DETAILED ACTION
Applicant’s amendment and response received on 6/11/26 has been entered. Claims 1-18 are pending and under examination in the instant application. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA . An action on the merits follows.
Those sections of Title 35, US code, not included in this action, can be found in a previous office action.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 6/11/26 is in compliance with the provisions of 37 CFR 1.97 and 1.98. Accordingly, the information disclosure statement has been considered by the examiner, and an initialed and signed copy of the 1449 is attached to this action.
Claim Rejections - 35 USC § 112
The rejection of claims 10-11 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or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention, is withdrawn in view of applicant’s amendments to the claims.
Applicant’s amendment has necessitated the following new grounds of rejection.
Claims 10-11 are newly 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. This is a new matter rejection.
The applicant has amended claims 10 and 11 to recite where the capsid protein comprises “one, two, or three additional amino acid substitutions”. The as filed specification does not appear to provide a sufficient description for a genus of capsid proteins with one, two, or three additional substitutions in addition to the insertion of a motif as claimed. The only reference to the substitution, insertion, or deletion of one, two, or three amino acids in the specification appears to disclosure that such insertions, deletions, or substitutions of one, two, or three amino acids occurs as a result of CRISPR/Cas9 gene editing in a sequence present in a cell. There is no disclosure that the sequence in the cell to be edited is an AAV capsid. The generic guidance provided for using CRISPR/Cas9 gene editing is directed to the introduction of a mutation into a target sequence present in a cell and focus on the structure of the guide RNA using in CRIPSR/Cas9 gene editing. The specification, however, does not identify any particular target sequences present in a cell, and further does not identify any particular one, two, or three amino acid substitutions, additions, or deletions in any target sequence. The specification does not teach that the target sequence is a viral capsid protein present in any type of cell, and does not disclose any one, two, or three amino acid substitutions, additions, or deletions to any viral capsid protein and specifically an AAV9 or AAVrh74 capsid protein aside from the insertion of the target peptide motif. Thus, the as filed specification does not provide the requisite support for the new limitation added to amended claims 10-11.
It is suggested that applicant amend the claims to delete the new matter.
Claim Rejections - 35 USC § 103
The rejection of claims 1-9, and 12-18 under 35 U.S.C. 103 as being unpatentable over Aguti et al. (2018) Exp. Opin. Biol. Ther., Vol. 18(6), 681-693, published online June 4, 2018, in view of US Patent Application Publication 2020/0325456 (October 15, 2020), hereafter referred to as Li et al., with an effective filing date of 12/19/2017, WO 2007/118245 (October 18, 2007), hereafter referred to as Pasqualini et al., Shi et al. (2003) Mol. Ther., Vol. 7(4), 515-525, and Sinanan et al. (2008) Bio. Cell, Vol. 100, 465-477, is maintained. Applicant’s amendments to the claims and arguments have been fully considered but have not been found persuasive in overcoming the rejection for reasons of record as discussed in detail below.
The applicant argues that none of Aguti et al., Li et al., Pasqualini et al., Shi et al., or Sinanan et al. teach and N-mer peptide motif which comprises RGDXn where X is 4-15 amino acids as required by independent claim 1, a recombinant AAV comprising the combination of a muscle specific promoter which is MHCK7 or CK8 operably linked to a cargo polynucleotides and a capsid protein with an RGDn4-n15 inserted into VR-VIII. According to applicant, Aguti et al. is a review article discussing the use of muscle-specific promoter in AAV vectors for DMD gene therapy and does not disclose an RGDn motif peptide inserted into VR-VIII, and that the RGD peptide taught by Li et al. are only RGDn where N=3. The applicant also argues that Li et al. teaches the use of constitutive, not muscle specific promoters. Regarding Pasqualini et al., the applicant argues that Pasqualini teaches an AAV particle which is a hybrid vector that incorporates bacteriophage structural proteins such that the viral particles are fundamentally different from the AAV particles as claimed. Finally, the applicant argues that Sinanon et al. does not provide evidence that skeletal and cardiac myofibers express sufficient levels of avb5 integrin to support efficient RGD-mediated AAV transduction because Sinanon tested avb5 integrin expression in craniofacial muscle precursor cells.
