DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
This action is in response to the amendment, filed 5/8/2026, in which claim 3 was amended. Claims 1-4, 7, 8, 10-14, 21, 23-25, 36-45 and 49 are pending.
Applicant’s arguments have been thoroughly reviewed but are not persuasive for the reasons that follow. Any rejections and objections not reiterated in this action have been withdrawn. This action is FINAL.
Election/Restrictions
Applicant’s election without traverse of Group I and the species (A) the polypeptide of SEQ ID NO: 1; (B) the A36S substitution; (C) the 5’UTR of SEQ ID NO: 6; and (D) the 3’UTR of SEQ ID NO: 24 in the reply filed on 7/10/2024 is acknowledged. The response indicated that claims 1-4, 7, 8, 10-14 and 21 encompass the elected species.
Upon further consideration, the species election requirement for (A) has been withdrawn. Each of SEQ ID NOS: 1, 2, 3 and 4 are under consideration. The species election requirement for 5’ UTR and 3’ UTR has been maintained.
Claims 23-25, 36-45 and 49 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 7/10/2024.
Claims 1-4, 7, 8, 10-14 and 21 are under consideration.
Information Disclosure Statement
Receipt of an information disclosure statement is acknowledged. The signed and initialed PTO-1449 has been mailed with this action.
Response to Arguments - Claim Objections
The objection to claim 3 has been withdrawn in view of Applicant’s amendment to the claim in the reply filed 5/8/2026.
Response to Arguments - 35 USC § 112
The rejection of claim 3 under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, has been withdrawn in view of Applicant’s amendment to the claim in the reply filed 5/8/2026. Claim 3 now depends from claim 1, and claim 3 further limits the scope of claim 1.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1, 3, 4, 8 and 10-14 are rejected under 35 U.S.C. 103 as being unpatentable over DeRosa et al (US Patent Application Publication No. 2015/0110857 A1; see the entire reference) in view of Simon-Chazottes et al (Virology, Vol. 417, pages 147-153, 2011; see the entire reference) and Tag-El-Din-Hassan et al (Japanese Journal of Veterinary Research, Vol. 60, pages 95-103, 2012), as evidenced by GenBank Accession No. NP_001077394.1 (publicly available May 2017, printed as pages 1/3-3/3). This rejection was made in the Office action mailed 1/5/2026.
Regarding claims 1, 3 and 13, DeRosa et al teach methods for effective delivery of messenger RNA (mRNA) to the central nervous system (CNS), by delivering to a subject in need thereof a composition comprising an mRNA encoding a protein encapsulated within a liposome, such that the administering of the composition results in the intracellular delivery of mRNA in neurons in the brain and/or spinal cord (e.g., Abstract). DeRosa et al teach that the method is useful for the treatment of CNS diseases, disorders or conditions, including Cree encephalitis, and Rasmussen’s Encephalitis (e.g., Abstract; paragraph [0103]). DeRosa et al teach that the mRNA may be used to deliver a protein deficient in a CNS disease, disorder or condition (e.g., paragraph [0112]).
Regarding claim 8, DeRosa et al teach the method where the mRNA comprises a 5’ UTR and/or 3’ UTR sequence, such as sequences derived from mRNA molecules which are stable, such as globin, actin, GAPDH, tubulin, histone, or citric acid cycle enzymes (e.g., paragraphs [0023] and [0143]-[0146]).
Regarding claims 10 and 11, DeRosa et al teach the method where the mRNA encoding the therapeutic protein comprises one or more modified nucleotides, such as N-1-methyl pseudouridine (e.g., paragraph [0024]).
Regarding claim 12, DeRosa et al teach the method where the mRNA is a codon-optimized sequence (e.g., paragraph [0112]).
Regarding claim 14, DeRosa et al teach the method where CNS delivery comprises injection directly into the CNS and/or CSF, such as intrathecal injection (e.g., paragraphs [0191]-[0196]-[0203]).
DeRosa et al do not teach the method for the treatment of West Nile virus infection, where the mRNA encodes Mus musculus resistant 2’-5’-oligoadenylate synthetase 1b (rOas1b).
