DETAILED ACTION
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 .
Priority
This application is a 371 of PCT/US2022/016924 filed 02/18/2022 which claims benefit of provisional application 63/289,439 filed 12/14/2021 and claims benefit of provisional application 63/151,190 filed 02/19/2021. Applicant's claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 06/26/2026 complies with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Status of the Claims
Claims 1-6, 9-18, 20-24 and 26-28 are pending. Claims 1-5 are amended. Claims 12-18, 20-24 and 26-28 are withdrawn.
Claims 1-6 and 9-11 (claim set filed 06/26/2026) are examined on the merits herein.
Withdrawal of Rejections
The response and amendment filed on 06/26/2026 are acknowledged. All of the amendment and arguments have been thoroughly reviewed and considered.
For the purposes of clarity of the record, the reasons for the Examiner's withdrawal and/or maintaining, if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner's response to arguments section.
The previous claim 2 objection has been withdrawn necessitated by amendment of claim 1 reciting description for acronym NTPDase.
The previous claims 3-5 rejections under 35 U.S.C. 112(b) have been withdrawn necessitated by amendment of claims 3-5.
Claim Objections
Claim 1 is objected to because of the following informalities:
Claim 1 recites: “wherein is the enzyme is a member”. Applicant is suggested to replace recitation with: “wherein the enzyme is a member”
Appropriate correction is required.
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 4 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 4 is directed to the enzyme being an acid phosphatase. Claim 4 is dependent on amended claim 1 which now requires the enzyme to be a member of the GDA_CD39 superfamily. Acid phosphatase of claim 4 belongs to a different enzyme family and not to the GDA_CD39 superfamily. The specification defines GDA_CD39 superfamily as: “enzymes comprised of nucleoside triphosphate diphosphohydolases (NTPDases) with common motifs in their protein sequences. … Non-limiting examples include ecto-ATPases, apyrases, CD39s, and ecto-ATP/Dases” (paragraph 0036). Additionally, Table 4 (paragraph 0154) provides list of enzymes of interest and clearly separates enzymes belonging to GDA_CD39 superfamily and belonging to acid phosphatase family. Therefore, since claim 4 does not further limit the independent claim 1, from which it depends, claim 4 is rejected.
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 5, dependent on claim 4, does not resolve the issue mentioned above and is rejected.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1, 2, 6 and 9-11 are rejected under 35 U.S.C. 103 as being unpatentable over Knowles (Knowles Purinergic Signalling, 2011, 7, 21-45), Idzko (Idzko et al. Nature, 2014, 509, 310-317) and Jolly (US 2011 0200574 A1).
Regarding claim 1, Knowles teaches GDA1_CD39 superfamily of nucleoside triphosphate diphosphohydrolases (NTPDases) (Abstract). Knowles describes that these proteins hydrolyze triphosphates and diphosphates, are present in many organisms (Abstract) and have common motifs in their sequences (p. 21, right column). Knowles reviews NTPDases from vertebrates (p. 23), plants (p. 29), yeast (p. 31) and pathogenic organisms including parasites (p. 30-31). Knowles describes bacterial NTPDase identified in Legionella pneumophila the sequence of which is closely related to vertebrate NTPDase1, and which can hydrolyze ATP and GTP (p. 31, left column, 3rd paragraph). Knowles mentions that with “the discovery of an NTPDase in bacteria, there is little doubt that NTPDases occur throughout the evolutionary tree” (p. 39, left column, last paragraph).
The limitation of enzyme being active at least from about pH 3.5 to pH 7, is interpreted as a functional property of the structure, the enzyme of GDA1_CD39 superfamily. MPEP 2112.01: “Products of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present.” Since Knowles teaches the enzymes of GDA1_CD39 superfamily, these enzymes would necessarily be active at least from about pH 3.5 to pH 7.
Knowles does not teach an enteric coating.
