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
This application filed 08/09/2023 is a National Stage entry of PCT/EP2022/053621, international filing date: 02/15/2022 and claims foreign priority to 21157213.6, filed on 02/15/2021.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 08/09/2023, 09/18/2023, 01/09/2026, 05/29/2026 complies with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Status of Claims
The amendments and arguments filed on 05/29/2026 are acknowledged and have been fully considered. Claims 9, 11, 12 are cancelled. Claims 8, 10, are currently amended. Claims 1-8, 10, 13-17 are now pending and will be examined on the merits herein.
Objections/Rejections Withdrawn
Objections and/or rejections not reiterated from previous Office Action are hereby withdrawn. The following rejections and/or objections are either reiterated or newly applied, and constitute the complete set presently being applied to the instant application.
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.
Claims 1, 3, 4, 6-8, 10, 14, 15 and 17 are rejected under 35 U.S.C. 103 as being obvious over Erik Nordling et al., hereinafter Nordling (Nordling et al., Patent number US 9,982,022B2; Date: 29 May, 2018) in view of Hamideh Sabahnoo et al., hereinafter Sabahnoo (Hamideh Sabahnoo et al., European Journal of Medicinal Chemistry, 127 (2017) 1012-1024).
The applied reference has a common Applicant with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(2).
This rejection under 35 U.S.C. 103 might be overcome by: (1) a showing under 37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in accordance with 35 U.S.C.102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public disclosure under 35 U.S.C. 102(b)(2)(B); or (3) a statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing date of the claimed invention, the subject matter disclosed and the claimed invention were either owned by the same person or subject to an obligation of assignment to the same person or subject to a joint research agreement. See generally MPEP § 717.02.
Regarding claim 1, Nordling teaches SEQ ID NO: 28 (see Fig 1B) with affinity for HER2 as shown in Example 12, and having improved stability (see page 29, line 60). SEQ ID NO: 28 AEAKYAKEMRNAYWEIALLPNLTNQQKRAFIRKLYDDPSQSSELLSEAKKLSESQAPK as taught in Nordling, matches (underlined) with 55 amino acid residues (of the total 59 residues) of SEQ ID NO: 1 in the instant claim 1 (SEQ ID NO: 1 AEAKYAKEMRNAYWEIALLPNLTNQQKRAFIRKLYDDPSQSSELLSEAKK LSESQGGGC). Please note, amino acids that are identical in the sequence of Nordling (i.e. SEQ ID NO: 28) and the instant claim (SEQ ID NO: 1) are underlined. Nordling teaches that polypeptide variants disclosed, comprise a common scaffold sequence and binding specificity defined by the amino acid sequence within a binding motif (BM) (see SEQ ID NO: 63; page 26). Binding motif corresponds to positions 1-29 of the polypeptide variant sequence (see page 26, line 43). Nordling teaches disclosed polypeptides having 0-3 amino acid residues at the C-terminus. The additional amino acid residues play a role in the binding of the polypeptide, but may equally well serve other purposes, related for example to one or more of the production, purification, stabilization, coupling or detection of the polypeptide. Nordling specifically teaches that such additional amino acid residues may comprise one or more amino acid residues added for purposes of chemical coupling. An example of this is the addition of a cysteine residue at the very first or very last position in the polypeptide chain, i.e. at the N- or C-terminus. A cysteine residue to be used for chemical coupling may also be introduced by replacement of another amino acid on the surface of the protein domain, preferably on a portion of the surface that is not involved in target binding (see page 25, column 5; last 2 paragraphs).
Nordling does not teach that the additional amino acids in the C-terminus is GGGC.
Sabahnoo teaches anti-HER2 target peptide conjugated with cysteine-based chelators CGGG (Cys-Gly-Gly-Gly) (see page 1013, last paragraph Introduction). Sabahnoo teaches target peptide labelling by incorporating 99mTc to cysteine-based CGGG (Cys-Gly-Gly-Gly) (see Abstract). Sabahnoo specifically teaches that chelating moieties comprised of a combination of amino acids have advantages such as easy addition to small peptides during solid phase synthesis and increased receptor binding affinity (see page 1013, last paragraph Introduction).