Simon-Chazottes et al teach that West Nile virus (WNV) is a positive-sense, single-stranded RNA flavivirus that infects a wide range of vertebrate hosts and causes severe illness in humans, including encephalitis, meningitis, or flaccid paralysis (e.g., page 147, left column). Simon-Chazottes et al teach that in vitro experiments demonstrated that expression of full-length mouse OAS1B protein (rOas1b of the claims) but not the C-terminally truncated form inhibits WNV replication inside infected mouse cells (e.g., page 147, right column). Simon-Chazottes et al teach that there is mounting evidence that the OAS family may play a crucial role in antiviral host immunity to WNV, because, similar to mouse strains, genetic variations in human and horse OAS1 are risk factors for infection with neuropathogenic WNV (e.g., page 147, right column; page 149, right column). Simon-Chazottes et al teach expression of the cDNA corresponding to Oas1b mRNA expresses in resistant MBT/Pas mice via transgenesis in susceptible BALB/c mice, resulting in upregulation of Oas1b expression in BALB/c mice and resistance against lethal WNV-induced encephalitis (e.g., page 148, left column, 1st full paragraph). At the left column of page 151, Simon-Chazottes et al state the following:
Together, the results of knock-in and transgenesis experiments establish that expression of a full-length OAS1B protein is a cornerstone in the resistance to infection with flaviviruses.
Important for the outcome of the disease in transgenic made were the levels of Oas1bMBT mRNA in the brain prior to and after infection.
Thus, Simon-Chazottes et al teach the level of OAS1B mRNA in brain is important to resistance to WNV infection.
Tag-El-Din-Hassan et al teach the evaluation of antiviral activity of mouse Oas1b (rOas1b of the claims) and chicken OAS-A in hamster BHK-21 cells transfected with pmOas1b-FL-EGFP and ChOAS-A-FL, respectively (e.g., page 98, paragraph bridging columns; page 99). Tag-El-Din Hassan et al teach the mOas1b protein sequence of NP_001077394.1 (e.g., Fig. 1). Tag-El-Din-Hassan et al teach that both the chicken and mouse Oas1b proteins were effective at inhibiting replication of WNV in hamster BHK-21 cells (e.g., page 99, paragraph bridging columns). In contrast, Tag-El-Din-Hassan et al teach that human OASL has been shown to possess antiviral activity against single-stranded RNA viruses such as picornavirus and encephalomyocarditis viruses (e.g., page 101, left column, full paragraph).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the methods for effective delivery of messenger RNA (mRNA) to the central nervous system (CNS), by delivering to a subject in need thereof a composition comprising an mRNA encoding a protein of DeRosa et al to include the coding sequence of full length mouse Oas1b taught by Simon-Chazottes et al and Tag-El-Din-Hassan et al, because DeRosa et al teach it is within the ordinary skill in the art to use mRNA encoding a protein for therapeutic purposes, including various forms of encephalitis, and Simon-Chazottes et al and Tag-El-Din-Hassan et al teach that mouse Oas1b is capable of providing resistance to West Nile Virus replication, which is known to result in encephalitis. One would have had a reasonable expectation of success in making such a modification, because Simon-Chazottes et al teach that the expression of full-length mouse Oas1b is “a cornerstone in the resistance to infection with flaviviruses.” See page 151, left column. Further Simon-Chazottes et al teach that what is important is Oas1b mRNA levels in the brain, and DeRosa et al specifically teach how to deliver mRNA to the brain for therapeutic purposes. Moreover, one would have had a reasonable expectation of success in administering the mouse Oasb1 mRNA to a human for the purpose of treating West Nile virus infection, because Tag-El-Din Hassan et al teach that mouse Oas1b is function for inhibition of West Nile virus replication across species, specifically demonstrating the nucleic acid encoding NP_001077394.1 is functional in hamster cells. Even the more distantly related chicken protein was function in hamster. Thus, one would have had a reasonable expectation of success in administering the mouse Oas1b mRNA, including mRNA encoding NP_001077394.1, to the brain of a human for the purpose of inhibiting West Nile virus replication.
One would have been motivated to make such a modification in order to receive the expected benefit of being able to inhibit West Nile virus replication in a human for therapeutic purposes.
Regarding claim 3, Tag-El-Din Hassan et al teach the mOas1b protein sequence of NP_001077394.1. Shown below is an alignment of the protein sequence of NP_001077394.1 (Query) and instant SEQ ID NO: 1 (Sbjct).
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The alignment shows that the sequence of NP_001077394.1 is that of instant SEQ ID NO: 1 with Q266R, A322T, S336P and L354F substitution mutations.
