Applicant’s specification discloses a single antibody clone, namely, “the bispecific antibody, MF3958 × MF3178, a full length IgG1 Bispecific Antibody Targeting HER2 and HER3, in Patients with Solid Tumors” (Example 1) in all of Examples 1-4. The specification does not specifically teach the VL domain for the clone but by implication, that the antibody is full, a VL domain is presumably present. Thus, it is not clear if the light chain or VL domain of the full antibody corresponds to the LC VL of either claims 20 or 21 of the instant claims. Thus, it is not clear if the light chain or VL domain of the of either claims 20 or 21 of the instant claims is common to each of the binding domains for MF3958 × MF3178.
Are the disclosed species representative of the claimed genus?
It is asserted that the disclosed species are not representative of the claimed genus because the most generic claims encompass any ErbB-2 (HER2) and any ErbB-3 (HER3) binding entity that is defined only by the function without an accompanying structure. The specification does not identify which VL domain, which combination of all six VLCDRs, or which subset of residues in the combination of CDRs is essential for the recited function of binding either one or both of ErbB-2 and/or ErbB-3 for the MF3958 × MF3178 clone. Neither the specification nor the prior art provides guidance as to what structural changes can be made to the parent sequences and still predictably arrive at an antibody that binds ErbB-2 and erbB-3 having a common or shared VL domain. The disclosed species therefore does not represent the claimed genus.
Has Applicant provided a common structure sufficient to visualize the genus?
Applicant has not provided a common structure sufficient to visualize the genus of all possible bispecific antibody constructs. While the disclosure provides the examples of anti-ErbB-2 VH domains and anti-ErbB-3 VH domains the specification is deficient in showing the ability of single domain antibodies being specific in binding much less capable of overcoming tolerance in extant cancer subjects and possessing therapeutic outcomes for the genus of NRG1 fusion-gene, ErbB-2+, ErbB3+ cancers. One of ordinary skill in the art would have known which of the anti-ErbB-2 VH domains and anti-ErbB-3 VH domains could be combined into a single bispecific antibody with or without a specific or common VL domain, and that would still maintain antigen selectivity and affinity.
Even in 2021, therapeutic antibodies are still not understood well enough to allow researchers to predict with certainty what modifications can be made to a primary antibody sequence such that binding is maintained. “[T]he major test of understanding is whether the changes associated with antibody maturation can be predicted with any reasonable accuracy, and whether there is sufficient information for developing therapeutic antibodies,” Vajda et al., “Progress toward improved understanding of antibody maturation,” Current Opinion in Structural Biology, 67 pp. 226-231 (2021 (PTO 892)) at p. 226, col. 2, lines 20-24.
As recently as 2020, researches were still speculating as to how to reliably identify further putative binders from antibody sequence data, see, e.g., Marks et al., “How repertoire data are changing antibody science,” J. Biol. Chem. 295(29) 9823-9837 (2020 (PTO 892)), acknowledging that “there is a vast amount of the antibody sequence space that remains unknown,” p. 9831, col. 2, para. 2.
Even though the protein sequence of ErbB-2/HER2 and ErbB-3/HER3 was known in the art, this would not have translated into knowledge of the genus of antibodies that could possibly engage the corresponding proteins. Computational and machine learning approaches for sequence-based prediction of paratope-epitope interactions are accumulating, but “it remains unclear whether antibody-antigen binding is predictable” (Akbar et al., Cell Reports 34, 108856, Mar. 16, 2021 at p. 2, col. 2, para. 2 (PTO 892)). The current state of the art continues to work toward finding an effective and efficient prediction tool for reliably assigning antibody structure based on known target epitopes. See e.g., Lo et al., “Conformational epitope matching and prediction based on protein surface spiral features,” BMC Genomics volume 22, Article number: 116 (2021 (PTO 892)) (disclosing new algorithms that calculate physicochemical properties, such as polarity, charge or the secondary structure of residues within the targeted protein sequences, and then applying quantitative matrix analyses or machine-learning algorithms to predict linear and conformational epitopes).
It is asserted that neither the specification nor the state of art at the time of filing disclosed structural features common to the members of the genus for reliably assigning different antibody structures based on sequence data for one antibody clone, which would support the premise that the inventors possessed the full scope of the claimed invention.
The rejection is maintained.
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.