Obviousness can be established by combining or modifying the teachings of the prior art to
produce the claimed invention where there is some teaching, suggestion, or motivation to do so. In re
Kahn, 441 F.3d 977, 986, 78 USPQ2d 1329, 1335 (Fed. Cir. 2006) (discussing rationale underlying the
motivation-suggestion-teaching test as a guard against using hindsight in an obviousness analysis).
Consequently, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the HER2 affinity peptide of Nordling, which corresponds to 93.2% sequence identity to the peptide in the instant application, and introduce CCCG chelator at the C-terminus, as taught in Sabahnoo to create the peptide as in the instant application. One motivated to do so would have a reasonable expectation of success as Nordling identifies SEQ ID NO: 28 as having improved stability (see page 29, line 60) and teaches that additional amino acid residues may comprise one or more amino acid residues added for chemical coupling. An example of this is the addition of a cysteine residue at the very first or very last position in the polypeptide chain, i.e. at the N- or C-terminus. Nordling further teaches, that the cysteine residue to be used for chemical coupling may also be introduced by replacement of another amino acid on the surface of the protein not involved in target binding (see page 25, column 5; last 2 paragraphs) -binding specificity as disclosed in Nordling, is position 1-29 of the polypeptide variant sequence (see page 26, line 43).
Thus, one would have recognized that applying the teaching of Nordling, on HER2 affinity peptide, to the method of Sabahnoo, as demonstrated on the HER2 binding peptide, would have yielded predictable results and improved the biological suitability of the peptide as claimed (See MPEP § 2143 I(A)(D)).
Regarding claims 3, 4 and 15, in addition to rationale as applied in claim 1, Sabahnoo teaches Technetium-99 m (99mTc; half-life, 6.02 h; g ray ¼ 142 keV) (i.e. radionuclide), in molecular imaging applications, photon energy (nearly ideal for Single Photon Emission Tomography (SPECT)), low cost, widespread availability, and low absorbed-dose burden to the patient (see page 1013, last paragraph Introduction). Embodiments of the instant specification disclose ‘radionuclide’ suitable for medical imaging as selected from the group consisting of 99mTc, 51Mn, 52mMn, 52Mn, 186Re and 188Re (see page 13, line 14); and ‘radiochelate’ as provided by the nitrogen atoms of three consecutive peptide bonds and a cysteine residue at the C-terminal of the polypeptide (see page 13, line 8).
Sabahnoo teaches that peptide conjugated with cysteine-based chelators CGGG (Cys-Gly-Gly-Gly) and CSSS (Cys-Ser-Ser-Ser) (i.e. radiochelate) for labeling with 99mTc. The 99mTc-labeling is used in vitro and in vivo for the purpose of finding a favorable HER2-targeted peptide for tumor imaging in vivo (see page 1013, last paragraph Introduction; page 1020, last paragraph; sections 2.11, 2.12, 3.10; Fig 9).
Consequently, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the peptide of Nordling, with radiochelate ‘CCCG’, and radionucleide 99mTc, as taught in Sabahnoo, to create the radiolabelled polypeptide in instant claims 3 and 4. One motivated to do so would have a reasonable expectation of success as Sabahnoo asserts that traditional methods for radiolabeling peptides with 99mTc is via stabilization of [Tc(V)O]3+ metal core with ligands of the so-called N3S type. Among heteroatom N3S type ligands, chelating moieties comprised of a combination of amino acids have advantages such as easy addition to small peptides during solid phase synthesis and increased receptor binding affinity (see page 1013, last paragraph Introduction).
Thus, one would have recognized that applying the teaching of Nordling to the method of Sabahnoo, would have yielded predictable results and improved the biological suitability of the peptide for medical imaging (See MPEP § 2143 I(A)(D)).
