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 .
Election/Restrictions
Applicant’s election without traverse of Group I (i.e., claims 1-2, 4-6, and 13-14 drawn to a modified BNP) in the reply filed on June 9, 2026, is acknowledged. Additionally, Applicant’s election without traverse of Species A (i.e., a single and specific modified BNP as SEQ ID NO: 1 that is modified with a polymer of 800 amino acids at the N-terminus comprising SEQ ID NO: 2 repeated 40 times) in the reply filed on June 9, 2026, is acknowledged.
Status of Claims
Claims 1-20 were originally filed on November 14, 2023.
The amendment received on June 9, 2026, canceled claims 3, 7-12, and 16; and amended claims 2-20, 22-23, 25, 27-30.
Claims 1-2, 4-6, 13-15, and 17-20 are currently pending and claims 1-2, 5-6, and 13-14 are under consideration as claims 15 and 17-20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, and claim 4 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on June 9, 2026.
Priority
The present application continuation-in-part of PCT/US2022/29436 filed May 16, 2022, and claims priority under 119(e) to U.S. Provisional Application No. 63/188,743 filed on May 14, 2021.
Sequence Interpretation
For claim 1, please note that the Examiner is interpretating the scope as open-ended requiring 100% identity to elected SEQ ID NO: 1 with any N- and/or C-terminal additions that is fused to elected SEQ ID NO: 2 repeated 40 times with any N- and/or C-terminal additions thereby resulting in a polymer comprising 800 amino acids of alanine, proline and serine. Also please note that the scope of claim 1 does not require the polymer to be directly bound to the N-terminus of the BNP sequence.
Drawings
Figure 2 is objected to because it depicts an amino acid sequence without including SEQ ID NO:. However, it is noted that the SEQ ID NO: need to be present in either the figure or the Brief Description of the Drawings. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
The drawings; in particular, Figure 5, is objected to because of the following reason:
The drawings have a line quality that is too light to be reproduced (weight of all lines and letters must be heavy enough to permit adequate reproduction) or text that is illegible (reference characters, sheet numbers, and view numbers must be plain and legible) see 37 CFR 1.84(l) and (p)(1)); See Figure 5.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
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.
Claim 13 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 13 is directed to where the half-life increase of the modified BNP (i.e., BNP covalently bound to a polymer comprising at least 600 amino acids consisting of proline, alanine, and optionally serine residues) compared to the half-life of the BNP without the polymer, when administered subcutaneously into a rat, is greater than 50-fold when the polymer is about 600 amino acids or greater. As such, it is unclear if the BNP is modified with a polymer comprising at least 600 amino acids consisting of proline, alanine, and optionally serine residues as recited in instant claim 1, or a polymer that is about 600 amino acids (i.e., any amino acids) or greater. In other words, it is unclear the structure of the modified BNP since it is administered subcutaneously into a rat with a polymer that can be shorter than 600 amino acids (i.e., about encompasses a range above and below a given value) and a polymer that is not limited to proline, alanine, and optionally serine residues. Thus, an ordinary skilled artisan would be unable to ascertain the metes and bounds with respect to modified BNP structure of claim 13.
Please note that the Examiner is interpreting the scope of claim 13 such that the modified BNP is a BNP that is modified covalently at its N-terminus with a polymer comprising at least 600 amino acids consisting of proline, alanine, and optionally serine residues
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 6 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 6 is directed to where the polymer comprises about 600-1200 amino acids. However, claim 6 is dependent upon claim 1, which recites that the length of the polymer is at least 600 amino acids. “About” encompasses a value below and above an integer. As such, “about” 600 amino acids encompasses less than 600 amino acids, which is not encompassed by the scope of claim 1. Thus, the scope of claim 6 broadens the scope of claim 1. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 103
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 set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under pre-AIA 35 U.S.C. 103(a) are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims under 35 U.S.C. 103(a), the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were made absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and invention dates of each claim that was not commonly owned at the time a later invention was made in order for the examiner to consider the applicability of 35 U.S.C. 103(c) and potential 35 U.S.C. 102(e), (f) or (g) prior art under 35 U.S.C. 103(a).