Idzko teaches that inflammatory conditions are associated with the extracellular release of nucleotides, particularly ATP (Abstract). ATP functions as signaling molecule activating P2 receptors. P2X/P2Y signaling can promote chronic inflammation during different conditions including inflammatory bowel disease (IBD) (Abstract). Idzko mentions that deficiency of NTPDase 1(CD39) could be associated with IBD (p. 314, right column, 5th paragraph). Idzko discloses that termination of P2 receptor signaling involves hydrolysis of ATP by ectonucleotidases, such as NTPDases, especially NTPDase 1 (p. 314, right column, 4th paragraph). Idzko suggests treatment strategies for acute and chronic inflammatory disease by blocking P2R signaling and promoting ATP conversion to adenosine (p. 315, right column, 2nd paragraph).
Jolly teaches enzyme compositions used to treat gluten intolerance (Abstract). Jolly describes that the composition may be formulated for oral delivery and contain enteric coating (paragraph 0014). Jolly mentions that the enteric coating allows delivery of the active agent to the intestine resisting digestion in acidic stomach conditions (paragraph 0119). Jolly discloses different polymers and other agents to be used for the enteric coating (paragraphs 0120, 0121).
First, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to make composition comprising GDA1_CD39 NTPDase from Knowles teaching which can be used for treatment of inflammatory disease such as IBD. One would have been motivated to do that because Knowles describes NTPDases from various organisms with ATPases activity and Idzko teaches that extracellular release of ATP promotes chronic inflammation in conditions such as IBD and suggests treatment of chronic inflammation by conversion of ATP. A skilled artisan would have reasonably expected success in that since Knowles and Idzko teach NTPDases with ATP hydrolyzing activity.
Second, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to add enteric coating taught by Jolly to the enzyme composition for hydrolysis of ATP based on Knowles and Idzko teachings. One would have been motivated to do that because Idzko teaches that removal of ATP can be used for treatment of chronic inflammatory diseases such as IBD and Jolly teaches the enteric coating for delivery of the active agent to the intestine resisting digestion in acidic stomach conditions and provides instructions for enteric coating preparation. A skilled artisan would have reasonably expected success in that since Knowles provides the GDA1_CD39 enzyme for conversion of ATP, Idzko identifies inflammatory bowel disease as one of the conditions requiring ATP hydrolysis to decrease inflammation and Jolly provides enteric coating for delivery of enzymes to the intestines. Thus, Knowles, Idzko and Jolly teachings render claim 1 obvious.
Regarding claim 2, Knowles teaches NTPDases of different organisms belonging to GDA1_CD39 superfamily, including several plant NTPDase, e.g. from pea, Arabidopsis, soybean (Abstract, p. 29, right column, 1st paragraph). Thus, Knowles, Idzko and Jolly teachings render claim 2 obvious.
Regarding claim 6, Knowles teaches the nucleotide triphosphate to comprise ATP. For instance, L. pneumophila NTPDase expressed in E. coli was shown to hydrolase ATP, GTP, ADP and GDP (p. 31, left column, 3rd paragraph). Thus, Knowles, Idzko and Jolly teachings render claim 6 obvious.
Regarding claim 9, the recited in the “wherein” clause, i.e. hydrolysis of ATP with a specific activity of at least about 500 µmol/mg/min to about 2700 µmol/mg/min from about pH 3.5 to about pH 7, is interpreted as functional property of the claimed structure. MPEP 2112.01 states: "Products of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present." In instant case, the art renders the instantly claimed composition obvious and therefore, the composition taught by prior art of Knowles, Idzko and Jolly will necessarily have the same property of the recited rate of ATP hydrolysis in the recited pH range, especially since Knowles and Idzko teach NTPDases to hydrolyze ATP. Thus, Knowles, Idzko and Jolly teachings render claim 9 obvious.
