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 .
DETAILED ACTION
Claims 10, 16, 17, 19, 20, and 22 are pending.
Claims 11, 14, 15, 18, and 21 are canceled.
Claims 10, 19, 20, and 22 are currently amended.
Claims 10, 16, 17, 19, 20, and 22 are under examination on the merits.
Rejections Withdrawn
35 U.S.C. 112(a)
The rejection of the claims 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or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement, has been withdrawn in view of the claim amendments, dated 12/15/2025.
The rejection of the claims under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for treating diabetic autonomic neuropathy (DAN) by administering an anti-RGMa antibody, does not reasonably provide enablement for preventing DAN by administering an anti-RGMa antibody, has been withdrawn in view of the claim amendments, dated 12/15/2025.
The rejection of the claims under 35 U.S.C. 103 as being unpatentable over Hashimoto et al. (US PG PUB 2018/0100012, publication date: 04/12/2018) and Lincoln et al. (Tzu Chi Medical Journal, 20(3): 161-168, 2008) has been withdrawn in view of the claim amendments, dated 12/15/2025.
The rejection of the claims under 35 U.S.C. 103 as being unpatentable over Hashimoto et al. (US PG PUB 2018/0100012, publication date: 04/12/2018), Lincoln et al. (Tzu Chi Medical Journal, 20(3): 161-168, 2008), and Issar et al. (Clinical Neurophysiology, 130: 2088-2095, 2019), has been withdrawn in view of the claim amendments, dated 12/15/2025.
The nonstatutory double patenting rejections of record have been withdrawn in view of the claim amendments, dated 12/15/2025.
Response to Arguments
With respect to the rejection of the claims under 35 U.S.C. 103, Applicant asserts that “a person of ordinary skill in the art would not have had a reasonable expectation of success for the present invention based on the disclosure of Issar et al. because Issar et al. discloses a causal mechanism that is the inverse of the causal mechanism upon which the claimed method is based. Issar et al. discloses that the ‘CKD component has a major role in causing axonal dysfunction’ (page 2094, right column, third paragraph). Issar et al. concludes that a systemic uremic state associated with CKD (kidney dysfunction), such as hyperkalemia, is the cause of the peripheral nerve dysfunction (pages 2093-2094, text under ‘Discussion’). Therefore, a person of ordinary skill in the art would understand that the causal relationship disclosed by Issar et al. is as follows:
CKD (Kidney Dysfunction) [Cause] → Systemic State → Peripheral Neuropathy [Result].
Accordingly, a person of ordinary skill in the art seeking to treat the neuropathy, i.e.
the result, as disclosed by Issar et al., would be motivated to treat the underlying cause of the
neuropathy, i.e., to treat the CKD or the systemic state, for example by potassium restriction.
In contrast, the present application discloses that (1) RGMa expression is upregulated
locally in the “kidney” under diabetic conditions (Fig. 1), (2) the anti-RGMa antibody
suppresses the degeneration of local autonomic (sympathetic) nerves “within the kidney”
(Fig. 3), and (3) as a result, the “kidney dysfunction” itself is improved (Fig. 4, showing
improvement in urinary albumin/urinary creatinine ratio (UACR)).
Therefore, the causal relationship upon which the present invention relies is as follows:
Anti-RGMa Antibody → Treats Local Neuropathy in the Kidney [Cause] → Improves
Kidney Dysfunction [Result].
The present application discloses that treating local neuropathy in the kidney results in
improved kidney dysfunction, therefore suggesting a causal mechanism opposite of that
disclosed by Issar et al. Issar et al. discloses that CKD [Cause] causes neuropathy [Result] and provides no suggestion of the opposite, i.e., that that treating the neuropathy [Result]
would improve the CKD [Cause].
Therefore, the disclosure of Issar et al. would not have provided a credible reason for a
person of ordinary skill in the art to have used a neuropathy treatment as taught by Hashimoto
et al. to treat the CKD-caused neuropathy disclosed by Issar et al., let alone with a reasonable
expectation of success that doing SO would treat DAN-caused CKD (rather than merely the
CKD-caused neuropathy). Such a reasonable expectation of success for the claimed method is
only possible with the hindsight knowledge of the core discovery disclosed in the present
application regarding the local role of RGMa in the kidney and its causal link to kidney
dysfunction as shown, for example, in Figs. 1, 3, and 4 of the present application.
