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 .
Claim Status
Applicant’s amendments and remarks, filed 05/05/2026, are acknowledged.
Claims 1-31 are canceled.
Claims 32-43 are new.
Claims 32-43 are pending.
Claims 37-39 and 43 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 11/04/2025.
As such, claims 32-36 and 40-42 are pending examination and currently under consideration for patentability under 37 CFR 1.104.
DETAILED ACTION
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 05/05/2026 is acknowledged. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Withdrawn Objections
The specification objections are withdrawn. Issues regarding minor informalities and trademarks/names have been sufficiently addressed through amendments to the specification on 05/05/2026.
The claim objections are withdrawn. Issues regarding minor informalities have been sufficiently addressed through amendments to the claims filed on 05/05/2026.
Withdrawn Rejections
Applicant’s arguments, see page 6, filed 05/05/2026, with respect to claims 12 and 23 rejected under 35 USC 112(d) as allegedly being of improper dependent form have been fully considered and are persuasive. The issue regarding improper dependent subject matter have been sufficiently addressed through amendments to the claim(s). As such, the rejection under 35 USC 112(d) is withdrawn.
Applicant’s arguments, see pages 7 and 8, filed 05/05/2026, with respect to claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 rejected under 35 USC 112(b) as allegedly being indefinite have been fully considered and are persuasive. The issue regarding the claims comprising indefinite language have been sufficiently addressed through amendments to the claims. Further, Examiner acknowledges that claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 are canceled thus rendering the rejection moot. As such, the rejection under 35 USC 112(b) is withdrawn.
Applicant’s arguments, see pages 8 and 9, filed 05/05/2026, with respect to claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 rejected under 35 USC 112(a) as allegedly lacking written description have been fully considered and are persuasive. Examiner acknowledges that claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 are canceled thus rendering the rejection moot.
Applicant’s remarks, see pages 9-11, filed 05/05/2026, with respect to claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 rejected under 35 USC 102 as allegedly anticipated by Mimoto et al (US 2014/0199294 A1, publication date: 07/17/2014) and Igawa et al (US 2015/0344570 A1, publication date: 12/03/2015) have been fully considered and are persuasive. Examiner acknowledges that claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 are canceled, thus rendering the rejection moot. Further, Examiner acknowledges that instant new claim 32 recites various, specific arrangements of amino acid alterations which are not disclosed by the art. As such, the rejection of claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 under 35 USC 102 is withdrawn.
Applicant’s remarks, see pages 11 and 12, filed 05/05/2026, with respect to claims 1, 2, 4, 9, 10, 12, 13, 15, and 22-25 provisionally rejected under 35 U.S.C. 101 as claiming the same invention as that of claims 1-3, 5-6, 10-13, 15-18, and 20 of copending Application No. 18/022,342 (reference application) has been fully considered and are persuasive. Specifically, Examiner acknowledges that claims 1, 2, 4, 9, 10, 12, 13, 15, and 22-25 are canceled, thus rendering the rejection moot. Further, Examiner acknowledges that the present claims and the copending claims recite overlapping amino acid alterations, but also different amino acid alterations. As such, the provisional statutory double patenting rejection is withdrawn.
Applicant’s remarks, see pages 12-17, filed 05/05/2026, with respect to:
Claims 1-2, 4-5, 9, 12, 15-17, 23, and 25-27 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 and 7-29 of U.S. Patent No. 12,371,511 B2;
Claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-51 of U.S. Patent No. 11,673,947 B2 (patent date: 06/13/2023);
Claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 ejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-17 of U.S. Patent No. 10,766,960 in view of Mimoto et al (US 2014/0199294 A1, publication date: 07/17/2014);
Claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-39 of U.S. Patent No. 9,890,218 in view of Mimoto et al (US 2014/0199294 A1, publication date: 07/17/2014); and,
Claims 5, 16-17, and 26-27 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5-6, 10-13, and 15-20 of copending Application No. 18/022,342
have been fully considered and are persuasive. Specifically, Examiner acknowledges that claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 are canceled, thus rendering the rejections moot.
New Rejections Necessitated by Amendment
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 41 and 42 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.
The phrase “which binds to” in claim 41 makes the claim indefinite because the limitation indicates a method step; thus, it is unclear whether Applicant is claiming a composition or a method. As such, claim 41 and dependent claim 42 are rejected. Examiner suggests amending claim 41 to recite “is capable of binding to an antigen” to overcome the rejection.
Claim Rejections - 35 USC § 112(a) Written Description
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.
Claims 40-42 are rejected 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. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The MPEP states that the purpose of the written description requirement is to ensure that the inventor had possession, as of the filing date of the application, of the specific subject matter later claimed. The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention.”
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, disclosure of drawings, or by disclosure of relevant identifying characteristics, for example, structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the Applicants were in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
Claim 40 is drawn to the molecule comprising a variant Fc region of claim 32, which is an antibody.
Claim 41 is drawn to the antibody of claim 40, which binds to an antigen present on the cell surface of a target cell.
Claim 42 is drawn to the antibody of claim 41, wherein the target cell is a tumor cell.