In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). Further, the test for obviousness is not whether the features of a secondary reference may be bodily incorporated into the structure of the primary reference; nor is it that the claimed invention must be expressly suggested in any one or all of the references. Rather, the test is what the combined teachings of the references would have suggested to those of ordinary skill in the art. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981). Obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007).
In the instant rejection, Aguti et al., as the primary reference, was cited for teaching the transduction of muscle cells in vivo and the treatment of Duchenne’s Muscular Dystrophy (DMD) in a subject by administering either a recombinant AAV9 or AAVrh74 viral vector comprising a muscle specific promoter operably linked to a sequence encoding a therapeutic protein such as microdystrophin or GALGT2, where the muscle specific promoter is an MCK promoter or more specifically the hybrid MHCK7 promoter (Aguti et al., pages 683-685 and Table 1). Aguti et al. also teaches that other muscle specific promoters have been used in AAV to express therapeutic genes in muscle cells including the CK8 promoter which was selected to limit expression of the therapeutic gene to skeletal and cardiac muscles (Aguti et al., pages 684 and 686).
The rejection of record acknowledged that Aguti et al. differs from the instant claimed AAV9 or AAVrh74 by not teaching to further insert a muscle targeting moiety into variable region VIII (VR-VIII), where the targeting moiety comprises an n-mer motif comprising RGDXn, where X is any amino acid and n is 4-15. However, Li et al. and Pasqualini et al. were cited to supplement the teachings of Aguti et al. by providing teachings and motivation to insert a muscle targeting moiety into variable region VIII, where the targeting moiety comprises an n-mer motif comprising RGDXn, and Shi et al. was cited for teaching additional RGDXn targeting motifs including RGDXn where X=6. Specifically, Li et al. was cited for teaching AAV comprising modified capsid protein with enhanced transduction of muscle cells, including skeletal, and cardiac muscle cells, and reduced transduction of the liver (Li et al., paragraphs 186). Li et al. teaches that the capsid can be modified by inserting 1-10 or more amino acids into the region of amino acids 575-600 of native AAV2 capsid protein or the corresponding positions of the capsid protein from other AAV, or more specifically amino acid position 585-590 of AAV2 or the corresponding positions of other AAV, including specifically amino acid positions 588-589 of AAV9 (Li et al., paragraphs 188-190, and 232). Note that amino acid positions 585-590 of AAV2 correspond to variable region VIII. More specifically, Li et al., teaches the insertion of peptide comprising an RGD motif following the amino acid position 587 of AAV2, where the RGD motif can function as an integrin receptor binding motif (Li et al., paragraph 208). Li et al., like Aguti et al., further teaches that the modified AAV can be used of the treatment of muscular dystrophy, including Duchenne or Becker muscular dystrophy (Li et al., paragraphs 266 and 289). Li et al. also like Aguti teaches that the AAV comprises muscle specific promoter/enhancer elements to express a therapeutic protein such as a mini- or micro-dystrophin (Li et al., paragraphs 270 and 285). Thus, Li et al. provides specific motivation to further modify the AAV9 or AAVrh74 vectors taught by Aguti et al. for expressing a therapeutic protein in muscle cells by inserting a targeting peptide, including peptides comprising an RGD motif, into the AAV capsid, particularly at positions 588-589 of AAV9, or positions corresponding to 585-590 of AAV2, in order to enhance muscle cell transduction. Applicant’s argument that Li et al. does not teach AAV9 or AAVrh74 which express the therapeutic protein using an MHCK7 or CK8 promoter is not persuasive as Aguti et al., the primary reference, already teaches the use of these promoters in the same types of AAV vectors for expressing therapeutic proteins for treatment of the same types of muscular dystrophy. As noted above, there is no requirement that each reference cited in a 103 obviousness rejection recite each and every limitation of the claims. The rejection of record is properly based on what the combined teachings of the references would have suggested to those of ordinary skill in the art.