Accordingly, the present invention as defined by claim 10, as well as claims 16, 17,
19, 20, and 22 dependent thereon, would not have been obvious over the combined
disclosures of Hashimoto et al., Lincoln et al., and Issar et al., such that the obviousness
rejection based on Hashimoto et al., Lincoln et al., and Issar et al. should be withdrawn.”
These arguments have been fully considered but are not deemed persuasive, as detailed in the rejection of the claims under 35 U.S.C. 103 below.
Briefly it is noted that at [0034], Hashimoto et al. teach that anti-RGMa neutralizing antibodies of the invention may be used to treat diabetes mellitus. At [0036], Hashimoto et al. teach 1) an anti-RGM neutralizing antibody that comprises the LCDRs 1-3 and the HCDRs 1-3 of SEQ ID NO(s): 30-35, respectively, and these CDRs share 100% sequence homology with the instant SEQ ID NO(s): 5-10, respectively, corresponding to (a) of claim 10, and 2) an anti-RGM neutralizing antibody that comprises the LCDRs 1-3 and the HCDRs 1-3 of SEQ ID NO(s): 36-40 and SFG, respectively, and these CDRs share 100% sequence homology with the instant SEQ ID NO(s): 11-15 and SFG, respectively, corresponding to (b) of claim 10. Furthermore Lincoln et al. suggest that axonopathy and axonal degeneration are characteristics of DAN. Given that the anti-RGMa antibodies of Hashimoto et al. promote the generation of axons, there would have been a reasonable expectation that said antibodies may be used to reverse or improve the negative characteristics of DAN, thereby providing a therapeutic benefit to DAN patients. Additionally Issar et al. suggest that neuropathy may be more severe in DKD patients. As such one of ordinary skill in the art would have been motivated to practice the method of Hashimoto et al., Lincoln et al., and Issar et al. on patients having diabetic neuropathy, such as DAN, with associated DKD, because said patients likely have an increased need for relief from neuropathy. The invention of Hashimoto et al., Lincoln et al., and Issar et al. functions by the same mechanism as the claimed invention, specifically, an anti-RGMa antibody is used to treat neuropathy in the kidney, thereby improving kidney disfunction.
New Ground(s) of Rejection - Necessitated by Amendment
35 U.S.C. 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
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 10, 16, 17, 19, 20, and 22 are rejected under 35 U.S.C. 103 as being unpatentable over Hashimoto et al. (US PG PUB 2018/0100012, publication date: 04/12/2018) in view of Lincoln et al. (Tzu Chi Medical Journal, 20(3): 161-168, 2008) and Issar et al. (Clinical Neurophysiology, 130: 2088-2095, 2019).
Hashimoto et al. teach that “[t]herapeutic uses of anti-RGMa antibody against neurological and immunological diseases are disclosed as described above, but conventional antibodies have problems such as insufficient activity, possibility of impairing intrinsic functions of RGMa, and side effects. In particular, conventional antibodies may inhibit binding between RGMa and neogenin, thereby also inhibiting favorable effects such as apoptosis suppression exerted by neogenin bound to RGMa… Thus, an object of the present invention is to provide an RGMa-binding protein which does not inhibit RGMa/neogenin interaction but neutralizes the neurite outgrowth inhibiting activity of RGMa… The inventors of the present invention intensively studied in order to solve the above problems. As a result, the present inventors have succeeded in obtaining an RGMa-binding protein which does not inhibit binding between RGMa and neogenin but neutralizes the neurite outgrowth inhibiting activity of RGMa, and have found that the RGMa-binding protein can be used as a medicine for neurological or immunological diseases, thereby completing the present invention.” At [0006], Hashimoto et al. teach that an anti-RGM neutralizing antibody may serve as an axon regeneration promoting agent. At [0034], Hashimoto et al. teach that anti-RGMa neutralizing antibodies of the invention may be used to treat diabetes mellitus. At [0036], Hashimoto et al. teach 1) an anti-RGM neutralizing antibody that comprises the LCDRs 1-3 and the HCDRs 1-3 of SEQ ID NO(s): 30-35, respectively, and these CDRs share 100% sequence homology with the instant SEQ ID NO(s): 5-10, respectively, corresponding to (a) of claim 10, and 2) an anti-RGM neutralizing antibody that comprises the LCDRs 1-3 and the HCDRs 1-3 of SEQ ID NO(s): 36-40 and SFG, respectively, and these CDRs share 100% sequence homology with the instant SEQ ID NO(s): 11-15 and SFG, respectively, corresponding to (b) of claim 10. Based upon the teachings of Hashimoto et al., one of ordinary skill in the art would have been motivated to treat immunological diseases, such as diabetes mellitus, by administering an anti-RGMa antibody that does not inhibit binding between RGMa and neogenin but neutralizes the neurite outgrowth inhibiting activity of RGMa. Hashimoto et al. do not teach or suggest a method of treating diabetic autonomic neuropathy (DAN) by administering an anti-RGMa antibody that does not inhibit binding between RGMa and neogenin but neutralizes the neurite outgrowth inhibiting activity of RGMa, wherein the DAN is associated with kidney disfunction or chronic kidney disease. These deficiencies are remedied by Lincoln et al. and Issar et al.