The specification discloses the production of Fc region variants with enhanced FcγR-binding activity (see Example 1). The specification discloses that variants with symmetrically engineered CH2 domains and low-fucose antibodies made by sugar chain modifications all still had room for further enhancement of FcγR binding (see [0125]). In addition, although the variants with asymmetrically engineered CH2 domains described in prior art had greatly enhanced FcγR-binding ability compared to symmetrically-engineered Fc region variants, they had room for further improvement (see [0125]). Existing Fc region variants to be used as references for comparison were prepared as follows: First, antibody heavy chain gene H240-G1d (SEQ ID NO: 1) was produced (see [0126]). G1d is a sequence obtained by deleting C-terminal Lys and Gly from the heavy chain constant region sequence of native human IgG1 (see [0126]). Knobs-into-holes modifications were introduced into the CH3 domain of H240-G1d, and modifications for enhancing FcγR-binding were asymmetrically introduced into the CH2 domain, to produce Fc region variants to be used as references for comparison, ART1 and ART2 (see [0126]). ART1 was produced as follows: modifications for enhancing FcγR-binding, L234Y/L235Q/G236W/S239M/H268D/D270E/S298A, were introduced into the CH2 domain of H240-G1d, and Y349C/T366W were introduced into the CH3 domain, to produce H240-Kn125 (SEQ ID NO: 2) (see [0126]). In addition, D270E/K326D/A330M/K334E were introduced into the CH2 domain of H240-G1d, and D356C/T366S/L368A/Y407V were introduced into the CH3 domain, to produce H240-H1076 (SEQ ID NO: 3) (see [0126]). Similarly, an Fc region variant with enhanced binding to both FcγRIIa and FcγRIIIa, EGL-ART2, was produced (see [0127]). Further, different combinations of FcγR binding-enhancing modifications, G236A, S239D, A330L, and I332E, were symmetrically introduced into the CH2 domain to produce known FcγR binding-enhanced antibodies, EGL-SDALIE, EGL-GASDIE, and EGL-GASDALIE (see [0127]). The specification also discloses of Fc region variants that are superior to these existing variants, wherein all of these variants had L234F, L235Q, G236W, S239M, H268D, D270E, and S298A introduced into one of the heavy chains and D270E, S298A, K326D, and 334E introduced into the other heavy chain (see Table 1; [0128]).
Example 2 discloses the evaluation of FcγR-binding of Fc region variants. ART3, ART4, ART5, ART6, ART8, ART10, ART11, and ART12 were all enhanced as compared to G1d for FcγRIIIaF and FcγRIIIaV (see [0133]). These variants were also more enhanced than the existing symmetrically-modified FcγR-enhanced antibodies GASDALIE, SDALIE, GASDIE, and Afucosyl antibody for both FcγRIIIaF and FcγRIIIaV (see [0133]).
Example 3 discloses the evaluation of antibodies having modified Fc regions by ADCC reporter bioassay. Specifically, Table 3 discloses the EC50 value of each modified Fc-containing antibody induction activity to hFcγRIIIaV-mediated reporter gene. The results showed that the antibodies with modified Fc produced a stronger reporter gene activity against Hepa1-6/hEREG cells than the wildtype human IgG1 constant region, and that all these variants exhibited the activity at lower concentrations than variants with symmetrically engineered CH2 domains and low-fucose antibodies produced by sugar chain modification (see [0140]).
Example 4 discloses the evaluation of antibodies having modified Fc regions by ADCP reporter bioassay. Specifically, Table 4 discloses the EC50 value of each modified Fc-containing antibody induction activity to hFcγRIIaH-mediated reporter gene. The results showed that the antibodies with modified Fc produced a stronger reporter gene induction activity against Hepa1-6/hEREG cells than the wildtype human IgG1 constant region, and exhibited the activity at lower concentrations than variants with symmetrically engineered CH2 domains and low-fucose antibodies produced by sugar chain modifications (see [0143]). Among the variants, ART2, ART3, ART5, ART6, and ART8 were shown to have the activity at lower concentration than ART1 (see [0143]). In particular, ART3, ART6, and ART8 exhibited the activity at lower concentrations even when compared to ART2, which has more enhanced hFcγRIIaH binding (see [0143]).
Example 5 discloses the evaluation of the antitumor effect of antibodies having modified Fc regions in a syngeneic tumor cell transplant model using human FcγR transgenic mice. The specification discloses both FcγR binding-enhanced antibodies EGL-afucosyl and EGL-ART6, administered at 10 mg/kg, showed an efficacy of TGI=80 or higher on day 19 after administration; on the other hand, the control antibody EGL-G1d showed TGI=31 (see Fig. 3; [0150]). This confirmed that the in vivo antitumor effect of EGL-ART6 is also enhanced as compared to EGL-afucosyl (see [0150]).