Regarding claim 4, Tag-El-Din Hassan et al teach the mOas1b protein sequence of NP_001077394.1. Shown below is an alignment of the protein sequence of NP_001077394.1 (Query) and instant SEQ ID NO: 2 (Sbjct).
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The alignment shows that the sequence of NP_001077394.1 is that of instant SEQ ID NO: 2.
Claim 2 rejected under 35 U.S.C. 103 as being unpatentable over DeRosa et al (US Patent Application Publication No. 2015/0110857 A1; see the entire reference) in view of Simon-Chazottes et al (Virology, Vol. 417, pages 147-153, 2011; see the entire reference) and Tag-El-Din-Hassan et al (Japanese Journal of Veterinary Research, Vol. 60, pages 95-103, 2012) as applied to claim1, 3, 8 and 10-14 above, and further in view of GenBank Accession No. Q60856.3 (publicly available June 2017, printed as pages 1/7-7/7; see the entire reference).
The combined teachings of DeRosa et al, Simon-Chazottes et al, and Tag-El-Din-Hassan et al are described above and applied as before. This rejection was made in the Office action mailed 1/5/2026.
DeRosa et al, Simon-Chazottes et al, and Tag-El-Din-Hassan et al do not teach the method where the mRNA encodes the Oas1b polypeptide of SEQ ID NO: 1.
Q60856.3 teaches an amino acid sequence of mouse Oas1b, which displays antiviral activity against flaviviruses such as West Nile virus (WNV) (e.g., page 3/7, Comment Section; enumerated amino acid sequence at page 7/7). The alignment of instant SEQ ID NO: 1 (Query) and Q60856.3 (Sbjct) is shown here below.
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It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined teachings of DeRosa et al, Simon-Chazottes et al, and Tag-El-Din-Hassan et al to include an mRNA sequence encoding the mouse Oas1b protein of Q60856.3, because Simon-Chazottes et al and Tag-El-Din-Hassan et al teach mouse Oas1b provides resistance to WNV, and Q60856.3 teaches that the specific mouse Oas1b sequence provides the same function. It would have been obvious to substitute one coding sequence for the other in order to achieve the predictable result of providing a sequence capable of treating WNV infection.
Claim 21 is rejected under 35 U.S.C. 103 as being unpatentable over DeRosa et al (US Patent Application Publication No. 2015/0110857 A1; see the entire reference) in view of Simon-Chazottes et al (Virology, Vol. 417, pages 147-153, 2011; see the entire reference) and Tag-El-Din-Hassan et al (Japanese Journal of Veterinary Research, Vol. 60, pages 95-103, 2012) as applied to claims 1, 3, 8 and 10-14 above, and further in view of de Fougerolles et al (US Patent No. 9,533,047 B2; see the entire reference). This rejection was made in the Office action mailed 1/5/2026.
The combined teachings of DeRosa et al, Simon-Chazottes et al, and Tag-El-Din-Hassan et al are described above and applied as before.
DeRosa et al, Simon-Chazottes et al, and Tag-El-Din-Hassan et al do not teach the method where the 5’ UTR of the mRNA is SEQ ID NO: 6, and/or the 3’ UTR of the mRNA is SEQ ID NO: 24.
De Fougerolles et al teach pharmaceutical compositions containing modified mRNA (mmRNA), where the mmRNA is introduced into cells to modulate protein expression with enhanced efficiency of expression (e.g., column 2, lines 3-13; column 4, lines 65-67; column 5, lines 10-23). De Fougerolles et al teach that the mmRNAs can be used as therapeutic agents and can be administered to a subject to produce a therapeutic protein in the subject (e.g., column 13, lines 44-59). De Fougerolles et al teach that it is beneficial to provide a 5’ untranslated region (UTR) and/or a 3’ UTR in the mmRNA(e.g., column 10, lines 30-67). De Fougerolles et al teach that mmRNA is produced according to standard laboratory methods and materials, where the open reading frame of the gene of interest may be flanked by a 5’ UTR containing a strong Kozak translational initiation signal, and an alpha-globin 3’ UTR which may include an oligo(dT) sequence for templated addition of a poly-A tail, which is 160 nucleotides in length and encoded in the template for in vitro transcription (e.g., column 53, lines 10-31; column 60, lines 48-55). De Fougerolles et al specifically teach the use of the 5’ UTR and 3’ UTR sequence given in SEQ ID NO: 6 (e.g., column 64, lines 8-32).