Regarding claim 10, Jolly teaches enzyme composition formulated for oral delivery and containing enteric coating (paragraph 0014). Regarding claim 11, Jolly teaches rectal administration of the composition and describes the corresponding dosage units as suppositories or gelatin-rectal capsules containing enzyme mixed with a vegetable oil or paraffin oil (paragraph 0122). The gelatin in gelatin capsules can serve as enteric coating formulated for rectal administration.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use enteric coating taught by Jolly for oral and rectal administration of the enzyme composition for hydrolysis of ATP based on Knowles and Idzko teachings. One would have been motivated to do that with reasonably expected success because Knowles provides the GDA1_CD39 enzyme for conversion of ATP, Idzko identifies inflammatory bowel disease as one of the conditions requiring ATP hydrolysis to decrease inflammation and Jolly provides instructions for preparation of specific enteric coating for oral delivery to intestines to avoid composition digestion in acidic stomach conditions and for rectal delivery. Thus, Knowles, Idzko and Jolly teachings render claims 10 and 11 obvious.
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Knowles (Knowles Purinergic Signalling, 2011, 7, 21-45), Idzko (Idzko et al. Nature, 2014, 509, 310-317) and Jolly (US 2011 0200574 A1) as applied to claim 1 above, and further in view of GenBank EKE69473.1 (nucleoside phosphatase GDA1/CD39, NCBI, 2012 [retrieved on 03/24/2026]. Retrieved from the Internet: <nucleoside phosphatase GDA1/CD39 [Gallaecimonas xiamenensis 3-C-1] - Protein - NCBI>).
The teaching of Knowles, Idzko and Jolly have been set forth above.
Knowles, Idzko and Jolly do not teach the enzyme to comprise a polypeptide at least 40% identical to SEQ ID NO:9.
GenBank EKE69473.1 teaches nucleoside phosphatase of GDA1/CD39 family derived from Gallaecimonas xiamenensis. The sequence of that nucleoside phosphatase comprises the polypeptide 100% identical to SEQ ID NO:9 (elected species).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to try using nucleoside phosphatase taught by GenBank EKE69473.1 in the enzyme composition for hydrolysis of ATP based on Knowles, Idzko and Jolly teachings. One would have been motivated to do that because GenBank EKE69473.1 provides annotated sequence for bacterial nucleoside phosphatase of GDA1/CD39 family and Knowles teaches NTPDases of GDA1/CD39 family to have common sequence motifs and describes bacterial NTPDase of GDA1/CD39 family from Legionella pneumophila the sequence of which is closely related to vertebrate NTPDase1 and which can hydrolyze ATP and indicates the potential presence of similar enzymes in other organisms, including bacteria. A skilled artisan would have reasonably expected success in that since combination of Knowles, Idzko and Jolly teaches enzyme composition for treatment of inflammatory bowel disease including various NTP hydrolases and GenBank EKE69473.1 provides sequence for such enzyme. Thus, teachings of Knowles, Idzko, Jolly and GenBank EKE69473.1 teachings render claim 3 obvious.
Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Knowles (Knowles Purinergic Signalling, 2011, 7, 21-45), Idzko (Idzko et al. Nature, 2014, 509, 310-317) and Jolly (US 2011 0200574 A1) as applied to claim 1 above, and further in view of Anand (Anand and Srivastava Appl. Biochem. Biotechnol., 2012, 167, 2174-2197).
The teachings of Knowles, Idzko and Jolly have been set forth above.
Knowles, Idzko and Jolly do not teach acid phosphatase in the composition.
Regarding claim 4, Anand teaches structure, properties and catalytic mechanism of acid phosphatases (Abstract). Anand discloses that acid phosphatases (EC 3.1.3.2) catalyze hydrolysis of phosphate monoesters in acidic conditions at pH 4-7 (p. 2174, last paragraph). Anand provides examples of acid phosphatases of different origin having activity at acidic pH and mentions acid phosphatase from Aspergilius niger which is active at highly acidic pH of 2.0-2.4 (p. 2183, last paragraph, p. 2184, 1st paragraph). Anand describes that acid phosphatases can hydrolyze a wide range of phosphorylated esters and some of them are more specific to triphosphate nucleotides, such as ATP, UTP or GTP (p. 2184, last paragraph). Anand discloses that acid phosphatases are abundantly present in nature and were found in plants, animals, bacteria and fungi (p. 2175, 1st paragraph). Anand mentions homology of the catalytic site of acid phosphatases in plants, animals and bacteria (p. 2181, last paragraph). Anand provides examples of acid phosphatases derived from different sources and not from Shigella (p. 2177-2178, Table 1).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to follow Anand teaching and substitute GDA1_CD39 NTPDase in the composition for treatment of inflammatory disease such as IBD based on Knowles, Idzko and Jolly teachings with acid phosphatase from Anand teaching. One would have been motivated to do that because acid phosphatase can perform the same function of ATP hydrolysis and in acidic pH as taught by Anand as NTPDase of Knowles teaching and hence can be used for treatment of chronic inflammation by conversion of ATP as suggested by Idzko. A skilled artisan would have reasonably expected success in that since Knowles and Anand teach enzymes hydrolyzing ATP, Idzko identifies inflammatory bowel disease as one of the conditions requiring ATP hydrolysis to decrease inflammation and Jolly provides enteric coating for delivery of enzymes to the intestines. Thus, teachings of Knowles, Idzko, Jolly and Anand teachings render claim 4 obvious.