Lastly, Example 6 discloses the evaluation of C1q-binding activity of antibodies having modified Fc regions. As shown in Fig. 4 and Fig. 5, among the variants evaluated, ART3, ART5, and ART11 had an enhanced C1q binding ability as compared to G1d (see [0155]). In addition, the C1q binding of ART1, ART2, ART4, ART6, ART10, ART12, GASDALIE, SDALIE, and GASDIE was reduced as compared to that of G1d (see [0155]). The common amino acid modifications shared by these variants with greatly reduced C1q binding include a modification at Ala330 or a modification at Ile332; these regions, in particular Ala330, are very important regions for interaction with C1q (see [0155]). On the other hand, ART3, ART5, and ART11, which had enhanced C1q binding as compared to G1d, did not have a modification introduced at position 330 or position 332, suggesting that the enhanced binding was due to the effect of the S298A modification or a modification at position 326, which is believed to improve the binding to C1q (see [0155]).
However, the specification fails to disclose that Applicant was in possession of the large genus of antibodies that bind to a large genus of antigens on the cell surface of a large genus of target cells, specifically tumor cells.
Although the specification discloses of different species of Fc region variant antibodies that target human Epiregulin (see Table 1; [0126] and [0127]), the claims are not limited to these antibodies, and are inclusive of any antibody that binds to any antigen present on the cell surface of any target cell or tumor cell. This indicates that there are hundreds, if not thousands, of possible antibodies encompassed by the claims. Thus, the claims encompass a vast genus of antibodies that have the claimed functions. However, the specification provides limited guidance on the structure required for maintaining the claimed function(s). Therefore, the specification does not provide adequate written description to identify the broad and variable genus of antibodies because, inter alia, the specification does not disclose a correlation between the necessary structure of the antibodies and the function(s) recited in the claims; and thus, the specification does not distinguish the claimed genus from others, except by function. Although the term antibody does impart some structure, the structure that is common to antibodies is generally unrelated to its specific binding function; therefore, correlation is less likely for antibodies than for other molecules. Accordingly, the specification does not define any structural features commonly possessed by the members of the genus, because while the description of an ability of the claimed substance may generically describe the molecule’s function, it does not describe the substance itself. A definition by function does not suffice to define the genus because it is only an indication of what the substance does, rather than what it is; therefore, it is only a definition of a useful result rather than a definition of what achieves the result. In addition, because the genus of substances is highly variable (i.e. each substance would necessarily have a unique structure, See MPEP 2434), the generic description of the substance is insufficient to describe the genus. Further, given the highly diverse nature of antibodies, particularly in CDRs, even one of skill in the art cannot envision the structure of an antibody by only knowing its binding characteristics. Thus, the specification does not provide substantive evidence for possession of this large and variable genus, encompassing a potentially massive number of antibodies claimed only be a functional characteristic(s) and/or partial structure.
A biomolecule sequence described only by a functional characteristic, without any known or disclosed correlation between that function and the structure of the sequence, normally is not sufficient identifying characteristics for written description purposes, even when accompanied by a method of obtaining the agent. The specification does not adequately describe the correlation between the chemical structure and function of the genus, such as structural domains or motifs that are essential and distinguish members of the genus from those excluded. Thus, the genus of antibodies has no correlation between their structure and function.
MPEP § 2163.03(V) states:
While there is a presumption that an adequate written description of the claimed invention is present in the specification as filed, In re Wertheim, 541 F.2d 257, 262, 191 USPQ 90, 96 (CCPA 1976), a question as to whether a specification provides an adequate written description may arise in the context of an original claim. An original claim may lack written description support when (1) the claim defines the invention in functional language specifying a desired result but the disclosure fails to sufficiently identify how the function is performed or the result is achieved or (2) a broad genus claim is presented but the disclosure only describes a narrow species with no evidence that the genus is contemplated. See Ariad Pharms., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1349-50 (Fed. Cir. 2010) (en banc). The written description requirement is not necessarily met when the claim language appears in ipsis verbis in the specification. "Even if a claim is supported by the specification, the language of the specification, to the extent possible, must describe the claimed invention so that one skilled in the art can recognize what is claimed. The appearance of mere indistinct words in a specification or a claim, even an original claim, does not necessarily satisfy that requirement. “Enzo Biochem, Inc. v. Gen-Probe, Inc., 323 F.3d 956, 968, 63 USPQ2d 1609, 1616 (Fed. Cir. 2002).
Applicant has not shown possession of a representative number of species of antibodies. The disclosure of only one or two 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.") (MPEP 2163).
The instant claims do not fully describe the structure of the antibody to achieve the required function. Accordingly, the specification also does not provide adequate written description to identify the broad genus of antibodies, claimed only by a function characteristic(s) and not structures per se, because inter alia, it does not describe a sufficient number and/or a sufficient variety of representative species to reflect the breadth and variation within the claimed genus. Consequently, based on the lack of information within the specification, there is evidence that a representative number and a representative variety of the numerous antibodies had not yet been identified and thus, the specification represents little more than a wish for possession. Therefore, one of skill in the art would not conclude that Applicant was in possession of the broad and highly variable genus of antibodies claimed only by a partial structure and functional characteristic(s). Thus the antibodies described by the instant claims encompasses an overly broad genus and the functional outcome.
In Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017), relying upon Ariad Pharms., Inc. v. Eli Lily & Co., 94 USPQ2d 1161 (Fed Cir. 2010), it is noted that to show invention, a patentee must convey in its disclosure that is “had possession of the claimed subject matter as of the filing date. Demonstrating possession “requires a precise definition” of the invention. To provide this precise definition” for a claim to a genus, a patentee must disclose “a representative number of species within the scope of the genus of structural features common to the members of the genus so that one of skill in the art can visualize or recognize the member of the genus” (see Amgen at page 1358). Also, it is not enough for the specification to show how to make and use the invention, i.e., to enable it (see Amgen at page 1361). An adequate written description must contain enough information about the actual makeup of the claimed products — “a precise definition, such as structure, formula, chemic name, physical properties of other properties, of species falling with the genus sufficient to distinguish the gene from other materials”, which may be present in “functional terminology when the art has established a correlation between structure and function” (Amgen page 1361). Most significant to the present case, the Court held that "knowledge of the chemical structure of an antigen [does not give] the required kind of structure-identifying information about the corresponding antibodies" (Amgen at 1361). The idea that written description of an antibody can be satisfied by the disclosure of a newly-characterized antigen “flouts basic legal principles of the written description requirement” as it “allows patentees to claim antibodies by describing something that is not the invention, i.e., the antigen... And Congress has not created a special written description requirement for antibodies” (Amgen at page 1362).
Abbvie v. Centocor (Fed. Cir. 2014) is also relevant to the instant claims. In Abbvie, the Court held that a disclosure of many different antibodies was not enough to support the genus of all neutralizing antibodies because the disclosed antibodies were very closely related to each other in structure and were not representative of the full diversity of the genus. The Court further noted that functionally defined genus claims can be inherently vulnerable to invalidity challenge for lack of written description support especially in technology fields that are highly unpredictable where it is difficult to establish a correlation between structure and function for the whole genus or to predict what would be covered by the functionally claimed genus.
The instant case has many similarities to AbbVie above. First, the claims clearly attempt to define the genus of antibodies by the function of binding to any antigen present on the cell surface of any target cell/tumor cell. As noted by AbbVie above, functionally defined genus claims can be inherently vulnerable to invalidity challenge for lack of written description. Second, there is no information in the specification based upon which one of skill in the art would conclude that the disclosed species for which applicant has identified as having the recited functions would be representative of the entire genus. The specification discloses no structure to correlate with the function. Therefore, the specification provides insufficient written description to support the genus encompassed by the claim.
Furthermore, regardless whether a compound is claimed per se or a method is claimed that entails the use of the compound, the inventor cannot lay claim to that subject matter unless he can provide a description of the compound sufficient to distinguish infringing compounds from non-infringing compounds, or infringing methods from non-infringing methods. Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920-23, 69 USPQ2d 1886, 1890-93 (Fed. Cir. 2004).
Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111, makes clear that "applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the 'written description' inquiry, whatever is now claimed." (See page 1117.) The specification does not "clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed." (See Vas-Cath at page 1116.)
Further, the skilled artisan cannot envision the detailed chemical structure of the encompassed antibodies, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. The nucleic acid and/or protein itself is required. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. In Fiddes v. Baird, 30 USPQ2d 1481, 1483, claims directed to mammalian FGF's were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence.
Finally, University of California v. Eli Lilly and Co., 43 USPQ2d 1398, 1404. 1405 held that: ... To fulfill the written description requirement, a patent specification must describe an invention and does so in sufficient detail that one skilled in the art can clearly conclude that "the inventor invented the claimed invention." Lockwood v. American Airlines Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (1997); In re Gosteli, 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989) (" [T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus, an applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using “such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2d 1966.
Regarding the encompassed antibodies, the functional characteristics of antibodies (including binding specificity and affinity are dictated on their structure. Amino acid sequence and conformation of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. For example, Vajdos et al. (J Mol Biol. 2002 Jul 5;320(2):415-28 at 416; previously submitted with the Office Action mailed on 02/05/2026) teaches that, “ … Even within the Fv, antigen binding is primarily mediated by the complementarity determining regions (CDRs), six hypervariable loops (three each in the heavy and light chains) which together present a large contiguous surface for potential antigen binding. Aside from the CDRs, the Fv also contains more highly conserved framework segments which connect the CDRs and are mainly involved in supporting the CDR loop conformations, although in some cases, framework residues also contact antigen. As an important step to understanding how a particular antibody functions, it would be very useful to assess the contributions of each CDR side-chain to antigen binding, and in so doing, to produce a functional map of the antigen-binding site." The art shows an unpredictable effect when making single versus multiple changes to any given CDR. For example, Brown et al. (J Immunol. 1996 May;156(9):3285-91 at 3290 and Tables 1 and 2; previously submitted with the Office Action mailed on 02/05/2026), describes how the VH CDR2 of a particular antibody was generally tolerant of single amino acid changes, however the antibody lost binding upon introduction of two amino changes in the same region.
The claims encompass an extremely large number of possible antibodies that have specific required functions. In the instant application, neither the art nor the specification provide a sufficient representative number of antibodies or a sufficient structure-function correlation to meet the written description requirements.