SEQ ID NO: 6 of de Fougerolles et al (Sbjct) comprises the sequence of instant SEQ ID NO: 6 (Query):
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SEQ ID NO: 6 of de Fougerolles et al (Sbjct) comprises the sequence of nucleotides 1-101 of instant SEQ ID NO: 24 (Query):
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SEQ ID NO: 6 of de Fougerolles et al (Sbjct) is identical to nucleotides 1-50 and 1178-1284 of instant SEQ ID NO: 42 (Query):
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The remaining sequence of instant SEQ ID NO: 24 and (AAAAA) is present in the transcript by de Fougerolles et al, because de Fougerolles et al teach the addition of a polyA tail of 160 nucleotides (e.g., column 60, lines 48-55). Thus, de Fougerolles et al teach that it is within the skill of the art to produce mmRNA with the sequence of instant SEQ ID NOS: 6 and 24 flanking a coding sequence for an open reading frame.
It would have been obvious to one of ordinary skill in the art at the time the invention was made to modify the combined teachings of DeRosa et al, Simon-Chazottes et al, and Tag-El-Din-Hassan et al to include the 5’ UTR, 3’ UTR and polyA sequences taught by de Fougerolles et al, because DeRosa et al teach the method where the mRNA comprises a 5’ UTR and/or 3’ UTR sequence, such as sequences derived from mRNA molecules which are stable, such as globin, and de Fougerolles et al teach it is within the ordinary skill in the art to use the sequence of 5’ UTR, 3’ UTR of SEQ ID NO: 6 with the addition of a polyA tail for the production of therapeutic mRNA, where the 3’ UTR is an alpha-globin 3’ UTR. One would have expected to use the specific sequences taught by de Fougerolles et al to provide UTR sequences known to function in the context of therapeutic mRNA. One would have been motivated to make such a modification in order to receive the expected benefit of including sequences deems as beneficial for enhanced protein production as taught by de Fougerolles et al.
Claim 7 is rejected under 35 U.S.C. 103 as being unpatentable over DeRosa et al (US Patent Application Publication No. 2015/0110857 A1; see the entire reference) in view of Simon-Chazottes et al (Virology, Vol. 417, pages 147-153, 2011; see the entire reference), Tag-El-Din-Hassan et al (Japanese Journal of Veterinary Research, Vol. 60, pages 95-103, 2012), and de Fougerolles et al (US Patent No. 9,533,047 B2; see the entire reference) as applied to claims 1, 3, 8, 10-14 and 21 above, and further in view of Chakraborty et al (US Patent No. 9,192,651 B2; see the entire reference). This rejection was made in the Office action mailed 1/5/2026.
The combined teachings of DeRosa et al, Simon-Chazottes et al, Tag-El-Din-Hassan et al and de Fougerolles et al are described above and applied as before. Further, SEQ ID NO: 6 of de Fougerolles et al (Sbjct) is identical to nucleotides 1-50 and 1178-1284 of instant SEQ ID NO: 42 (Query):
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The remaining sequence of instant SEQ ID NO: 42 (AAAAA) is present in the transcript by de Fougerolles et al, because de Fougerolles et al teach the addition of a polyA tail of 160 nucleotides (e.g., column 60, lines 48-55). Thus, de Fougerolles et al teach that it is within the skill of the art to produce mmRNA with the sequence of instant SEQ ID NOS: 6 and 24 flanking a coding sequence for an open reading frame. Moreover, de Fougerolles et al teach that the mmRNA are typically codon-optimized (e.g., column 86, lines 15-28).
Moreover, Tag-El-Din-Hassan et al teach mRNA encoding mouse Oas1b (rOas1b of the claims) expressed in cells transfected with pmOas1b-FL-EGFP (e.g., page 98, paragraph bridging columns; page 99). Tag-El-Din Hassan et al teach the mOas1b protein sequence of NP_001077394.1 (e.g., Fig. 1). Instant SEQ ID NO: 42 (Query) encodes the amino acid sequence of NP_001077394.1 (Sbjct):
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DeRosa et al, Simon-Chazottes et al, Tag-El-Din-Hassan et al and de Fougerolles et al do not teach the method where the mRNA comprises the sequence of SEQ ID NO: 42. Specifically, the mRNA where the coding sequence is nucleotides 47-1174 of SEQ ID NO: 42 followed by the stop codon UAG.