14. The rejection of Claims 1, 6, 8-15, 18, 20-21 and 23 under 35 U.S.C. 103 as being obvious over Throsby et al (US 11780925 or US 12247078) is maintained for the pending claims.
a) Applicants allege the reference patents do not teach or suggest the claimed methods are efficacious following a failed therapy.
Response to Arguments
Applicants appear to have overlooked the arguments presented in the Office Action of 1/20/2026 where Throsby is cited as teaching the selection criteria for patients having received a prior treatment without benefit:
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Unless Applicants have not explained how “a failed therapy” differs in standard meaning from the progression of a cancer following previous (“having received”) treatment “with all available therapies”, thus this aspect of the rejection is maintained.
b) Applicants allege tolerance and resistance are significant issues and cast doubt on the ability of use a second therapy to successfully overcome a previous, failed therapy. For example, Frederiksen et al. (Exhibit A) showed that "patients, who have previously developed antibodies against [infliximab], are highly prone to develop antibodies also against [adalimimumab] after switching resulting in therapeutic failure." See, p. 1720. Therefore, a skilled artisan would not have been motivated or reasonably expect that switching from a previously unsuccessful therapy to the claimed antibody would be efficacious.
Response to Arguments
None of the claims are drawn to infliximab as the pretreatment monospecific bivalent antibody of instant claim 1 or claim 23.
None of the claims are drawn to adalimimumab (monospecific) as the antibody of the invention (bispecific).
The POSA would find no reason to associate and/or correlate the Frederiksen reference results to the instant claimed anti-cancer methods.
See Ex parte Murphy and Burford (217 USPQ 479 (BPAI 1982)) stating in part:
"The determination that a reference is from a nonanalogous art is therefore two-fold. First, we decide if the reference is within the field of the inventor's endeavor. If it is not, we proceed to determine whether the reference is reasonably pertinent to the particular problem with which the inventor was involved."
Frederiksen is not considered to meet either criterion under Murphy. Frederiksen is irrelevant in its teaching of infliximab, an anti-TNF alpha antibody, that bears no relationship to a ErbB-2+/Erb-B3+ cancer. See medchemexpress.com/batch_ Infliximab-DataSheet-Med.pdf. Frederiksen is irrelevant in its teaching of adalimimumab, an anti-TNF alpha antibody, that bears no relationship to a ErbB-2+/Erb-B3+ cancer. See medchemexpress.com/batch_ Adalimumab-DataSheet-MedChemExpress.pdf.
The citation of Frederiksen begs the question how the reference relates to the method invention for treating an Erb-B2+, erb-B3+ cancer.
c) Applicants allege Throsby et al. do not teach and suggest that the claimed methods are efficacious following a failed therapy, much less the specifically claimed failures of a prior treatment with a monospecific bivalent antibody comprising antigen-binding sites that bind an extracellular part of ErbB-2 or an extracellular part of ErbB-3, or a prior treatment with a tyrosine kinase inhibitor (TKI) of ErbB-2 or chemotherapy or with a combination thereof. Furthermore, there is also no reasonable expectation of success to treat the patients that failed previous therapy with the claimed bispecific antibody.
Response to Arguments
See the comments herein under section 10(a).
Even assuming, arguendo, Throsby et al. do not teach and suggest that the claimed methods are efficacious following a failed therapy, the fact that the inventor has recognized another advantage which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious. See Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985).
IN addition, Applicants rely on Attorney arguments which are not substantiated by extrinsic evidence showing that there is no reasonable expectation of success to treat the patients that failed previous therapy with the claimed bispecific antibody. MPEP 716.01 and 2145 (The arguments of counsel cannot take the place of evidence in the record. In re Schulze, 346 F.2d 600, 602, 145 USPQ 716, 718 (CCPA 1965); In re Geisler, 116 F.3d 1465, 43 USPQ2d 1362 (Fed. Cir. 1997)).
Taken together and in view of the foregoing arguments and observations, the rejection of the claims is maintained.
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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
15. The rejection of Claims 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 11780925 is maintained for the pending claims.
Applicants allege the arguments presented in reliance on the specification are improper in an ODP analysis under General Foods Corp.
Response to Arguments
The decision under General Foods Corp. is dispositive to Applicants allegations when read in full. MPEP 804(II)(B)(1) stating in part [underlined text]:
When considering whether the invention defined in a claim of an application would have been anticipated by or is an obvious variation of the invention defined in the claim of a patent or copending application, no part of the reference patent or application may be used as if it were prior art. General Foods Corp. v. Studiengesellschaft Kohle mbH, 972 F.2d 1272, 1281, 23 USPQ2d 1839, 1846 (Fed. Cir. 1992) (“Our precedent makes clear that the disclosure of a patent cited in support of a double patenting rejection cannot be used as though it were prior art, even where the disclosure is found in the claims”). This does not mean that one is precluded from all use of the reference patent or application disclosure to understand the meaning of the reference claims.