Pasqualini et al. was cited for providing additional guidance for RGD targeting peptides inserted into AAV capsid. Pasqualini et al., like Li et al., teaches AAV comprising a capsid comprising a targeting peptide, where the targeting peptide is an RGD targeting peptide which is 3-20 amino acids, or 4-10 amino acids in length (Pasqualini et al., paragraphs 72, 79, and page 76). Pasqualini et also discloses an RGD targeting peptide which is CDCRGDCFC, and teaches that this peptide selectively binds avb5 integrins (Pasqualini et al., paragraph 72). Pasqualini et al. teaches an additional RGD targeting peptide which includes RGDFV and may be up to 20-30 amino acids in length (Pasqualini et al., paragraph 79). Applicant’s argument that Pasqualini et al. uses a hybrid AAV and therefore is not equivalent to the claimed AAV is not persuasive because Li et al. already has been cited for AAV as claimed with AAV capsid comprising RGD targeting peptides for targeting muscle. Pasqualini et al., while teaching a different AAV, was cited for teaching that RGD containing targeting peptides of up to 20-30 amino acids in length bind to avb5 integrins. The relevance of this teaching is tied in to the teachings of Shi et al. and Sinanon et al. Shi et al. has also been cited for teaching AAV capsid comprising RGD targeting peptides, and in particular AAV2 with capsid comprising TGCDCRGDCFCGLS inserted at amino acid position 588, or TGCDCRGDCFCALS into amino acid position 584, where the resulting AAV were capable of efficient transduction of cells expressing avb5 integrins (Shi et al., pages 517-518, and Table 1). While applicant is correct that the specific RGD peptide motifs taught by Li et al. and Pasqualini et al., including CDCRGDCFC and CRGDGWC, are RGDn where N=3 and not 4-15 as claimed, both of these targeting peptides taught by Shi et al. qualify as RGDn where n=6. Shi et al. further teaches that AAV comprising the targeting peptide exhibited increased cell binding and cell transduction compared to AAV without the targeting peptide (Shi et al., pages 518-519). Applicant’s argument that Shi et al. teaches some of amino acid residues are structural linkers is not persuasive as the Shi et al. teaches the insertion of a targeting peptide TGCDCRGDCFCGLS or TGCDCRGDCFCALS with demonstrated targeting of cells expressing avb5 integrins. There is no recitation in the claims that each amino acid in the targeting motif comprising RGDXn be specifically involved in binding to any particular ligand. The claims as written do not distinguish between the functions of various amino acids present in the targeting motif and thus encompass the presence of amino acids whose function is structural rather than binding to any particular ligand.
Furthermore, while both Pasqualini et al. and Shi et al. demonstrated enhanced transduction of a number of cells types expressing integrins, and more specifically cell types expressing avb5 integrins, using AAV comprising a capsid having an targeting RGD peptide motif, it was acknowledged that neither reference specifically tested the transduction of muscle using AAV whose capsid comprises and RGD motif. Sinanan et al., however, teaches that cells present in muscle were well known at the time of filing to expressing avb5 integrins (Sinanan et al., page 468, Figure 2, and page 469). Applicant’s argument that the teachings of Sinanon t al. don’t apply because the cells tested by Sinanan et al. are muscle progenitor cells and not mature skeletal and cardiac myofibers is not persuasive because the claims as written do not require the specific transduction of mature skeletal and cardiac myofibers. Rather, the claims as written simply recite that the targeting motif targets “muscle” (claim 1), or that the method is for transducing a muscle cell. Sinanon et al. clearly teaches that avb5 integrin is a marker for mononuclear skeletal-muscle cells regardless of age, anatomical derivation, or animal species- see page 472 column 2. Thus, the avb5 integrin cells taught by Sinanon et al. clearly qualify as a type of “muscle cell”.
Thus, it is maintained that as Pasqualini et al. provides motivation to use an RGD motif targeting peptide of 4-10 or 3-20 amino acids in length, and Shi et al. provides particular motivation for using 2 different RGD motif targeting peptides which have an RGDXn motif where n is 6 to an AAV capsid, as targeting peptides in an AAV capsid in order to enhance the binding and transduction of cells, such as muscle cells, which express avb5 integrins with an AAV comprising the modified capsid.