Regarding the encompassed molecules, protein chemistry is one of the most unpredictable areas of biotechnology. This unpredictability prevents prediction of the effects that a given number or location of mutation will have on a protein (such as TNF or a cytokine) as taught by Skolnick et al. (Trends Biotechnol. 2000 Jan;18(1):34-9; previously submitted with the Office Action mailed on 02/05/2026), sequence-based methods for predicting protein function are inadequate because of the multifunctional nature of proteins (see e.g. abstract). Further, just knowing the structure of the protein is also insufficient for prediction of functional sites (see e.g. abstract). Sequence to function methods cannot specifically identify complexities for proteins, such as gain and loss of function during evolution, or multiple functions possible within a cell (see e.g. page 34, right column). Skolnick advocates determining the structure of the protein, then identifying the functionally important residues since using the chemical structure to identify functional sites is more in line with how a protein actually works (see e.g. page 34, right column).
The sensitivity of proteins to alterations of even a single amino acid in a sequence are exemplified by Burgess et al. (J. Cell Biol. 111:2129-2138, 1990; previously submitted with the Office Action mailed on 02/05/2026) who teach that replacement of a single lysine residue at position 118 of acidic fibroblast growth factor by glutamic acid led to the substantial loss of heparin binding, receptor binding and biological activity of the protein and by Lazar et al. (Mol. Cell. Biol., 8:1247-1252, 1988; previously submitted with the Office Action mailed on 02/05/2026) who teach that in transforming growth factor alpha, replacement of aspartic acid at position 47 with alanine or asparagine did not affect biological activity while replacement with serine or glutamic acid sharply reduced the biological activity of the mitogen. These references demonstrate that even a single amino acid substitution will often dramatically affect the biological activity and characteristics of a protein.
Further, Miosge (Proc Natl Acad Sci U S A. 2015 Sep 15;112(37):E5189-98; previously submitted with the Office Action mailed on 02/05/2026) teach that Short of mutational studies of all possible amino acid substitutions for a protein, coupled with comprehensive functional assays, the sheer number and diversity of missense mutations that are possible for proteins means that their functional importance must presently be addressed primarily by computational inference (see e.g. page E5189, left column). However, in a study examining some of these methods, Miosge shows that there is potential for incorrect calling of mutations (see e.g. page E5196, left column, top paragraph). The authors conclude that the discordance between predicted and actual effect of missense mutations creates the potential for many false conclusions in clinical settings where sequencing is performed to detect disease-causing mutations (see e.g. page E5195, right column, last paragraph). The findings in their study show underscore the importance of interpreting variation by direct experimental measurement of the consequences of a candidate mutation, using as sensitive and specific an assay as possible (see e.g. page E5197, left column, top paragraph). Additionally, Bork (Genome Research, 2000,10:398-400; previously submitted with the Office Action mailed on 02/05/2026) clearly teaches the pitfalls associated with comparative sequence analysis for predicting protein function because of the known error margins for high-throughput computational methods. Bork specifically teaches that computational sequence analysis is far from perfect, despite the fact that sequencing itself is highly automated and accurate (p. 398, column 1). One of the reasons for the inaccuracy is that the quality of data in public sequence databases is still insufficient. This is particularly true for data on protein function. Protein function is context dependent, and both molecular and cellular aspects have to be considered (p. 398, column 2). Conclusions from the comparison analysis are often stretched with regard to protein products (p. 398, column 3). Further, although gene annotation via sequence database searches is already a routine job, even here the error rate is considerable (p. 399, column 2). Most features predicted with an accuracy of greater than 70% are of structural nature and, at best, only indirectly imply a certain functionality (see legend for table 1, page 399). As more sequences are added and as errors accumulate and propagate it becomes more difficult to infer correct function from the many possibilities revealed by database search (p. 399, paragraph bridging columns 2 and 3). The reference finally cautions that although the current methods seem to capture important features and explain general trends, 30% of those features are missing or predicted wrongly. This has to be kept in mind when processing the results further (p. 400, paragraph bridging cols 1 and 2).
One key issue is the prediction of protein function based on sequence similarity, which could be one way to identify the functional proteins that are useful in the instant claims. Kulmanov et al (Bioinformatics, 34(4), 2018, 660–668; previously submitted with the Office Action mailed on 02/05/2026), teach that there are key challenges for protein function prediction methods (see e.g. page 661, left column). These challenges arise from the difficulty identifying and accounting for the complex relationship between protein sequence structure and function (see e.g. page 661, left column). Despite significant progress in the past years in protein structure prediction, it still requires large efforts to predict protein structure with sufficient quality to be useful in function prediction (see e.g. page 661, left column). Another challenge is that proteins do not function in isolation. In particular higher level physiological functions that go beyond simple molecular interactions will require other proteins and cannot usually be predicted by considering a single protein in isolation (see e.g. page 661, left column). Due to these challenges it is not obvious what kinds of features should be used to predict the functions of a protein and whether they can be generated efficiently for a large number of proteins, such as the vast genus of proteins and peptides that may be encompassed by the instant claims (see e.g. page 661, left column).