Chakraborty et al teach methods for the therapeutic use of mRNA molecules (e.g., Abstract). Chakraborty et al teach that the mRNA is constructed by selecting a target sequence encoding a polypeptide, where the target polynucleotide sequence is codon optimized (e.g., paragraph bridging columns 36-37; column 37). Chakraborty et al teach that codon optimization methods are known in the art and may be useful in efforts to achieve one or more of several goals, including increase mRNA stability and adjust translational rates (e.g., column 37, line 30 to column 38, line 40). Chakraborty et al teach that codon optimization tools, algorithms and services are known in the art (e.g., column 37, lines 46-51). Further, Chakraborty et al teach it is beneficial to flank the open reading frame (ORF) encoding the protein with 5’ UTR and/or 3’ UTR (e.g., column 38, lines 40-67). Chakraborty et al teach that Tables 2 and 3 provide a listing of exemplary UTRs that can be used in the primary construct as flanking regions, where Table 2 shows 5’ UTRs and Table 3 shows 3’ UTRs (e.g., columns 39-52). Table 2 shows the 5’ UTR sequence of SEQ ID NO: 1 (Db), which is identical to instant SEQ ID NO: 6 (Qy) when transcribed to mRNA.
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Chakraborty et al teach SEQ ID NO: 9 for the alpha-globin 3’ UTR in table 3. SEQ ID NO: 9 (Db) is identical to instant SEQ ID NO: 24 (Qy) when transcribed into mRNA.
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It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the combined teachings of DeRosa et al, Simon-Chazottes et al, Tag-El-Din-Hassan et al and de Fougerolles et al to include the codon optimization of the sequence encoding mouse Oas1b taught by Tag-El-Din Hassan et al along with an AUG stop codon, because both de Fougerolles et al and Chakraborty et al teach it is within the ordinary skill in the art to use mRNA sequences that have been codon optimized for the production of therapeutic mRNA. Chakraborty et al teach that codon optimization methods were known in the art and routinely applied for stability and control of expression, and one could have pursued these known potential solutions with a reasonable expectation of success. Due to codon degeneracy, there is a finite number of predictable solutions to alter the codons encoding the mouse Oas1b protein with a stop codon. One would have sought out these solutions in order to provide stability and increased expression of the mouse Oas1b protein in the therapeutic context.
Response to Arguments - 35 USC § 103
With respect to the rejection of claims 1, 3, 4, 8 and 10-14 under 35 U.S.C. 103 as being unpatentable over DeRosa et al in view of Simon-Chazottes et al and Tag-El-Din-Hassan et al, as evidenced by GenBank Accession No. NP_001077394.1, Applicant's arguments filed 5/8/2026 have been fully considered but they are not persuasive.
The response asserts that there is no evidence in the cited reference that supports the predictable use of mouse Flavivirus-resistant Oasb1 protein to confer Flavivirus resistance when transgenically expressed in human neurons. The response asserts that the mouse and human OAS genes are not conserved, human OAS1 proteins are active 2'-5' adenyl synthetases (2-5 A). Active 2-5 A binds to RNase L and activates its endonuclease activity. Activated RNase L cleaves UA sites in single stranded regions of RNAs to degrade cellular and viral RNAs. The response asserts that Oasb1 is not a functional synthetase, and the mechanism by which Oas1b provides resistance to flavivirus-induced disease was not known. Thus, the response asserts that there was no way for one of ordinary skill in the art to predict whether mouse Oasb1 would be able to function by itself in human cells that do not have a known homologue. The response asserts that this was an unexpected result.
These arguments are not found persuasive. The cited prior art teaches the role of the claimed mouse Oasb1 in antiviral host immunity to West Nile virus (WNV). Simon-Chazottes et al teach expression of the cDNA corresponding to Oas mRNA expresses in resistant MBT/Pas mice via transgenesis in susceptible BALB/c mice, resulting in upregulation of Oas 1b expression in BALB/c mice and resistance against lethal WNV-induced encephalitis (e.g., page 148, left column, 1st full paragraph). At the left column of page 151, Simon-Chazottes et al state the following:
Together, the results of knock-in and transgenesis experiments establish that expression of a full-length OAS1B protein is a cornerstone in the resistance to infection with flaviviruses.