Therefore, in view of the teachings of Aguti et al. that a number of muscle specific promoters, including the MHCK7 promoter and the CK8 promoter, can be used effectively in AAV such as AAV9 and AAVrh74 to express a therapeutic gene in muscle cells, the motivation provided by Li et al. to modify the capsid of any AAV serotype to enhance muscle cell transduction, and in particular to insert a peptide into the region of amino acids 585-590 of native AAV2 capsid protein or the corresponding positions of the capsid protein from other AAV, such as amino acid positions 588-589 of AAV9, the further motivation provided by Li et al. to insert a peptide with an RGD motif such as CDCRGDCFC or CRGDGWC, the motivation provided by Pasqualini et al. and Shi et al. to utilize RGD targeting peptides which are 3-20 or 4-10 amino acids in length, and more specifically an RGD peptide which has an RGDXn motif where the n is 6, the teachings of both Pasqualini et al. and Shi et al. that RGD motif peptides bind and transduce cells expressing integrins, particularly the avb5 integrin, and the evidence provided by Sinanan et al. that muscle cells express avb5 integrin, it is maintained that it would have been prima facie obvious to the skilled artisan at the time of filing to modify the AAV9 or AAVrh74 vectors taught by Aguti et al. comprising a MHCK7 or CD8 promoter operably linked to a therapeutic gene useful for treating DMD by inserting a targeting peptide comprising an RGD motif, and in particular the peptides TGCDCRGDCFCGLS or TGCDCRGDCFCALS, at positions 588-589 of AAV9 capsid, or positions in the AAVrh74 capsid in corresponding to 585-590 of AAV2 capsid, in order to enhance muscle cell transduction with reasonable expectation of success. Furthermore, in view of the teachings of Shi et al. teaches that RGD targeting peptides can comprise two amino acid (e.g. TG) upstream of the main RGD targeting motif, and up to 3 amino acids (e.g. GLS or ALS) downstream of the RGD motif which can act as flexible linkers to significantly enhance particle assembly and infectious titer, it would have been further prima facie obvious to the skilled artisan at the time of filing to add the two amino acid upstream linker and 3 amino acid upstream linker to other RGD motif peptides such as the RGDFV peptide taught by Pasqualini et al., thus generating a peptide with RGDXn motif where n is 5, in order to enhance AAV particle assembly and infectious titer, and to transduce muscle cells with a reasonable expectation of success. In addition, or alternatively, based on the teachings and motivation provided by Pasqualini et al. to use an RGD motif targeting peptide of 4-10 or 3-20 amino acids in length, and the teachings of Pasqualini et al. and Shi et al. that it the RGD tripeptide itself which binds to integrin and facilitates transduction of integrin expressing cells, it would have been prima facie obvious to the skilled artisan at the time of filing to generate a number of RGD motif targeting peptides based on the any of the RGD containing peptides taught by Li et al., Pasqualini et al., or Shi et al., with an RGDXn motif where n is for example 4 with a reasonable expectation of success of generating an AAV capsid comprising the RGDX4 peptide and in transducing muscle cells with an AAV comprising a capsid comprising the RGDX4 peptide.
Double Patenting
The rejection of previously pending claims 1-9 and 12-18 on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of U.S. Patent No. 11,920,150, hereafter referred to as the ‘150 patent, in view of Aguti et al. (2018) Exp. Opin. Biol. Ther., Vol. 18(6), 681-693, published online June 4, 2018, is maintained. Applicant’s amendments to the claims and arguments have been fully considered but have not been found persuasive in overcoming the rejection for reasons of record as discussed in detail below.