The state of the art regarding the structure-function correlation cannot be relied upon because functional characteristics of any peptide/protein are determined by its structure as evidenced by Greenspan et al. 1999 (Defining epitopes: It's not as easy as it seems; Nature Biotechnology, 17:936-937; previously submitted with the Office Action mailed on 02/05/2026). Greenspan et al. teach that as little as one substitution of an amino acid (e.g. alanine) in a sequence results in unpredictable changes in the 3-dimenstional structure of the new peptide sequence which, in turn, results in changes in the functional activity such as binding affinity of the peptide sequence (page 936, 1st column). Greenspan et al. teach that contribution of each residue (i.e. each amino acid) cannot be estimated with any confidence if the replacement affects the properties of the free form of the molecule (page 936, 3rd column).
Given not only the teachings of Skolnick et al., Lazar et al., Burgess et al., and Greenspan et al., but also the limitations and pitfalls of using computational sequence analysis and the unknown effects of alternative splicing, post translational modification and cellular context on protein function as taught by Bork, the claimed polypeptides could not be predicted based on sequence identity. Clearly, it could not be predicted that a polypeptide or a variant that shares only partial homology with a disclosed protein or that is a fragment of a given SEQ ID NO. will function in a given manner.
The claimed invention as a whole may not be adequately described where an invention is described solely in terms of a method of its making coupled with its function and there is no described or art-recognized correlation or relationship between the structure of the invention and its function (see MPEP 2163). A patent specification must set forth enough detail to allow a person of ordinary skill in the art to understand what is claimed and to recognize that the inventor invented what is claimed. In the case of proteins, an adequate written description requires a precise definition, such as by structure, formula, chemical name, or physical properties, not a mere wish or plan for obtaining the claimed chemical invention (see Lilly, 119 F.3d at 1566 (quoting Fiers, 984 F.2d 15 1171 ). Because the specification does not describe the amino acid sequences nor any core structures for potentially numerous different antibody amino acid sequences which would have the recited dissociation constant, one of skill in the art would reasonably conclude that applicant was not in possession of the claimed genus of all polypeptides.
A key role played by the written description requirement is to prevent “attempt[s] to preempt the future before it has arrived.” Ariad at 1353, (quoting Fiers v. Revel, 984 F.2d at 1171). Upholding a patent drawn to a genus of antibodies that includes members not previously characterized or described could negatively impact the future development of species within the claimed genus of antibodies.
While "examples explicitly covering the full scope of the claim language" typically will not be required, a sufficient number of representative species must be included to "demonstrate that the patentee possessed the full scope of the [claimed] invention." Lizard tech v. Earth Resource Mapping, Inc., 424 F.3d 1336, 1345, 76 USPQ2d 1724,1732 (Fed. Cir. 2005).
In the absence of sufficient recitation of distinguishing characteristics, the specification does not provide adequate written description of the claimed genus. One of skill in the art would not recognize from the disclosure that the applicant was in possession of the claimed antibodies. Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features (see, Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916,927, 69 USPQ2d 1886, 1895 (Fed. Cir. 2004); accord Ex Parte Kubin, 2007-0819, BPAI 31 May 2007, opinion at p. 16, paragraph 1). The specification does not clearly allow persons of ordinary skill in the art to recognize that he or she invented what is claimed (see Vas-Cath at page 1116).
Without an adequate structural description of the claimed components and descriptive support on how to put them together, one of ordinary skill in the art would not be reasonably apprised that Applicant was in possession of the genus of antibodies as claimed. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. 112 is severable from its enablement provision (see page 1115).
Applicant’s Arguments
Applicant respectfully submits that the amended claims are commensurate in scope with the disclosure of the specification and are limited to the specific embodiments for which Applicant has demonstrated possession. Independent claim 32 is directed to a molecule comprising a variant Fc region that is a heterodimer of a first CH2 domain and a second CH2 domain, wherein both the first CH2 domain and the second CH2 domain are variants of a human IgG1 CH2 domain and wherein the amino acid sequence of the first CH2 domain and the second CH2 domain differ from the amino acid sequence of one another and the sequence of the human IgG1 CH2 domain by a set of specified alterations. Far from being an unbounded genus, claim 32 explicitly specifies the precise positions and types of amino acid differences present in the two polypeptide chains. These specific structural modifications are not merely exemplary; they correspond directly to the variant Fc regions identified as ART5, ART6, and ART8 in the specification, which were produced and evaluated for activity in Examples 1-2 of the present application. Specifically, the variant Fc regions recited in elements (a), (b), and (c) of independent claim 32 find direct support in the experimental data provided for variants ART5, ART6, and ART8, respectively (see, e.g., specification, Tables 1 and 2).
Furthermore, the written description requirement is satisfied because the specification provides sufficient technical detail to show that the Applicant recognized the identity of the claimed subject matter. The experimental data in the specification confirms that molecules containing these specific variant CH2 domains exhibit enhanced binding activity to activating Fcgamma receptors and/or improved selectivity between activating Fcgamma and inhibitory Fcgamma receptors, as compared to a molecule comprising the two human IgG1 CH2 domains that do not contain their respective set of amino acid alterations. Because the specification identifies the specific amino acid differences by position and identity and provides functional data proving their efficacy, a person having ordinary skill in the art would recognize that Applicant was in possession of the claimed invention at the time of filing. Accordingly, the rejections under 35 U.S.C. § 112(a) should be reconsidered and withdrawn.