Important for the outcome of the disease in transgenic made were the levels of Oas MBT mRNA in the brain prior to and after infection.
Thus, Simon-Chazottes et al teach the level of OAS1B mRNA in brain is important to resistance to WNV infection. Additionally, the teachings of Tag-El-Din-Hassan et al provide evidence of predictability. Tag-El-Din Hassan et al teach the mOas1b protein sequence of NP_001077394.1 (e.g., Fig. 1). Tag-El-Din-Hassan et al teach that both the chicken and mouse Oaslb proteins were effective at inhibiting replication of WNV in hamster BHK-21 cells (e.g., page 99, paragraph bridging columns). Accordingly, the prior art provides predictability in using mouse Oas1b in different species of mammals, and the more distantly related chicken protein was also functional. Based on these results, one would have had an expectation of success in expressing the mouse Oas1b protein of Simon-Chazottes et al and Tag-El-Din-Hassan et al in neurons of the brain in humans to inhibit replication of WNV. In particular, DeRosa et al teach that mRNA can be delivered intrathecally to the CNS and expressed in neurons. Simon-Chazottes et al and Tag-El-Din-Hassan et al teach the very protein recited in the claims and its antiviral utility against flavivirus infection. The proper inquiry under § 103 is whether the claimed subject matter as a whole would have been obvious to a person of ordinary skill in the art in view of the combined teachings of the references. Here, the combination of a known CNS delivery technique with a known antiviral murine Oas1b payload would have been a predictable use of prior art elements according to their established functions.
The rejection of record does not rely upon the use of a human OAS gene. The fact that they are distantly related to the protein of Simon-Chazottes et al and Tag-El-Din-Hassan et al does not negate the teachings of these references.
Applicant’s reliance on the fact that the precise mechanism of Oas1b-mediated resistance was not fully characterized is not sufficient to overcome the rejection. A reference need not explain the exact mechanism of action to render a claimed therapeutic use obvious, where the record establishes that the protein itself was known to confer the relevant antiviral effect. No objective evidence of unexpected results has been provided. Attorney argument alone is insufficient to overcome a prima facie case of obviousness.
Thus, the rejection is maintained.
With respect to the rejection of claim 2 under 35 U.S.C. 103 as being unpatentable over DeRosa et al in view of Simon-Chazottes et al and Tag-El-Din-Hassan et al, and further in view of GenBank Accession No. Q60856.3, Applicant's arguments filed 5/8/2026 have been fully considered but they are not persuasive.
The response asserts that the additional reference does not cure the deficiencies of the prior rejection by providing a reasonable expectation of success that mouse Oasb1 would function in human cells.
This argument is not found persuasive for the reasons set forth above with regard to the rejection of claims 1, 3, 4, 8 and 10-14. Thus, the rejection is maintained.
With respect to the rejection of claim 21 under 35 U.S.C. 103 as being unpatentable over DeRosa et al in view of Simon-Chazottes et al and Tag-El-Din-Hassan et al, and further in view of de Fougerolles et al, Applicant's arguments filed 5/8/2026 have been fully considered but they are not persuasive.
The response asserts that the additional reference does not cure the deficiencies of the prior rejection by providing a reasonable expectation of success that mouse Oasb1 would function in human cells.
This argument is not found persuasive for the reasons set forth above with regard to the rejection of claims 1, 3, 4, 8 and 10-14. Thus, the rejection is maintained.
With respect to the rejection of claim 7 under 35 U.S.C. 103 as being unpatentable over DeRosa et al in view of Simon-Chazottes et al, Tag-El-Din-Hassan et al, and de Fougerolles et al, and further in view of Chakraborty et al,
Applicant's arguments filed 5/8/2026 have been fully considered but they are not persuasive.
The response asserts that the additional reference does not cure the deficiencies of the prior rejection by providing a reasonable expectation of success that mouse Oasb1 would function in human cells.
This argument is not found persuasive for the reasons set forth above with regard to the rejection of claims 1, 3, 4, 8 and 10-14. Thus, the rejection is maintained.
Conclusion
No claim is allowed.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Yvonne Eyler can be reached at 571-272-1200. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
Jennifer Dunston
Supervisory Patent Examiner
Art Unit 1637
/Jennifer Dunston/Supervisory Patent Examiner, Art Unit 1637
Prosecution Insights