The applicant argues that the rejection provides no motivation to select MHCK7 or CK8 as the promoter for expression of the therapeutic cargo in the AAV vector recited in the ‘150 patent claims. In response, the ‘150 patent claims broadly encompass the use of any regulatory element to drive expression of the therapeutic transgene in the claimed AAV (see in particular ‘150 patent claim 12), and further specifically claim where the AAV is used in a method of administration to a subject for treatment of muscular dystrophy (‘150 patent claims 20 and 30). Aguti et al. was cited to supplement the ‘150 patent claims by providing motivation to use muscle specific regulatory elements in AAV9 and AAVrh74 vectors to express therapeutic transgenes for the treatment of DMD. In particular, Aguti et al. teaches the transduction of muscle cells in vivo and the treatment of Duchenne’s Muscular Dystrophy (DMD) in a subject by administering either a recombinant AAV9 or AAVrh74 viral vector comprising a muscle specific promoter operably linked to a sequence encoding a therapeutic protein such as microdystrophin or GALGT2, where the muscle specific promoter is an MCK promoter or more specifically the hybrid MHCK7 promoter (Aguti et al., pages 683-685 and Table 1). Note that Table 1 indicates that AAV using the MHCK7 promoter to express micro-dystrophin in clinical trials in human patients with muscular dystrophy. Aguti et al. also teaches that other muscle specific promoters have been used in AAV to express therapeutic genes in muscle cells including the CK8 promoter which was selected to limit expression of the therapeutic gene to skeletal and cardiac muscles (Aguti et al., pages 684 and 686). Aguti et al. teaches that muscle specific expression reduces possibly off-target vents in non-muscle cells (Aguti et al., page 686). Thus, contrary to applicant’s arguments, Aguti et al. provides specific motivation to use either an MHCK7 promoter or a CK8 promoter in an AAV to express a therapeutic gene for the treatment of muscular dystrophy by teaching that AAV expressing micro-dystrophin under control of the MHCK7 promoter has been used in clinical trials in humans, and that the CK8 promoter can reduce the possibility of off-target events in non-muscle cells.
Therefore, it is maintained that based on the motivation provided by Aguti et al. to use muscle specific promoters in AAV for therapy of DMD, and particularly the MHCK7 or CK8 promoters, it would have been obvious to the skilled artisan at the time of filing to use either the MHCK7 or CK8 muscle specific promoters as the regulatory element to express a therapeutic transgene in the AAV recited in the ‘150 patent claims with a reasonable expectation of success.
The provisional rejection of claims 1-2, 4-9 and 12-18 on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 4-5, 7-8, 13-14, 16-17, 19-26, 31-39, and 41 of copending application 17/707,944, hereafter referred to as the ‘944 application, in view of Aguti et al. (2018) Exp. Opin. Biol. Ther., Vol. 18(6), 681-693, published online June 4, 2018, has been converted into a non-provisional rejection based on the issuance of U.S. Patent 12,618,082.
In view of the issuance of U.S. Patent 12,618,082, claims 1-2, 4-9, and 12-18 are now rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-28 of U.S. Patent 12,618,082, hereafter referred to as the ‘082 patent, in view of Aguti et al. (2018) Exp. Opin. Biol. Ther., Vol. 18(6), 681-693, published online June 4, 2018. Applicant’s amendments to the claims and arguments have been fully considered but have not been found persuasive in overcoming this rejection for reasons of record as discussed in detail below.