Response to Arguments
Applicant's arguments filed 05/05/2026 have been fully considered but they are not persuasive. As stated above, Examiner acknowledges that claims 1-2, 4-5, 9-10, 12-13, 15-17, and 22-27 are canceled thus rendering the rejection moot. Further, Examiner acknowledges that independent claim 32 is directed to a molecule comprising a variant Fc region that is a heterodimer of a first CH2 domain and a second CH2 domain, wherein both the first CH2 domain and the second CH2 domain are variants of a human IgG1 CH2 domain and wherein the amino acid sequence of the first CH2 domain and the second CH2 domain differ from the amino acid sequence of one another and the sequence of the human IgG1 CH2 domain by a set of specified alterations. However, Applicant has not addressed the rejection regarding the antibody claimed solely by function (i.e., binding to an antigen) without providing a structure. While Applicant is entitled to use functional language in the description of claimed agents, according to MPEP 2163, an invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function. This matches the facts here. The claims require specific functionality for the antibody, but neither the instant disclosure, nor the art, provide description of the corresponding structure for that functionality or a representative number of species for the antibody. For example, the antibody is defined by its ability to bind to an antigen present on the cell surface of a target cell. In both the base claims and the dependent claims, the claims only describe what the antibody does, not what the antibody is. While the antibody comprises the variant Fc region, the antibody is not defined in any way except for its functional properties. Even when given possible sequences from which to select a fragment of a peptide that would bind to an antigen, the question remains about which one(s) of the encompassed peptides would actually perform the claimed function. While methods to identify the peptides with the required function may be routine in the art, the fact that any experimentation is required to figure out exactly what is encompassed necessarily means that applicant has not sufficiently described the claimed subject matter.
There are thousands of possible antibodies encompassed by the instant claims. One of skill in the art could not immediately envisage the encompassed species in each genus from the guidance provided in the instant specification and claims. Applicant has supplied a single species of antibodies which bind to an antigen present on the surface of a target cell/tumor cell. The claims encompass all antigens on the surface of any target cell. This encompasses an extremely broad genus of antibodies with a specific function, for which no correlating structure is provided. While one of skill in the art could likely screen for said antibodies, the mere fact that experimentation is necessary to identify the members of the genus indicates that proper description has not been provided.
The Federal Circuit has explained that a specification cannot always support expansive claim language and satisfy the requirements of 35 U.S.C. 112 "merely by clearly describing one embodiment of the thing claimed." LizardTech v. Earth Resource Mapping, Inc., 424 F.3d 1336, 1346, 76 USPQ2d 1731, 1733 (Fed. Cir. 2005). Describing a composition by its function alone typically will not suffice to sufficiently describe the composition. See Eli Lilly, 119 F.3 at 1568, 43 USPQ2d at 1406 (Holding that description of a gene' s function will not enable claims to the gene "because it is only an indication of what the gene does, rather than what it is."); see also Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen Inc. v. Chugai Pharm. Co., 927 F.2d 1200, 18 USPQ2d 1016 (Fed. Cir. 1991)). An adequate written description of a chemical invention also requires a precise definition, such as by structure, formula, chemical name, or physical properties, and not merely a wish or plan for obtaining the chemical invention claimed. See, e.g., Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 927, 69 USPQ2d 1886, 1894-95 (Fed. Cir. 2004) (The patent at issue claimed a method of selectively inhibiting PGHS-2 activity by administering a non-steroidal compound that selectively inhibits activity of the PGHS-2 gene product; however the patent did not disclose any compounds that can be used in the claimed methods. While there was a description of assays for screening compounds to identify those that inhibit the expression or activity of the PGHS-2 gene product, there was no disclosure of which peptides, polynucleotides, and small organic molecules selectively inhibit PGHS-2. The court held that "[w]ithout such disclosure, the claimed methods cannot be said to have been described.").
The Federal Circuit explained in Amgen that when an antibody is claimed, 35 U.S.C. § 112(a) requires adequate written description of the antibody itself even when preparation of such an antibody would be routine and conventional. Amgen Inc., v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017). A key role played by the written description requirement is to prevent “attempt[s] to preempt the future before it has arrived.” Ariad at 1353, (quoting Fiers v. Revel, 984 F.2d at 1171). Upholding a patent drawn to a genus of antibodies that includes members not previously characterized or described could negatively impact the future development of species within the claimed genus of antibodies. In the instant application, neither the art nor the specification provide a sufficient representative number of antibodies or a sufficient structure-function correlation to meet the written description requirements.
Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. The protein itself is required. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. In Fiddes v. Baird, 30 USPQ2d 1481, 1483, claims directed to mammalian FGF's were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence. Further, arguments relating to the isolation of an antibody with specific characteristics may be more appropriately directed to the invention' s enablement, since the method of isolating would detail how to make the invention. However, the enablement of the invention has not been rejected by the Examiner.
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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Claims 32-36 and 40-42 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 27-32 and 36-42 of copending Application No. 18/022,342 in view of Mimoto et al (US 2014/0199294 A1, publication date: 07/17/2014; previously submitted with the Office Action mailed on 02/05/2026).