Regarding claims 6 and 17, including rationale as applied in claim 1, embodiments of the specification disclose pharmaceutically acceptable excipient or carrier as selected to enable or enhance the administration of radiolabeled polypeptide to a subject to be treated or imaged (see page 14; line 10). Sabahnoo teaches 99mTc-conjugated peptides diluted in saline and injected via the tail vein into healthy mice (0.1 mL/200 mCi, peptide dose z1 mg), and the biodistribution evaluated at 1, 2, 4, and 24 h postinjection using four mice for each time point (see section 2.9, page 1014).
Regarding claims 7, 8, 10 the Examiner interprets the disjunctive conjunctive ‘or’ as presenting a set of alternatives. So, in claim 7, the Examiner interprets “or” in the claims as -at least one: “treating” or “diagnosing” or “prognosing”. Embodiments of the instant specification disclose “diagnosing” as comprising in vivo imaging and establishing said diagnosis on the basis of the obtained images (see page 16, line 11). The specification discloses “prognosis” as comprising performing the method of in vivo imaging and establishing said prognosis on the basis of obtained images (see page 16, line 16). As disclosed, method of treatment of a mammalian, including human, subject having a cancer
characterized by overexpression of HER2, comprising the step of administering a therapeutically effective amount of a radiolabeled polypeptide, comprising a radionuclide suitable for
therapy, to said subject. The instant specification does not disclose a therapeutically effective amount (see page 16, line 25).
In addition to the rationale for rejection under 35 U.S.C. 103 as applied to claims 1, 3 and 4, Sabahnoo teaches SKOV3 cells as HER2 overexpressing (see Fig 2 legend, section 2.5). Imaging of HER2 expression in SKOV-3 ovarian cancer xenografts nude mice using 99mTc-cysteine-triglycine (see Fig 9) is captured using an E-CAM dual head equipped with a low energy high resolution collimeter (see section 2.12). Peptides in SKOV3 tumor bearing mice exhibit considerable tumor uptake at 1 h and 4 h. Images are acquired at 1 h and 4 h after injection (see section 3.10, Tumor imaging). Sabahnoo teaches that specific targeted molecule in combination with a suitable radionuclide, result in a selective and sensitive imaging technique (see page 1018, 2nd paragraph).
Consequently, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the peptide of Nordling, with radiochelate ‘CCCG’, and radionucleide 99mTc, as taught in Sabahnoo, and administer the radiolabeled peptide to a mammal (i.e. HER2 overexpressing SKOV3 xenograft model) and acquire images in the body of the mammal (see Fig 9). One motivated to do so would have a reasonable expectation of success as Sabahnoo specifically teaches that specific targeted molecule in combination with a suitable radionuclide, result in a selective and sensitive imaging technique (see page 1018, 2nd paragraph).
Regarding claim 14, Nordling teaches recombinant expression of a polynucleotide encoding
the desired polypeptide. The production may also be carried out using chemical synthesis of the desired polypeptide de novo (see page 29, column 13). Nordling teaches polynucleotide encoding a polypeptide or a fusion polypeptide as described. Also encompassed in Nordling is a method of producing a polypeptide or fusion polypeptide as described above comprising expressing such a polynucleotide; an expression vector comprising the polynucleotide; and a host cell comprising said expression
vector (see page 27, column 9).
Claims 1, 3, 5, 13 and 16 are rejected under 35 U.S.C. 103 as being obvious over Erik Nordling et al., hereinafter Nordling (Nordling et al., Patent number US 9,982,022B2; Date: 29 May, 2018) in view of Hamideh Sabahnoo et al., hereinafter Sabahnoo (Hamideh Sabahnoo et al., European Journal of Medicinal Chemistry, 127 (2017) 1012-1024) further in view of Lepareur et al., hereinafter Lepareur (Nicolas Lepareur et al., Current Clinical Applications in Oncology and Promising Perspectives, 6 (2019) 132).
The teachings of Nordling and Sabahnoo have been set forth above.