103 - KSR Examples of 'Rationales' Supporting a Conclusion of Obviousness(Consistent with the "Functional Approach" of Graham)
Further regarding 35 USC 103(a) rejections, the Supreme Court in KSR International Co. v. Teleflex Inc., 550 U.S. 398, 127 S. Ct. 1727, 82 USPQ2d 1385, 1395-97 (2007) (KSR) identified a number of rationales to support a conclusion of obviousness which are consistent with the proper "functional approach" to the determination of obviousness as laid down in Graham. The key to supporting any rejection under 35 U.S.C. 103 is the clear articulation of the reason(s) why the claimed invention would have been obvious. The Supreme Court in KSR noted that the analysis supporting a rejection under 35 U.S.C. 103 should be made explicit.
Exemplary rationales that may support a conclusion of obviousness include:
(A) Combining prior art elements according to known methods to yield predictable results;
(B) Simple substitution of one known element for another to obtain predictable results;
(C) Use of known technique to improve similar devices (methods, or products) in the same way;
(D) Applying a known technique to a known device (method, or product) ready for improvement to yield predictable results;
(E) "Obvious to try" - choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success;
(F) Known work in one field of endeavor may prompt variations of it for use in either the same field or a different one based on design incentives or other market forces if the variations are predictable to one of ordinary skill in the art;
(G) Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention.
Note that the list of rationales provided is not intended to be an all-inclusive list. Other rationales to support a conclusion of obviousness may be relied upon by Office personnel.
Also, a reference is good not only for what it teaches by direct anticipation but also for what one of ordinary skill in the art might reasonably infer from the teachings. (In re Opprecht 12 USPQ 2d 1235, 1236 (Fed Cir. 1989); In re Bode 193 USPQ 12 (CCPA) 1976).
Claims 1, 3, 5-6, and 13 are rejected under 35 U.S.C. 103 as being unpatentable over Skerra et al. WO 2008/155134 A1 published on December 24, 2008, in view of Rosen et al. US Publication No. 2007/0027306 A1 published on February 1, 2007.
For claims 1, 3 and 5-6, Skerra et al. teaches biologically active proteins (i.e., fusion proteins) comprising at least two domains where a first domain comprises an amino acid sequence having and/or mediating biological activity and a second domain comprising an amino acid sequence consisting preferably of at least about 100 amino acid residues forming a random coil conformation whereby the random coil conformation mediates an increased in vivo and/or in vitro stability of the biologically active protein (See Skerra, pg. 1, 1st paragraph; pg. 3, 4th to 5th paragraph; pg. 23, 2nd paragraph). Skerra et al. unexpectedly found that when a biologically active protein is covalently bound to a random coil domain, there was prolonged plasma half-life (See Skerra, pg. 3, last paragraph to pg. 4, 1st paragraph). The amino acid sequence adopting/having/forming random coil conformation consists of at least about 100 to 1000 amino acid residues, and more preferably of maximally about 800 amino acid residues (See Skerra, pg. 9, 2nd paragraph). The amino acid sequence forming the random coil conformation comprises alanine, serine and proline as main or unique residues (See Skerra, pg. 9, 2nd paragraph). A specific embodiment of amino acid sequence forming the random coil conformation comprising alanine, serine and proline residues is SEQ ID NO: 18, which is denoted as PAS#1 (See Skerra, pg. 11, last paragraph; pg. 14, last paragraph). When comparing Skerra’ SEQ ID NO: 18 with instant SEQ ID NO: 2, there is 100% identity. Polymers consisting of about 200 or about 400 or about 600 amino acid residues and comprising PAS#1/SEQ ID NO: 18 have an advantageous serum stability or plasma half-life, even in vivo as compared to the non-modified biologically active protein (See Skerra, pg. 19, 1st paragraph; pg. 26, 2nd paragraph). Moreover, Skerra et al. teaches that biologically active protein that the random coil conformational peptide is bound to includes signaling proteins/peptides