With respect to instant claims 32-35, the ‘342 application is drawn to a molecule comprising a variant Fc region, that is a heterodimer of a first CH2 domain and a second CH2 domain, wherein both the first CH2 domain and the second CH2 domain are variants of a human IgG1 CH2 domain and wherein the amino acid sequences of the first CH2 domain and the second CH2 domain differ from the amino acid sequence of the human IgG1 CH2 domain by a set of amino acid alterations selected from the group consisting of (A) to (D) below: (A) (i) Phe at position 234, Gln at position 235, Typ at position 236, Met at position 239, Val at position 250, Asp at position 268, Glu at position 270, Ala at position 298, Pro at position 307, and Met at position 330 according to EU numbering in the first CH2 domain, and(ii) Val at position 250, Glu at position 270, Ala at position 298, Pro at position 307, Asp at position 326, Met at position 330 and Glu at position 334 according to EU numbering in the second CH2 domain; (B) (i) Phe at position 234, Gln at position 235, Trp at position 236, Met at position 239, Val at position 250, Asp at position 268, Glu at position 270, Ala at position 298, Pro at position 307, Met at position 330, and Glu at position 332 according to EU numbering in the first CH2 domain, and(ii) Ala at position 236, Val at position 250, Glu at position 270, Ala at position 298, Asp at position 326, Met at position 330, Glu at position 332, and Glu at position 334 according to EU numbering in the second CH2 domain; (C) (i) Phe at position 234, Gln at position 235, Trp at position 236, Met at position 239, Val at position 250, Asp at position 268, Glu at position 270, Ala at position 298, and Pro at position 307 according to EU numbering in the first CH2 domain; and (ii) Val at position 250, Glu at position 270, Ala at position 298, Pro at position 307, Asp at position 326, and Glu at position 334 according to EU numbering in the second CH2 domain; and (D) (i) Phe at position 234, Gln at position 235, Trp at position 236, Met at position 239, Val at position 250, Asp at position 268, Glu at position 270, Ala at position 298, Pro at position 307, and Glu at position 332 according to EU numbering in the first CH2 domain; and(ii) Val at position 250, Glu at position 270, Ala at position 298, Pro at position 307, Asp at position 326, Glu at position 332, and Glu at position 334 according to EU numbering in the second CH2 domain (see claims 27-31).
While the present application includes additional species “Asp at position 326” for the first domain and “Ala at position 236” for the second domain, the teachings of Mimoto et al disclose that constructs comprising 326D and/or 236A demonstrated enhanced binding to FcgRIIa R and FcgRIIa H (see Tables 52 and 53; [0656]; [0659]). Therefore, it would have been obvious to modify the teachings of the ‘342 application to add the substitutions of Mimoto et al because one would have a reasonable expectation that adding these substitutions would enhance FcgR binding.
Further, with respect to instant claim 36, the ‘342 application is drawn to the molecule comprising a variant Fc region of claim 27, wherein: (a) binding activity to at least one activating Fcy receptor selected from the group consisting of FcyRIa, FcyRIIa, and FcyRIIIa is enhanced in the variant Fc region as compared to an Fc region that does not contain the amino acid alterations; or (b) selectivity between an activating Fcy receptor and an inhibitory Fcy receptor is improved in the variant Fc region as compared to an Fc region that does not contain the amino acid alterations (see claim 32).
With respect to instant claims 40-42, the ‘342 application is drawn to the molecule comprising a variant Fc region of claim 27, which is an antibody which binds to an antigen present on the cell surface of a target cell wherein the target cell is a tumor cell (see claims 37-39).
Lastly, while the ‘342 application is also drawn to methods of using the claimed molecule, the Federal Circuit has held that obviousness-type double patenting exists for method claims that simply claim the disclosed use of a composition in the specification. See Sun Pharmaceutical Industries v. Eli Lilly and Co., 611 F.3d 1381, 1389 (2010). The instant application and the copending application are not divisional applications resulting from restriction, and therefore no protection under the provisions of 35 USC 121.
This is a provisional nonstatutory double patenting rejection.
Applicant’s Arguments
Without acquiescence to the Office's reasoning, Applicant respectfully requests that the double patenting rejection be held in abeyance until otherwise allowable subject matter is found. At that point, if the rejection has not been withdrawn, then Applicant will consider filing a Terminal Disclaimer or arguments, if necessary, to overcome the rejection. As the current claims are still in a state of change and may not be in their final state, to request a terminal disclaimer before a notice of allowance would be prejudicial to Applicant.
Response to Arguments
Applicant's arguments filed 05/05/2026 have been fully considered but they are not persuasive. Applicant is reminded that a request for a rejection to be held in abeyance does not “distinctly and specifically points out the supposed errors in the examiner’s action” as required under 37 CFR 1.111. See MPEP 714.02.
Further, Applicant is advised that a rejection under double patenting precludes the identification of allowable subject matter. Applicant has not filed a terminal disclaimer, and the claims remain rejected for reasons set forth above.
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As such, the double patenting rejection is maintained.
Conclusion
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DANAYA L MIDDLETON whose telephone number is (571)270-5479. The examiner can normally be reached M-F 9:30AM - 6PM with flex.
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/DANAYA L MIDDLETON/Examiner, Art Unit 1674
/VANESSA L. FORD/Supervisory Patent Examiner, Art Unit 1674
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