Claim 5 is rejected under 35 U.S.C. 103 as being unpatentable over Knowles (Knowles Purinergic Signalling, 2011, 7, 21-45), Idzko (Idzko et al. Nature, 2014, 509, 310-317), Jolly (US 2011 0200574 A1) and Anand (Anand and Srivastava Appl. Biochem. Biotechnol., 2012, 167, 2174-2197) as applied to claims 1 and 4 above, and further in view of Zimmerman (US20200291366 A1).
The teachings of Knowles, Idzko, Jolly and Anand have been set forth above.
Knowles, Idzko, Jolly and Anand do not teach the enzyme at least 50% identical to SEQ ID NO:18 (elected species).
Regarding claim 5, Zimmerman teaches optimization of various enzymes for enhanced stability without changing either enzymatic properties or enzyme active site conformation. The design provides mutant enzymes with increased stability, surface polarity and higher functional expression compared to the wild-type enzyme (Abstract). Among various enzymes Zimmerman describes the wild-type and mutant bacterial acid phosphatases. Zimmerman mentions that acid phosphatases have optimum pH in the range of 4-6 and describes designed improved variants of acid phosphatases have improved stability at acidic pH (paragraph 0578). One of such acid phosphatases is the wild-type and variant acid phosphatase from Shimbella blattae with SEQ ID NO: 48 (paragraph 0579). The sequence with SEQ ID NO:48 of Zimmerman has 56.4% identity to instant SEQ ID NO:18 (elected species).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to try using acid phosphatase taught by Zimmermann in the enzyme composition for hydrolysis of NTP based on Knowles, Idzko, Jolly and Anand teachings. One would have been motivated to do that because Anand teaches bacterial acid phosphatases with hydrolytic activity at low pH and Zimmerman provides sequence for bacterial acid phosphatase with improved stability at acidic pH. A skilled artisan would have reasonably expected success in that since Knowles and Anand teach enzymes hydrolyzing ATP, Idzko identifies inflammatory bowel disease as one of the conditions requiring ATP hydrolysis to decrease inflammation, Anand describes properties of various acid phosphatases including bacterial acid phosphatases and Zimmerman provides sequence for improved bacterial acid phosphatase. Thus, Knowles, Idzko, Jolly, Anand and Zimmerman teachings render claim 5 obvious.
Response to Arguments
Applicant's arguments filed 06/26/2026 have been fully considered but they are not persuasive.
Applicant’s arguments with respect to prior art of Sevigny and NCBI WP_054306375.1 are moot because the current rejection is modified necessitated by amendment of claims and now rejection is based on combination of the prior art of Knowles, Idzko, Jolly, Anand and Zimmerman as described above. The arguments related to the same prior art as present in the previous Office action will be addressed.