Here is the case where the claims are drawn to methods of treatment in a patient using a particular compound where under the same provision in the MPEP at 804(II)(B)(1) states in part:
In AbbVie Inc. v. Kennedy Institute of Rheumatology Trust, 764 F.3d 1366, 112 USPQ2d 1001 (Fed. Cir. 2014), the court explained that it is also proper to look at the disclosed utility in the reference disclosure to determine the overall question of obviousness in a nonstatutory double patenting context. See Sun Pharm. Indus., Ltd. v. Eli Lilly & Co., 611 F.3d 1381, 95 USPQ2d 1797 (Fed. Cir. 2010); Pfizer, Inc. v. Teva Pharm. USA, Inc., 518 F.3d 1353, 86 USPQ2d 1001 (Fed. Cir. 2008); Geneva Pharmaceuticals Inc. v. GlaxoSmithKline PLC, 349 F3d 1373, 1385-86, 68 USPQ2d 1865, 1875 (Fed. Cir. 2003).
To avoid improperly treating what is disclosed in a reference patent or copending application as if it were prior art in the context of a nonstatutory double patenting analysis, the examiner must first properly construe the scope of the reference claims. The portion of the specification of the reference that describes subject matter that falls within the scope of a reference claim may be relied upon to properly construe the scope of that claim. In particular, when ascertaining the scope of the reference’s claim(s) to a compound, the examiner should consider the reference’s specification, including all of the compound’s uses that are disclosed. See Sun Pharm. Indus., 611 F.3d at 1386-88, 95 USPQ2d at 1801-02.
Ref claims
1. A method of treating a cancer in a subject, wherein the cancer comprises an ErbB-2 and ErbB-3 positive cancer cell, the method comprising administering a bispecific antibody that comprises a first antigen-binding site that can bind an extracellular part of ErbB-2, and a second antigen-binding site that can bind an extracellular part of ErbB-3 to the subject, wherein the cell comprises an NRG1 fusion gene comprising at least a portion of the NRG1-gene fused to a sequence from a different chromosomal location; the first antigen-binding site comprising a heavy chain CDR1 comprising the amino acid sequence of SEQ ID NO:40, a heavy chain CDR2 comprising the amino acid sequence of SEQ ID NO:41, and a heavy chain CDR3 comprising the amino acid sequence SEQ ID NO:42; the second antigen-binding site comprising a heavy chain CDR1 comprising the amino acid sequence of SEQ ID NO:54, a heavy chain CDR2 comprising the amino acid sequence of SEQ ID NO:55, and a heavy chain CDR3 comprising the amino acid sequence SEQ ID NO:56; and wherein the first antigen binding site and the second antigen binding site comprise a light chain CDR1 comprising the amino acid sequence of SEQ ID NO:75, a light chain CDR2 comprising the amino acid sequence of SEQ ID NO:76, and a light chain CDR3 comprising the amino acid sequence SEQ ID NO:77.
2. The method of claim 1, wherein the NRG1 fusion gene comprises at least the 3′ end of the NRG1 gene fused to a 5′ sequence from a different chromosomal location.
3. The method of claim 1, wherein the cell is a breast cancer cell, an ovarian cancer cell, a lung cancer cell, a non-small cell lung cancer, or a metastasis thereof.
4. A method of treating cancer in a subject, wherein the cancer comprises an ErbB-2 and ErbB-3 positive tumor, the method comprising administering a bispecific antibody that comprises a first antigen-binding site that can bind an extracellular part of ErbB-2 and a second antigen-binding site that can bind an extracellular part of ErbB-3 to the subject, wherein one or more cells of the cancer express an NRG1 fusion gene comprising at least the 3′ end of the NRG1 gene fused to a 5′ sequence from a different chromosomal location; wherein the first antigen-binding site comprising a heavy chain CDR1 comprising the amino acid sequence of SEQ ID NO:40, a heavy chain CDR2 comprising the amino acid sequence of SEQ ID NO:41, and a heavy chain CDR3 comprising the amino acid sequence SEQ ID NO:42; the second antigen-binding site comprising a heavy chain CDR1 comprising the amino acid sequence of SEQ ID NO:54, a heavy chain CDR2 comprising the amino acid sequence of SEQ ID NO:55, and a heavy chain CDR3 comprising the amino acid sequence SEQ ID NO:56; and wherein the first antigen binding site and the second antigen binding site comprise a light chain CDR1 comprising the amino acid sequence of SEQ ID NO:75, a light chain CDR2 comprising the amino acid sequence of SEQ ID NO:76, and a light chain CDR3 comprising the amino acid sequence SEQ ID NO:77.