such as cytokines, growth factors, hormones, or enzymes (See Skerra, pg. 21, 2nd paragraph). Skerra et al. also teaches that the random coil conformational peptide (i.e., “second” domain) is located in/at the N- or C-termini of the biologically active protein (i.e., “first” domain) (See Skerra, pg. 24, 2nd paragraph). Specific species of fusion proteins include IFNalpha covalently bound to PAS#1 repeated 10 times (i.e., 200 total residues), 20 times (i.e., 400 total residues), and 30 times (i.e., 600 total residues (See Skerra, pg. 37, 2nd paragraph; pg. 47, 2nd to last paragraph; Examples 19-20). Therefore, the teachings of Skerra et al. demonstrate that a polymer comprising at least 100 amino acid residues including 200, 400, 600, and 800 total residues consisting of proline, alanine and serine residues (i.e., instant SEQ ID NO: 2) covalently bound to the N-terminus of a biologically active protein such as a hormone improved serum stability or plasma half-life of the biologically active protein, even in vivo as compared to the non-modified biologically active protein. Thus, the teachings of Skerra et al. satisfy the claim limitations with respect to a fusion protein comprising a biologically active protein covalently attached to a polymer comprising at least 600 amino acids consisting of proline, alanine, and optionally, serine residues, where the polymer is covalently bound to the N-terminus of the biologically active protein as recited in instant claim 1; with respect to where the polymer comprises the amino acids proline, alanine, and serine as recited in instant claim 5; and with respect to where the polymer comprises 600-1200 amino acids as recited in instant claim 6. However, Skerra et al. does not expressly teach where the biologically active protein is hBNP(1-32).
Rosen et al. teaches albumin proteins comprising a therapeutic protein fused to albumin or a fragment thereof (See Rosen, [0009]). Fusing the albumin or albumin fragment to a therapeutic protein prolongs the shelf life of the therapeutic protein, increases the plasma stability of the therapeutic protein compared to its unfused state, and/or stabilizes the therapeutic protein and/or its activity in solution in vitro and/or in vivo (See Rosen, [0009], [0067]). Therapeutic proteins include hormones such as GLP-1, GLP-2, PACAP-27, PACAP-28, VIP, secretin, oxyntomodulin, ANP, BNP, and somatostatin (See Rosen, [0042]). The therapeutic protein can also be IFNalpha or beta (See Rosen, [0042]; Table 1 at pg. 10). Specific albumin fusion protein constructs include fusion numbers 40-41, 43-47, 49-53, which contain BNF fused to albumin (See Rosen, Table 2 at pg. 19-20; Example 80, [1456]-[). One of the BNP constructs exhibits similar activity to the recombinant BNP as depicted in Figure 8 (See Rosen, [1474]). Moreover, the BNP fusion protein increased plasma cGMP levels over baseline 5.6 fold compared to the recombinant BNP, which increased plasma cGMP levels over baseline 3.9-fold as depicted in Figure 10 (See Rosen, [1485]). Furthermore, Rosen et al. demonstrates that the BNP fusion protein exhibited improved half-life stability (i.e., 11.2 h via intravenous delivery or 19.3 h via subcutaneous delivery) compared to the half-life of recombinant BNP, i.e., 3.1 mins) (See Rosen, [1494]; Table 9). Moreover, the BNP utilized is the processed active form of BNP (i.e., amino acids 1-32) (See Rosen, [1456]) thereby constituting BNP(1-32). Rosen’s SEQ ID NO: 392 is 100% identical to instant SEQ ID NO: 1 thereby constituting the hBNP1-32 portion of the amino acid sequence as recited in instant claims 1-2. Rosen et al. also teaches that it is preferably that the albumin is the N-terminal portion of the fusion protein and the therapeutic protein is the C-terminal portion of the fusion protein (See Rosen, [0296]) thereby constituting where the albumin portion is at the N-terminal of the therapeutic protein. Thus, the teachings of Rosen et al. suggest a fusion protein comprising a therapeutic protein such as hBNP(1-32) covalently bound at its N-terminus to human serum albumin where such fusion prolongs the shelf life of BNP, increases the plasma stability of BNP compared to its unfused state, and/or stabilizes BNP and/or its activity in solution in vitro and/or in vivo.