The applicant argues that the ‘082 patent claims (previously the ‘944 application claims) recite an AAV capsid and do not recite an AAV as claimed which comprises the capsid, a cargo polynucleotide, and a regulatory element, and more specifically a regulatory element which is MHCK7 or CK8. In response, applicant is directed to claims 17-28 of the ‘082 patent, particularly claim 28, which specifically recites an AAV particle comprising species of the engineered AAV capsid polypeptide as claimed, and a species of the cargo polynucleotide as claimed. Claim 17 of the ‘082 patent further recites where the cargo is operatively linked to a regulatory element. Thus, contrary to applicant’s arguments, the claims of the ‘082 patent recite similar AAV as claimed with the exception that the ‘082 patent claims do not limit the regulatory element of an MHCK7 or CK8 promoter. It is further noted that applicant’s arguments regarding the teachings of Aguti et al. have been fully considered and were not found persuasive. Specifically, Aguti et al. teaches the transduction of muscle cells in vivo and the treatment of Duchenne’s Muscular Dystrophy (DMD) in a subject by administering either a recombinant AAV9 or AAVrh74 viral vector comprising a muscle specific promoter operably linked to a sequence encoding a therapeutic protein such as microdystrophin or GALGT2, where the muscle specific promoter is an MCK promoter or more specifically the hybrid MHCK7 promoter (Aguti et al., pages 683-685 and Table 1). Note that Table 1 indicates that AAV using the MHCK7 promoter to express micro-dystrophin in clinical trials in human patients with muscular dystrophy. Aguti et al. also teaches that other muscle specific promoters have been used in AAV to express therapeutic genes in muscle cells including the CK8 promoter which was selected to limit expression of the therapeutic gene to skeletal and cardiac muscles (Aguti et al., pages 684 and 686). Aguti et al. teaches that muscle specific expression reduces possibly off-target vents in non-muscle cells (Aguti et al., page 686). Thus, contrary to applicant’s arguments, Aguti et al. provides specific motivation to use either an MHCK7 promoter or a CK8 promoter in an AAV to express a therapeutic gene for the treatment of muscular dystrophy by teaching that AAV expressing micro-dystrophin under control of the MHCK7 promoter has been used in clinical trials in humans, and that the CK8 promoter can reduce the possibility of off-target events in non-muscle cells. Thus, the rejection of record stands.
The provisional rejection of claims 1-9 and 12-18 on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-8, 11, 13, 16, 18-19, 21, 23, 31-35, 37-39, 42, 44-45, 47-48, 52, 58-59, 61-62, 64, 74, 77, and 88-89 of copending application 17/764,509, hereafter referred to as the ‘509 application, in view of in view of Aguti et al. (2018) Exp. Opin. Biol. Ther., Vol. 18(6), 681-693, published online June 4, 2018, is maintained. The applicant argues that the instant application has the earlier filing date and that therefore this rejection should be withdrawn when is it the last remaining rejection. However, at this time, the claims remain rejected under several statutes and thus this is not the last remaining rejection. As such, the provisional rejection stands.
The provisional rejection of claims 1-9 and 12-18 on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 7, 9, 11-16, 18-22, 25, 31-32, 34, 44, 48, 51, 53-54, 56-57, 59, 62, 65, 67, and 69-70 of copending application 17/642,541, hereafter referred to as the ‘541 application, in view of Aguti et al. (2018) Exp. Opin. Biol. Ther., Vol. 18(6), 681-693, published online June 4, 2018, is withdrawn in view of applicant’s submission of a terminal disclaimer on 6/11/26.
The terminal disclaimer filed on 6/11/26 disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration date of any patent granted on application 17/642,541 has been reviewed and is accepted. The terminal disclaimer has been recorded.
The provisional rejection of claims 1-2, 4-6, 8-9 and 12-18 on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 5, 7-10, 15-34, and 36 of copending application 17/707,951, hereafter referred to as the ‘951 application, in view of Aguti et al. (2018) Exp. Opin. Biol. Ther., Vol. 18(6), 681-693, published online June 4, 2018, is withdrawn in view of applicant’s submission of a terminal disclaimer on 6/11/26.
The terminal disclaimer filed on 6/11/26 disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration date of any patent granted on application 17/707,951 has been reviewed and is accepted. The terminal disclaimer has been recorded.
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 from the examiner should be directed to Anne Marie S. Wehbé, Ph.D., whose telephone number is (571) 272-0737. If the examiner is not available, the examiner’s supervisor, Maria Leavitt, can be reached at (571) 272-1085. For all official communications, the technology center fax number is (571) 273-8300. Please note that all official communications and responses sent by fax must be directed to the technology center fax number. For informal, non-official communications only, the examiner’s direct fax number is (571) 273-0737. For any inquiry of a general nature, please call (571) 272-0547.
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.
Dr. A.M.S. Wehbé
/ANNE MARIE S WEHBE/Primary Examiner, Art Unit 1634
Prosecution Insights