5. The method of claim 4, wherein the tumor is a breast tumor, an ovarian tumor, a lung tumor, a non-small cell lung tumor, or a metastasis thereof.
6. The method of claim 4, wherein the NRG1-fusion gene expresses a protein that comprises an NRG1 EGF-like domain.
7. The method of claim 6, wherein the NRG-fusion is a fusion of NRG1 and a gene on human chromosome 8.
8. The method of claim 7, wherein the gene on human chromosome 8 encodes an excreted protein or a cellular membrane associated protein.
9. The method of claim 4, wherein the NRG1 fusion gene is a fusion of the 3′ end of the NRG1-gene with the 5′ sequence of one of the genes selected from the group consisting of CD74; DOC4; TNFRSF10B; CLU; VAMP2; SLC3A2; RBPMS; WRN; SDC4; KIF13B; SLECA2; PDE7A; ATP1B1; CDK1; BMPR1B; MCPH1; and RAB2IL1.
10. The method of claim 4, wherein the cell or tumor is of an epithelial origin.
11. The method of claim 4, wherein the individual has undergone a therapy targeted towards EGFR inhibition.
12. The method of claim 4, wherein a ErbB-1 cell-surface receptor density; a ErbB-2 cell-surface receptor density; a ErbB-3 cell-surface receptor density; a ErbB-4 cell-surface receptor density, or a combination thereof on cells of the tumor has been determined.
13. The method of claim 12, wherein the tumor has less than 400,000 ErbB-1 cell-surface receptors per cell or less than 200,000 ErbB-1 cell-surface receptors per cell.
14. The method of claim 4, further comprising administering to the individual an ErbB-1 inhibitor.
15. The method of claim 14, wherein the ErbB-1 inhibitor is cetuximab.
Here is the case where the reference teaches the patient having undergone prior treatment at (17) Preferably, the individual has undergone a therapy that targeted towards EGFR inhibition, preferably with an EGFR binding antibody, which is preferably cetuximab.
The rejection is maintained.
16. The rejection of Claims 1-6 and 8-23 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No.12247078 is maintained for the pending claims.
Applicants allege the arguments presented in reliance on the specification are improper in an ODP analysis under General Foods Corp.
Response to Arguments
The decision under General Foods Corp. is dispositive to Applicants allegations when read in full. MPEP 804(II)(B)(1) stating in part [underlined text]:
When considering whether the invention defined in a claim of an application would have been anticipated by or is an obvious variation of the invention defined in the claim of a patent or copending application, no part of the reference patent or application may be used as if it were prior art. General Foods Corp. v. Studiengesellschaft Kohle mbH, 972 F.2d 1272, 1281, 23 USPQ2d 1839, 1846 (Fed. Cir. 1992) (“Our precedent makes clear that the disclosure of a patent cited in support of a double patenting rejection cannot be used as though it were prior art, even where the disclosure is found in the claims”). This does not mean that one is precluded from all use of the reference patent or application disclosure to understand the meaning of the reference claims.
Here is the case where the claims are drawn to methods of treatment in a patient using a particular compound where under the same provision in the MPEP at 804(II)(B)(1) states in part:
In AbbVie Inc. v. Kennedy Institute of Rheumatology Trust, 764 F.3d 1366, 112 USPQ2d 1001 (Fed. Cir. 2014), the court explained that it is also proper to look at the disclosed utility in the reference disclosure to determine the overall question of obviousness in a nonstatutory double patenting context. See Sun Pharm. Indus., Ltd. v. Eli Lilly & Co., 611 F.3d 1381, 95 USPQ2d 1797 (Fed. Cir. 2010); Pfizer, Inc. v. Teva Pharm. USA, Inc., 518 F.3d 1353, 86 USPQ2d 1001 (Fed. Cir. 2008); Geneva Pharmaceuticals Inc. v. GlaxoSmithKline PLC, 349 F3d 1373, 1385-86, 68 USPQ2d 1865, 1875 (Fed. Cir. 2003).