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective date of the instant application to modify the teachings of Skerra et al. and substitute hBNP(1-32) as a biologically active hormone covalently bound to instant SEQ ID NO: 2 repeated 30-40 times thereby totaling 600 to 800 residues as a polymer instead of human serum albumin in order to improve serum stability or plasma half-life of the hBNP. One of ordinary skill in the art at the time the invention was made would have been motivated to do so because therapeutic proteins such as hormones such as IFNalpha, GLP-1, and BNP were known to be covalently bound at its N-terminus to human serum albumin where such fusion was known to prolong the shelf life of BNP, increase the plasma stability of BNP compared to its unfused state, and/or stabilize BNP and/or its activity in solution in vitro and/or in vivo as taught by Rosen et al. One of ordinary skill in the art at the time the invention was made would have had a reasonable expectation of success given that the fusion protein of Skerra et al. comprised a biologically active protein such as a hormone as a “first” domain covalently bound at it’s N-terminus to a polymer comprising at least 100 amino acid residues consisting of proline, alanine, and serine residues such as instant SEQ ID NO: 2 as a “second” domain where the second domain is repeated 30-40 times, and was known to improve serum stability or plasma half-life of the biologically active protein, even in vivo as compared to the non-modified biologically active protein . Therefore, substituting hBNP(1-32) as the biologically active protein would support the improvement of hBNP’s serum stability or plasma half-life by constituting the simple substitution of one known element for another to obtain predictable results and/or some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention pursuant to KSR.
With respect to the total length of the polymer amino acid sequence as recited in instant claims 1 and 6, as discussed supra, Skerra et al. teaches that the polymer sequence ranges from 100 to 1000 total amino acids with a specific species of 600 amino acids where the amino acids consist of proline, alanine, and serine. MPEP 2144.05(I) states that "[i]n the case where the claimed ranges "overlap or lie inside ranges discloses by the prior art" a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) (The prior art taught carbon monoxide concentrations of "about 1-5%" while the claim was limited to "more than 5%". The court held that "about 1-5%" allowed for concentrations slightly above 5% thus the ranges overlapped.) Moreover, the Federal Circuit found that a prima facie case existed where a claim reciting thickness of a protective layer as falling within a range of "50 to 100 Angstroms and the prior art taught that "for suitable protection, the thickness of the protective layer should be not less than about 10 nm [i.e., 100 Angstroms]." In re Geisler, 116 F.3d 1465, 1469-82, 43 USPQ2d 1362, 1365-66 (Fed. Cir. 1997). Therefore, the claimed polymer total amino acid range of methionine would have been obvious to one of ordinary skill in the art since the claimed range (i.e., at least 600 amino acids as recited in instant claim 1; and 600-1200 amino acids as recited in instant claim 6) overlaps with the prior art polymer total amino acid range (i.e., 100-1000 amino acids with a specific species of 600 total amino acids). Therefore, the teachings of Skerra et al. suggest the claim limitation with respect to the total length of the polymer amino acid sequence as recited in instant claims 1 and 6.
With respect to where the polymer inhibits degradation and/or elimination of the BNP in a subject as recited in instant claim 1, as discussed supra, Skerra et al. teaches that when conjugating a biologically active protein to a polymer such as instant SEQ ID NO: 2 repeated 30 times improves the stability and plasma half-life of the biologically active protein. However, it is unnecessary for Skerra et al. to teach this limitation because it is a functional property of the polymer. 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. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977). There is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the time of invention, but only that the subject matter is in fact inherent in the prior art reference. Schering Corp. v. Geneva Pharm. Inc., 339 F.3d 1373, 1377, 67 USPQ2d 1664, 1668 (Fed. Cir. 2003). Therefore, the teachings of Skerra et al. satisfy the claim limitation with respect to where the polymer inhibits degradation and/or elimination of the BNP in a subject as recited in instant claim 1.