Lincoln et al. teach that “[m]icroscopy studies at the light and ultrastructural level have revealed evidence for degenerative changes in autonomic nerves in experimental diabetes. With respect to the sympathetic supply to the small intestine, dystrophic changes have been reported both within the CG/SMG, where the neuronal cell bodies are located, and in their axons supplying the ileum. Terminal tyrosine hydroxylase (TH)-containing nerve fibers within the target have swollen varicosities, a feature characteristic of a degenerative process. Noradrenaline (NA) and its synthetic enzyme, TH, accumulate within the cell bodies of the CG/SMG possibly due to a defect in axonal transport, whereas both NA and TH levels are reduced in the target ileum. A similar pattern has been observed for the intrinsic neurons containing vasoactive intestinal polypeptide (VIP) located in the myenteric plexus that innervate the smooth muscle of the ileum. VIP accumulates in the myenteric neuronal cell bodies, VIP-containing nerves fibers within the smooth musculature have swollen varicosities with ultrastructural evidence of degeneration and fail to release VIP on nerve stimulation. These features reflect the dying back type of distal axonopathy that is generally held to be the characteristic feature of diabetic autonomic neuropathy [DAN] (emphasis added)” See p. 162-163. These teachings suggest that diabetes leads to degenerative changes in autonomic nerves, including features of axonopathy, which is a characteristic feature of DAN.
At p. 163, Lincoln et al. suggest that the neuronal cell death and loss of autonomic neurons that occurs in diabetes is characterized by axonal degeneration - “Whether neuronal cell death and loss of autonomic neurons occur in diabetes remain a matter of controversy. The issue of neuronal cell death was raised when it was reported that both high glucose in vitro and STZ-diabetes in vivo caused apoptosis in sensory neurons located in the lumbar dorsal root ganglion (DRG), and it was suggested that this contributes to the development of axonal degeneration. Since this report, other studies of DRG in diabetes have found conflicting results. It has been proposed that diabetes may cause activation of caspases but that this may not progress fully down the apoptotic pathway to cause cell death. In the sympathetic SMG, neuronal cell counts have not provided any evidence of neuronal loss in diabetes at a stage when degenerative changes in axons can readily be observed.”
Issar et al. teach that “[d]iabetic kidney disease (DKD) is the chronic loss of renal function due to diabetes. The leading cause of chronic kidney disease (CKD) is type 2 diabetes (T2DM) and the growing incidence of T2DM has led to an increase in DKD worldwide (Tuttle et al., 2014). Peripheral neuropathy is one of the most common complications of both T2DM and CKD…” See p. 2088. At p. 2094, Issar et al. teach that “[t]his study has provided evidence that DKD patients exhibit more severe neuropathy and greater nerve dysfunction when compared to patients with either CKD or T2DM alone. Patients with DKD had a higher total neuropathy score and exhibited greater reductions in motor and sensory nerve conduction amplitudes when compared to either T2DM or CKD alone… In conclusion, patients with DKD manifest a more severe neuropathy phenotype and greater nerve dysfunction than patients with either T2DM or CKD alone. Analysis of nerve excitability findings in DKD suggests the CKD component of the condition has a major role in causing axonal dysfunction. Future clinical studies of diabetic neuropathy should examine and report renal status of patients as a complicating pathophysiological factor.”