To avoid improperly treating what is disclosed in a reference patent or copending application as if it were prior art in the context of a nonstatutory double patenting analysis, the examiner must first properly construe the scope of the reference claims. The portion of the specification of the reference that describes subject matter that falls within the scope of a reference claim may be relied upon to properly construe the scope of that claim. In particular, when ascertaining the scope of the reference’s claim(s) to a compound, the examiner should consider the reference’s specification, including all of the compound’s uses that are disclosed. See Sun Pharm. Indus., 611 F.3d at 1386-88, 95 USPQ2d at 1801-02.
Ref claims
1. A method of treating non-small cell lung cancer or pancreatic cancer in a subject, wherein the method comprises administering to the subject a bispecific antibody that comprises a first antigen-binding site that can bind an extracellular part of ErbB-2, and a second antigen-binding site that can bind an extracellular part of ErbB-3, wherein cells of said cancer comprise an NRG1 fusion gene comprising at least a portion of the NRG1-gene fused to a sequence from a different chromosomal location; the first antigen-binding site comprising a heavy chain CDR1 comprising the amino acid sequence of SEQ ID NO:40, a heavy chain CDR2 comprising the amino acid sequence of SEQ ID NO: 41, and a heavy chain CDR3 comprising the amino acid sequence SEQ ID NO:42; and the second antigen-binding site comprising a heavy chain CDR1 comprising the amino acid sequence of SEQ ID NO:54, a heavy chain CDR2 comprising the amino acid sequence of SEQ ID NO: 55, and a heavy chain CDR3 comprising the amino acid sequence SEQ ID NO:56; and wherein the first antigen binding site and the second antigen binding site comprise a light chain CDR1 comprising the amino acid sequence of SEQ ID NO:75, a light chain CDR2 comprising the amino acid sequence of SEQ ID NO:76, and a light chain CDR3 comprising the amino acid sequence SEQ ID NO:77.
2. The method of claim 1, wherein the NRG1 fusion gene comprises at least the 3′ end of the NRG1-gene fused to a 5′ sequence from a different chromosomal location.
3. The method of claim 1, wherein the cancer is non-small cell lung cancer.
4. The method of claim 3, wherein the non-small cell lung cancer is of the invasive mucinous adenocarcinoma subtype.
5. The method of claim 1, wherein the cancer is pancreatic cancer.
6. The method of claim 1, wherein the cancer is a metastasis of non-small cell lung cancer.
7. The method of claim 1, wherein the NRG1-fusion gene expresses a protein that comprises an NRG1 EGF-like domain.
8. The method of claim 1, wherein the NRG-fusion is a fusion of NRG1 and a gene on human chromosome 8.
9. The method of claim 8, wherein the gene on human chromosome 8 encodes an excreted protein or a cellular membrane associated protein.
10. The method of claim 1, wherein the NRG1 fusion gene is a fusion of the 3′ end of the NRG1-gene with the 5′ sequence of one of the genes selected from the group consisting of CD74; DOC4; TNFRSFIOB; CLU; VAMP2; SLC3A2; RBPMS; WRN; SDC4; KIF13B; SLECA2; PDE7A; ATP1B1; CDK1; BMPR1B; MCPH1 and RAB2IL1.
11. The method of claim 1, wherein the cell is of an epithelial origin.
12. The method of claim 1, wherein the subject has undergone a therapy targeted towards EGFR inhibition.
13. The method of claim 1, wherein a ErbB-1 cell-surface receptor density; a ErbB-2 cell-surface receptor density; a ErbB-3 cell-surface receptor density; a ErbB-4 cell-surface receptor density, or a combination thereof on the cell has been determined.
14. The method of claim 13, characterized in that the cell has less than 400,000 ErbB-1 cell-surface receptors per cell, or less than 200,000 ErbB-1 cell-surface receptors per cell.
15. The method of claim 1, further comprising administering to the subject an ErbB-1 inhibitor.
16. The method of claim 15, wherein the ErbB-1 inhibitor is cetuximab.
17. The method of claim 1, wherein the first antigen-binding site comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:39.
18. The method of claim 1, wherein the second antigen-binding site comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:53.
19. The method of claim 1, wherein the first antigen binding site and the second antigen binding site comprise a light chain comprising the amino acid sequence of SEQ ID NO: 78.