With respect to where the BNP retains vasorelaxant activity, it is unnecessary for Skerra to teach this limitation because it is a functional property of the BNP. 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. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977). There is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the time of invention, but only that the subject matter is in fact inherent in the prior art reference. Schering Corp. v. Geneva Pharm. Inc., 339 F.3d 1373, 1377, 67 USPQ2d 1664, 1668 (Fed. Cir. 2003). Therefore, the teachings of Skerra et al. satisfy the claim limitation with respect to where the BNP retains vasorelaxant activity as recited in instant claim 1.
For claim 13, as discussed supra, Skerra et al. teaches that a biologically active protein exhibits an increased half-life when modified with the polymer such as instant SEQ ID NO: 2 repeated 30 times relative to the unmodified biologically active protein. MPEP 2112-2112.02 states that when a reference discloses all the limitations of a claim except for a property or function, and the examiner cannot determine whether or not the reference inherently possesses properties which anticipate or render obvious the claimed invention but has basis for shifting the burden of proof to applicant as in In re Fitzgerald, 619 F.2d 67, 205 USPQ 594 (CCPA 1980). In the instant case, as discussed supra, Skerra et al. and Rosen et al. suggest the claimed structural limitations of the modified BNP. Plus, Skerra et al. teaches that a biologically active protein when covalently bound to the polymer with at least 600 amino acid residues, but does not expressly demonstrate whether the increased half-life of the modified BNP is greater than 50-fold relative to the unmodified BNP when administered subcutaneously into a rat.
The Patent and Trademark Office is not equipped to conduct experimentation in order to determine whether or not applicants’ modified BNP differs, and if so to what extent, from the modified BNP suggested by Skerra et al. and Rosen et al. The cited art taken as a whole demonstrates a reasonable probability that the modified BNP suggested by Skerra et al. and Rosen et al. is either identical or sufficiently similar to the claimed modified BNP that whatever differences exist are not patentably significant. Therefore, with the showing of the reference, the burden of establishing non-obviousness by objective evidence is shifted to the Applicants.
Merely because a property of a modified BNP is not expressly taught in a reference does not make the known modified BNP composition patentable. The modified BNP possesses properties necessarily present which might not be displayed in the tests used in Skerra et al. and/or Rosen et al. Accordingly, the combined disclosures of Skerra et al. and Rosen et al. is a sufficient basis that the modified BNP exhibits a greater than 50-fold increased half-life when administered subcutaneously into a rat relative to an unmodified BNP.
In the alternative, even if the claimed modified BNP is not identical to the suggested modified BNP with regard to some unidentified properties, the differences between that which is taught and that which is claimed are considered to be so slight that the suggested modified BNP is likely to inherently possess the same properties of the claimed modified BNP particularly in view of the similar structural characteristics which they have been shown to share. Thus, the claimed modified BNP would have been obvious to those of ordinary skill in the art under the meaning of USC 103. Accordingly, the claimed invention as a whole was at least prima facie obvious, especially in the absence of sufficient, clear, and convincing evidence to the contrary.
Thus, the invention as a whole is prima facie obvious over the references, especially in the absence of evidence to the contrary.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
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.
Claims 1-2, 5-6 and 13 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5, 9-10, 15, 17-18, 21-23, 25-28, 30, 32, and 34 of copending Application No. 19/676,444 (not yet published). Although the claims at issue are not identical, they are not patentably distinct from each other because ‘444 claims:
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(See ‘444, claims 1-2, 4-5, 10, and 17). When comparing ‘444 SEQ ID NO: 1 with instant SEQ ID NO: 1, there is 100% identity. When comparing ‘444 SEQ ID NO: 2 with instant SEQ ID NO: 2, there is 100% identity. As such, ‘444 SEQ ID NO: 2 repeated 40 times equates to a total of 800 residues. Thus, the ‘444 claimed invention anticipates the instantly claimed invention. Therefore, the ‘444 claimed invention is not patentably distinct from the instantly claimed invention.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to THEA D' AMBROSIO whose telephone number is (571)270-1216. The examiner can normally be reached M-F 11:00 to 8:00 pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Lianko Garyu can be reached at 571-270-7367. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/THEA D' AMBROSIO/Primary Examiner, Art Unit 1654
Prosecution Insights