Additionally, regarding claims 5, 13 and 16, in addition to the rationale for rejection under 35 U.S.C. 103 as noted above, Nordling teaches SEQ ID NO: 28 polypeptide with HER2 affinity (see Example 12, see page 29, line 60). Nordling discloses that polypeptides have many applications, for example applications of therapeutic, diagnostic or prognostic significance for disease including cancer (See page 26, column 7 and 8; page 27, column 9; see claims 38 and 39). Sabahnoo teaches radiolabeled HER2 binding polypeptide with radiochelate ‘CCCG’, and radionucleide 99mTc, and imaging of HER2 expression in SKOV-3 ovarian cancer xenografts nude mice using 99mTc-cysteine-triglycine (see Fig 9).
Sabahnoo does not teach radionuclide suitable for therapy is 186Re and 188Re.
Lepareur teaches that 186Re is particularly suitable for treating small to mid-sized tumors while 188Re is a better match for larger sized tumors (see Introduction). Lepareur teaches that peptide
receptor radionuclide therapy (PRRT) demonstrates clinical effectiveness, with some radiopharmaceuticals currently approved and a many more under clinical investigation (see page 8, 2nd paragraph). Lepareur teaches that Rhenium-188 and technetium-99m exhibit similar chemical properties and represent a “theranostic pair.” Thus, preparation and targeting of 188Re agents for therapy is similar to imaging agents prepared with 99mTc, the most commonly used diagnostic radionuclide (see Abstract). Lepareur teaches that more widespread use of 188Re-radiopharmaceuticals will rely on availability of fully pharmaceutical grade generators and wide clinical proofs of its interest in radionuclide therapy, particularly with the possibility of having a matched theranostic pair with 99mTc.
Consequently, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the peptide of Nordling, with the method of Sabahnoo, and use Rhenium therapeutic radionuclide as taught in Lepareur.
One motivated to do so would have a reasonable expectation of success as Lepareur specifically teaches that 99mTc-labeled radiopharmaceuticals serve as a model to prepare 186/188Re-radiotracers using similar labeling methods (see Introduction).
Allowable Subject Matter
Claim 2 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
The following is a statement of reasons for the indication of allowable subject matter in claim 2: Claim 2 is directed to the sequence consisting of SEQ ID NO: 1. The closest prior art to SEQ ID NO: 1 is taught in Nordling et al., in SEQ ID NO: 28 and is 93.2% identical to the sequence as claimed.
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.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual 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/apply/applying-online/eterminal-disclaimer.
Claim 1 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 8 of U.S. Patent No. US 9,982, 022 B2. Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding claim 1, reference patent claims sequence comprising SEQ ID NO: 55, selected from an amino acid sequence which has at least 91% identity to SEQ ID NO: 55, which meets the limitations of the instant claim (see claims 1 and claim 8 in reference patent).
The critical limitations, that is the peptide sequence, in claim 1 are the same in the conflicting claims 1 and 8. The application depends on the inherent property of the peptide sequence. See MPEP § 2112. "[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably
new to the discoverer." Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947
(Fed. Cir. 1999). Thus, the claiming of a new use, new function or unknown property which is inherently
present in the prior art does not necessarily make the claim patentable. Although the claims at issue are not identical, they are not patentably distinct from each other. This is a nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Response to Arguments
Applicant's arguments filed 05/29/2026 have been fully considered but they are not persuasive.
Applicant argues that combining peptide scaffolds (Z-variants) with specific chelators and radionuclides is a highly unpredictable art. The rejection of record was that it would be obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to combine peptide scaffolds with chelator and radionuclide.