One of ordinary skill in the art would have been motivated with a reasonable expectation of success at the effective filing date of the invention to combine the teachings of Hashimoto et al. and Lincoln et al. to develop a method of treating DAN by administering an anti-RGMa antibody that does not inhibit binding between RGMa and neogenin but neutralizes the neurite outgrowth inhibiting activity of RGMa. Based upon the teachings of Hashimoto et al., one of ordinary skill in the art would have been motivated to treat immunological diseases, such as diabetes mellitus, by administering an anti-RGMa antibody that does not inhibit binding between RGMa and neogenin but neutralizes the neurite outgrowth inhibiting activity of RGMa, thereby promoting the generation of neurites, such as axons. Furthermore Lincoln et al. suggest that axonopathy and axonal degeneration are characteristics of DAN. Given that the anti-RGMa antibodies of Hashimoto et al. promote the generation of axons, there would have been a reasonable expectation that said antibodies may be used to reverse or improve the negative characteristics of DAN, thereby providing a therapeutic benefit to DAN patients. Therefore in view of the references cited, at the effective filing date of the invention, it would have been prima facie obvious to treat DAN by administering an effective dose of an anti-RGMa neutralizing antibody. Additionally Issar et al. suggest that neuropathy may be more severe in DKD patients. As such one of ordinary skill in the art would have been motivated to practice the method of Hashimoto et al. and Lincoln et al. on patients having diabetic neuropathy, such as DAN, with associated DKD, because said patients likely have an increased need for relief from neuropathy. The invention of Hashimoto et al., Lincoln et al., and Issar et al. meets the limitations of claims 10, 16, and 17.
With respect to claim 19, at [0026], Hashimoto et al. teach that anti-RGMa antibodies of the invention may be humanized.
With respect to claim 20, it is noted that the epitope of the instant SEQ ID NO: 36 is identical to the region from Glu298 to Gly311 of RGMa, and at [0165], Hashimoto et al. teach that anti-RGMa antibodies of the invention may bind to an RGMa protein at an epitope in the region from Glu298 to Gly311.
With respect to claim 22, as indicated above, Hashimoto et al. teach an anti-RGM neutralizing antibody that comprises the LCDRs 1-3 and the HCDRs 1-3 of SEQ ID NO(s): 30-35, respectively, and these CDRs share 100% sequence homology with the instant SEQ ID NO(s): 5-10, respectively, corresponding to (a) of claim 10.
Therefore the invention as a whole was prima facie obvious to one of ordinary skill in the art at the effective filing date of the invention, as evidenced by the references.
Nonstatutory 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 10, 16, 17, 19, 20, and 22 are rejected on the ground of nonstatutory double patenting as being unpatentable over 1) claim 1 of U.S. Patent No. 10,287,346 and 2) claim 1 of US PAT 11,008,388 in view of Hashimoto et al. (US PG PUB 2018/0100012, publication date: 04/12/2018), Lincoln et al. (Tzu Chi Medical Journal, 20(3): 161-168, 2008), and Issar et al. (Clinical Neurophysiology, 130: 2088-2095, 2019).
The teachings of Hashimoto et al., Lincoln et al., and Issar et al. are detailed above.
One of ordinary skill in the art would have been motivated with a reasonable expectation of success at the effective filing date of the invention to combine the conflicting claims with the teachings of Hashimoto et al., Lincoln et al., and Issar et al. to develop a method of treating DAN by administering an anti-RGMa antibody that does not inhibit binding between RGMa and neogenin but neutralizes the neurite outgrowth inhibiting activity of RGMa. One of ordinary skill in the art would have been motivated to do so, because the conflicting claims recite an anti-RGMa neutralizing antibody that comprises the HCDRs and LCDRs of the anti-RGMa neutralizing antibodies recited in parts (a) and (b) of claim 21 and claim 22. Based upon the teachings of Hashimoto et al., one of ordinary skill in the art would have been motivated to treat immunological diseases, such as diabetes mellitus, by administering an anti-RGMa antibody that does not inhibit binding between RGMa and neogenin but neutralizes the neurite outgrowth inhibiting activity of RGMa, thereby promoting the generation of neurites, such as axons. Furthermore Lincoln et al. suggest that axonopathy and axonal degeneration are characteristics of DAN. Given that the anti-RGMa antibodies of Hashimoto et al. promote the generation of axons, there would have been a reasonable expectation that said antibodies may be used to reverse or improve the negative characteristics of DAN, thereby providing a therapeutic benefit to DAN patients. Therefore in view of the references cited, at the effective filing date of the invention, it would have been prima facie obvious to treat DAN by administering an effective dose of an anti-RGMa neutralizing antibody. Additionally Issar et al. suggest that neuropathy may be more severe in DKD patients. As such one of ordinary skill in the art would have been motivated to practice the method of the conflicting claims, Hashimoto et al., and Lincoln et al. on patients having diabetic neuropathy, such as DAN, with associated DKD, because said patients likely have an increased need for relief from neuropathy. The invention of the conflicting claims, Hashimoto et al., Lincoln et al., and Issar et al. meets the limitations of claims 10, 16, and 17.