Applicant argues (addressing p. 7-8 of the Remarks) that “Anand provides no teaching or guidance that a person of ordinary skill in the art would select a particular non-mammalian CD39-like enzyme, expect it to hydrolyze extracellular ATP with high specific activity across a broad pH range of about 3.5 to about 7, or successfully employ such an enzyme in an enterically delivered composition for in vivo treatment of inflammatory bowel disease.” These arguments are not persuasive because:
In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., high specific activity, extracellular ATP, in vivo treatment of inflammatory bowel disease) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
Prior art of Anand is referred to in the rejection of claims 4 and 5 only which are directed acid phosphatases. Anand teaches that acid phosphatases from different organisms catalyze hydrolysis of phosphate monoesters including ATP in acidic conditions at pH 4-7 (p. 2174, last paragraph, p. 2184, last paragraph) that covers the requirements for the enzyme of claim 1, except being a member of GDA1_CD39 family. Please see 112(d) rejection regarding that issue. Since acid phosphatase from Anand teaching has features of the claimed enzyme, that provides motivation to substitute GDA1_CD39 NTPDase in the composition for treatment of inflammatory disease such as IBD based on Knowles, Idzko and Jolly teachings with acid phosphatase of Anand teaching.
Applicant argues (addressing p. 8-9 of the Remarks) that Jolly “discloses general principles of enteric coating to protect enzymes from gastric degradation, it does not address the selection, function, or therapeutic role of non-mammalian GDA1_CD39 enzymes, nor does it suggest that enteric coating would enable such enzymes to modulate inflammatory pathways in the gut by hydrolyzing nucleotide triphosphates”. These arguments are not persuasive because:
Jolly teaches the enteric coating for delivery of an active agent such as enzyme to the intestine resisting digestion in acidic stomach conditions and provides instructions for enteric coating preparation (paragraphs 0119-0121). Since GDA1_CD39 NTPDase can be used for treatment of intestinal inflammatory disease (IBD) as suggested based on prior art of Knowles and Idzko, that provides motivation to use instructions of Jolly for enteric coating to deliver the enzyme of interest to the same destination, i.e. intestines. Jolly mentions that enteric coating can be selected such that it does not degrade the active ingredient in the core (paragraph 0119). The purpose of enteric coating of Jolly is to deliver enzyme of interest to intestines, and the active ingredient (enzyme) is determined based on prior art of Knowles and Idzko as described in the current rejection.
Applicant argues (addressing p. 8-9 of the Remarks) that GenBank EKE69473.1 does not characterize the disclosed enzyme as suitable for gastrointestinal administration, as capable of hydrolyzing extracellular ATP in vivo, or as functioning across a broad pH range of about 3.5 to about 7 following enteric delivery. These arguments are not persuasive because:
Claim 3 and claim 1, claim 3 depends upon, do not require NTPDase to be capable of hydrolyzing extracellular ATP in vivo. The requirements for the enzyme are: to belong to GDA1_CD39 family of enzymes, have nucleotide triphosphate hydrolyzing activity in pH range of 3.5-7 (please see interpretation of claim 1 in the rejection), not being mammalian NTPDase and comprising at least 40% sequence identity to SEQ ID NO: 9. GenBank EKE69473.1 teaches enzyme belonging to GDA1_CD39 family, being not mammalian enzyme and having 100% sequence identity to SEQ ID NO: 9. Regarding activity at pH range of 3.5-7, this limitation is interpreted as inherent property of the enzyme of GDA1_CD39 superfamily as described in the rejection above. Knowles teaches GDA1_CD39 enzymes to be present in different organisms including bacteria and describes that enzymes belonging to that superfamily have common motifs in their sequences (p.21, right column). For instance, the sequence of L. pneumophila NTPDase is closely related to vertebrate NTPDase 1 (p. 31, left column, 3rd paragraph). NTPDase 1 is taught by Idzko to be expressed in many tissues and terminating P2R inflammatory signalling by ATP conversion (p. 314, right column, 4th paragraph). Therefore, one would be motivated to expect GDA1_CD39 NTPDase of GenBank EKE69473.1 to have nucleotide triphosphate hydrolyzing activity in pH range of 3.5-7 and to try using that NTPDase in the enteric composition for intestinal inflammatory conditions.
Therefore, the 35 U.S.C. 103 rejection is maintained and modified necessitated by the amendment of the claims.
Conclusion
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/L.G.K./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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