Applicant argues that the combination of Nordling and Sabahnoo is not obvious and relies on hindsight reasoning. In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971). One motivated to combine Nordling and Sabahnoo, would have a reasonable expectation of success, as Nordling identifies SEQ ID NO: 28 as having improved stability (see page 29, line 60) and teaches that additional amino acid residues may comprise one or more amino acid residues added for chemical coupling. An example of this is the addition of a cysteine residue at the very first or very last position in the polypeptide chain, i.e. at the N- or C-terminus. Nordling further teaches, that the cysteine residue to be used for chemical coupling may also be introduced by replacement of another amino acid on the surface of the protein not involved in target binding (see page 25, column 5; last 2 paragraphs) -binding specificity as disclosed in Nordling, is position 1-29 of the polypeptide variant sequence (see page 26, line 43). Sabahnoo teaches anti-HER2 target peptide conjugated with cysteine-based chelators CGGG (Cys-Gly-Gly-Gly) (see page 1013, last paragraph Introduction) and peptide labelling by incorporating 99mTc to cysteine-based CGGG (Cys-Gly-Gly-Gly) (see Abstract). Motivation to combine, in Sabahnoo, is that chelating moieties have advantages such as easy addition to small peptides during solid phase synthesis and increased receptor binding affinity (see page 1013, last paragraph Introduction).
Applicant argues that the modification of peptide with chelator is not a simple “plug-and-play” step and encloses a reference, Mitran et al. (2015) providing evidence of unpredictability. Examiner reminds the Applicant that "The use of patents as references is not limited to what the patentees describe as their own inventions or to the problems with which they are concerned. They are part of the literature of the art, relevant for all they contain." In re Heck, 699 F.2d 1331, 1332-33, 216 USPQ 1038, 1039 (Fed. Cir. 1983) (quoting In re Lemelson, 397 F.2d 1006, 1009, 158 USPQ 275, 277 (CCPA 1968)). A reference may be relied upon for all that it would have reasonably suggested to one having ordinary skill in the art, including nonpreferred embodiments. Merck & Co. v. Biocraft Labs., Inc. 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir. 1989), cert. denied, 493 U.S. 975 (1989). Disclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or nonpreferred embodiments. In re Susi, 440 F.2d 442, 169 USPQ 423 (CCPA 1971).
Applicant argues that Lepareur does not render the therapeutic claims obvious, is based on hindsight reasoning and that a skilled artisan would have been deterred, not motivated, by the teachings of Lepareur. Examiner would like to remind the Applicant that the rejection of record was that it would be obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to combine the teachings in Lepareur, as Lepaurer teaches that peptide receptor radionuclide therapy (PRRT) demonstrates clinical effectiveness (see page 8, 2nd paragraph), and specifically teaches that 99mTc-labeled radiopharmaceuticals serve as a model to prepare 186/188Re-radiotracers using similar labeling methods (see Introduction).
Applicant argues that the rejection under non-statutory double patenting, of the Nordling patent do not teach or suggest the GGGC modification because the claimed subject matter is non-obvious over the disclosure of Nordling. Examiner would like to remind the Applicant that the critical limitations, that is the peptide sequence, in claim 1 are the same in the conflicting claims 1 and 8. The application depends on the inherent property of the peptide sequence. See MPEP § 2112. "[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer." Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. As disclosed in the Nordling patent, SEQ ID NO: 55, is the natural result of the composition, explicitly disclosed by the instant claim “ Id. At 1195- 96, 112 USPQ2d at 1952. But see, Persion Pharms. LLC v. Alvogen Malta Operations LTD., 945 F.3d 1184, 1191, 2019 USPQ2d 494084 (Fed. Cir. 2019), where the court stated that a proper finding of inherency does not require that all limitations are taught in a single reference, and that inherency may meet a missing claim limitation when the limitation is “the natural result of the combination of prior art elements.” (see MPEP §2112 .IV).
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Correspondence
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ARCHANA VARADARAJ whose telephone number is (571)272-2366. The examiner can normally be reached Monday-Friday 10:00am-5:00pm.
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, Melissa Fisher can be reached at 5712707430. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/ARCHANA VARADARAJ/ Examiner, Art Unit 1658
/Melissa L Fisher/Supervisory Patent Examiner, Art Unit 1658
Prosecution Insights