With respect to claim 19, at [0026], Hashimoto et al. teach that anti-RGMa antibodies of the invention may be humanized.
With respect to claim 20, it is noted that the epitope of the instant SEQ ID NO: 36 is identical to the region from Glu298 to Gly311 of RGMa, and at [0165], Hashimoto et al. teach that anti-RGMa antibodies of the invention may bind to an RGMa protein at an epitope in the region from Glu298 to Gly311.
With respect to claim 22, as indicated above, Hashimoto et al. teach an anti-RGM neutralizing antibody that comprises the LCDRs 1-3 and the HCDRs 1-3 of SEQ ID NO(s): 30-35, respectively, and these CDRs share 100% sequence homology with the instant SEQ ID NO(s): 5-10, respectively, corresponding to (a) of claim 10.
Claims 10, 16, 17, 19, 20, and 22 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 17/322,482 in view of Hashimoto et al. (US PG PUB 2018/0100012, publication date: 04/12/2018), Lincoln et al. (Tzu Chi Medical Journal, 20(3): 161-168, 2008), and Issar et al. (Clinical Neurophysiology, 130: 2088-2095, 2019).
The teachings of Hashimoto et al., Lincoln et al., and Issar et al. are detailed above.
One of ordinary skill in the art would have been motivated with a reasonable expectation of success at the effective filing date of the invention to combine the conflicting claims with the teachings of Hashimoto et al. and Lincoln et al. to develop a method of treating DAN by administering an anti-RGMa antibody that does not inhibit binding between RGMa and neogenin but neutralizes the neurite outgrowth inhibiting activity of RGMa. One of ordinary skill in the art would have been motivated to do so, because the conflicting claims recite an anti-RGMa neutralizing antibody that comprises the HCDRs and LCDRs of the anti-RGMa neutralizing antibodies recited in parts (a) and (b) of claim 21 and claim 22. Based upon the teachings of Hashimoto et al., one of ordinary skill in the art would have been motivated to treat immunological diseases, such as diabetes mellitus, by administering an anti-RGMa antibody that does not inhibit binding between RGMa and neogenin but neutralizes the neurite outgrowth inhibiting activity of RGMa, thereby promoting the generation of neurites, such as axons. Furthermore Lincoln et al. suggest that axonopathy and axonal degeneration are characteristics of DAN. Given that the anti-RGMa antibodies of Hashimoto et al. promote the generation of axons, there would have been a reasonable expectation that said antibodies may be used to reverse or improve the negative characteristics of DAN, thereby providing a therapeutic benefit to DAN patients. Additionaly Issar et al. suggest that neuropathy may be more severe in DKD patients. As such one of ordinary skill in the art would have been motivated to practice the method of the conflicting claims, Hashimoto et al., and Lincoln et al. on patients having diabetic neuropathy, such as DAN, with associated DKD, because said patients likely have an increased need for relief from neuropathy. The invention of the conflicting claims, Hashimoto et al., Lincoln et al., and Issar et al. meets the limitations of claims 10, 16, and 17.
With respect to claim 19, at [0026], Hashimoto et al. teach that anti-RGMa antibodies of the invention may be humanized.
With respect to claim 20, it is noted that the epitope of the instant SEQ ID NO: 36 is identical to the region from Glu298 to Gly311 of RGMa, and at [0165], Hashimoto et al. teach that anti-RGMa antibodies of the invention may bind to an RGMa protein at an epitope in the region from Glu298 to Gly311.
With respect to claim 22, as indicated above, Hashimoto et al. teach an anti-RGM neutralizing antibody that comprises the LCDRs 1-3 and the HCDRs 1-3 of SEQ ID NO(s): 30-35, respectively, and these CDRs share 100% sequence homology with the instant SEQ ID NO(s): 5-10, respectively, corresponding to (a) of claim 10.
This is a provisional nonstatutory double patenting rejection.
Conclusion
No claims are 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 extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NELSON B MOSELEY II whose telephone number is (571)272-6221. The examiner can normally be reached on M-F 9:00 am - 6:00 pm EST
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Samira Jean-Louis, can be reached on 571-270-3503. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/NELSON B MOSELEY II/Primary Examiner, Art Unit 1642