20. The method of claim 1, wherein the bispecific antibody comprises the first antigen-binding site comprising the amino acid sequence of SEQ ID NO:39, the second antigen-binding site comprising the amino acid sequence of SEQ ID NO:53, and the common light chain comprising the amino acid sequence of SEQ ID NO: 78.
Here is the case where the reference teaches the patient having undergone prior treatment at (17) Preferably, the individual has undergone a therapy that targeted towards EGFR inhibition, preferably with an EGFR binding antibody, which is preferably cetuximab.
The rejection is maintained.
17. The provisional rejection of Claims 1-6, 8-16, 18, and 20-23 on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of copending Application No. 18/449,460 (reference application US 20240199747) is maintained for the pending claims.
Applicants allege the arguments presented in reliance on the specification are improper in an ODP analysis under General Foods Corp.
Response to Arguments
The decision under General Foods Corp. is dispositive to Applicants allegations when read in full. MPEP 804(II)(B)(1) stating in part [underlined text]:
When considering whether the invention defined in a claim of an application would have been anticipated by or is an obvious variation of the invention defined in the claim of a patent or copending application, no part of the reference patent or application may be used as if it were prior art. General Foods Corp. v. Studiengesellschaft Kohle mbH, 972 F.2d 1272, 1281, 23 USPQ2d 1839, 1846 (Fed. Cir. 1992) (“Our precedent makes clear that the disclosure of a patent cited in support of a double patenting rejection cannot be used as though it were prior art, even where the disclosure is found in the claims”). This does not mean that one is precluded from all use of the reference patent or application disclosure to understand the meaning of the reference claims.
Here is the case where the claims are drawn to methods of treatment in a patient using a particular compound where under the same provision in the MPEP at 804(II)(B)(1) states in part:
In AbbVie Inc. v. Kennedy Institute of Rheumatology Trust, 764 F.3d 1366, 112 USPQ2d 1001 (Fed. Cir. 2014), the court explained that it is also proper to look at the disclosed utility in the reference disclosure to determine the overall question of obviousness in a nonstatutory double patenting context. See Sun Pharm. Indus., Ltd. v. Eli Lilly & Co., 611 F.3d 1381, 95 USPQ2d 1797 (Fed. Cir. 2010); Pfizer, Inc. v. Teva Pharm. USA, Inc., 518 F.3d 1353, 86 USPQ2d 1001 (Fed. Cir. 2008); Geneva Pharmaceuticals Inc. v. GlaxoSmithKline PLC, 349 F3d 1373, 1385-86, 68 USPQ2d 1865, 1875 (Fed. Cir. 2003).
To avoid improperly treating what is disclosed in a reference patent or copending application as if it were prior art in the context of a nonstatutory double patenting analysis, the examiner must first properly construe the scope of the reference claims. The portion of the specification of the reference that describes subject matter that falls within the scope of a reference claim may be relied upon to properly construe the scope of that claim. In particular, when ascertaining the scope of the reference’s claim(s) to a compound, the examiner should consider the reference’s specification, including all of the compound’s uses that are disclosed. See Sun Pharm. Indus., 611 F.3d at 1386-88, 95 USPQ2d at 1801-02.
Ref claims
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Here is the case where the reference claims (Claim 14) and teaches the patient having undergone prior treatment at [0018] Preferably, the individual has undergone a therapy that targeted towards EGFR inhibition, preferably with an EGFR binding antibody, which is preferably cetuximab.
The rejection is maintained.
New Grounds for Objection
Claim Objections
18. Claim 23 is objected to because of the following informalities:
Amend claim 23 to delete the duplicate phrase “that comprises.”
Appropriate correction is required.
New Grounds for Rejection
Claim Rejections - 35 USC § 112
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.
19. Claim 22 is 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.
Claim 22 recites parenthetical text in two instances: “(with or without radiotherapy)” and “(or pemetrexed)”. It is unclear and confusing whether the parenthetical text is intended description of the invention or exemplary. It is unclear whether the limitation(s) following the parentheses are part of the claimed invention. See MPEP § 2173.05(d).
Conclusion
20. No claims are allowed.
21. Any inquiry concerning this communication or earlier communications from the examiner should be directed to LYNN A. BRISTOL whose telephone number is (571)272-6883. The examiner can normally be reached Mon-Fri 9 AM-5 PM.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Wu Julie can be reached on 571-272-5205. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/LYNN A BRISTOL/Primary Examiner, Art Unit 1643
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