Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
DETAILED ACTION
1. Applicant’s amendment and response filed 3/24/26 is acknowledged and has been entered.
2. Applicant is reminded of Applicant's election of the species of T1d (Type 1 diabetes) and IGRP as the antigen in Applicant’s amendment and response filed 6/27/25.
Claims 23, 28 and 32-34 are presently being examined.
3. Claim interpretation: The specification discloses at [0045] that “biocompatible” means that the components of the delivery system will not cause tissue injury or injury to the human biological system and be regarded as non-toxic to cells, and that “biocompatibility” means that the ingredients and excipients used in the composition will ultimately be bioabsorbed or cleared by the body with no adverse effects to the body. The specification at [0069] discloses that decreased toxicity may refer to a reduction in the accumulation of the NS in organs and/or tissues throughout the body, but may also refer to a decrease in an undesired biological response, such as a decrease in inflammation or in tissue damage of organs throughout the body. The specification discloses at [0046] that “antigen” refers to all, part, fragment, or segment of a molecule that can induce an immune response in a subject or an expansion of anti-pathogenic cells. The specification at [0051] discloses that an “effective amount” is an amount sufficient to achieve the intended purpose such as for example, modulation of T cell activity or T cell populations. The specification at [0057] discloses that “nanosphere” means small discrete particles that are administrable to a subject. The specification further discloses that some nanospheres are substantially spherical, meaning that the shape of the particle does not deviate from a sphere by more than about 10%. The specification discloses that nanospheres of the invention range in size from about 10 nm to about 150 um, and preferably from about 10 nm to about 1 um. The specification discloses at [0047] that the term “about” when used before a numerical designation indicates approximations which may vary by +/- 10%, 5%, or 1%. The specification discloses at [0064] that the term “treating” or “treatment” means treatment of a disease or condition in a patient including preventing or protecting against the condition, inhibiting the disease or condition (i.e., arresting or suppressing the development of clinical symptoms, and/or relieving the disease or condition (i.e., causing the regression of clinical symptoms. The specification discloses at [0196] that the term “iron oxide” is meant to be encompassing of all iron oxides available or known to the skilled artisan and include by way of example, iron oxyhydroxides.
4. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 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 (new matter rejection).
Applicant has amended instant base claim 23 to delete the recitation of “Kg” from the claim. Accordingly, for the purpose of prior art rejections, the filing date of the instant claims is deemed to be the filing date of provisional application 61/387,873.
5. The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
6. Claims 23, 28 and 30-34 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 written description rejection.
This is a new ground of rejection necessitated by Applicant’s amendment filed 3/24/26. Applicant has amended the claims to add new claim limitations and to delete other limitations; however, the issue of written description over the peptide/MHCII complexes was addressed in the prior office action of record and still remains an issue in light of the present amendment of instant base claim 23 for the reasons enunciated below in this rejection.
See claim interpretation section above in this office action.
An applicant shows possession of the claimed invention by describing the claimed invention with all of its limitations using such descriptive means as words, structures, figures, diagrams, and formulas that fully set forth the claimed invention. Lockwood v. Amer. Airlines, Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (Fed. Cir. 1997). Possession may be shown in a variety of ways including description of an actual reduction to practice, or by showing that the invention was "ready for patenting" such as by the disclosure of drawings or structural chemical formulas that show that the invention was complete, or by describing distinguishing identifying characteristics sufficient to show that the applicant was in possession of the claimed invention. See, e.g., Pfaff v. Wells Elecs., Inc., 525 U.S. 55, 68, 119 S.Ct. 304, 312, 48 USPQ2d 1641, 1647 (1998); Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406; Amgen, Inc. v. Chugai Pharm., 927 F.2d 1200, 1206, 18 USPQ2d 1016, 1021 (Fed. Cir. 1991) (one must define a compound by "whatever characteristics sufficiently distinguish it"). "Compliance with the written description requirement is essentially a fact-based inquiry that will ‘necessarily vary depending on the nature of the invention claimed.’" Enzo Biochem, 323 F.3d at 963, 63 USPQ2d at 1612. An invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function. See MPEP 2163 I.A.
An applicant may also show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics. Enzo Biochem, 323 F.3d at 964, 63 USPQ2d at 1613 (quoting the Written Description Guidelines, 66 Fed. Reg. at 1106, n. 49, stating that "if the art has established a strong correlation between structure and function, one skilled in the art would be able to predict with a reasonable degree of confidence the structure of the claimed invention from a recitation of its function".). "Thus, the written description requirement may be satisfied through disclosure of function and minimal structure when there is a well-established correlation between structure and function." See MPEP 2163 II.3.
Applicant has broadly claimed a method of treating an autoimmune disorder or disease comprising administering to a subject in need thereof a pharmaceutical composition comprising an effective amount of a composition comprising a plurality of nanosphere complexes, wherein each nanosphere complex comprises: a biocompatible bioabsorbable nanosphere (NS) metal core composed of iron (III) oxide, wherein the diameter of the metal core is between 5-15 nm, a biodegradable coating comprising dextran and PEG; and an antigen-pMHC class II protein complex covalently coupled to the metal core via an N-maleimide linker, wherein the peptide is derived from human IGRP and the MHC comprises all or part of a[n] HLA-DR, HLA-DQ, or HLA-DP; wherein each dose of the pharmaceutical composition comprises from 0.24 to 6.08 mg, wherein the effective amount is sufficient to expand antipathogenic autoreactive T cells in the subject (as is recited in instant base claim 23), and including the limitations of the dependent claims, and including instant dependent claim 31 that recites “wherein said autoimmune disorder of disease is type I diabetes”.
As such, the claimed method administers and effective amount of a NS comprising a class II MHC/peptide complex, wherein the peptide is derived from IGRP protein (i.e., peptide antigen) and MHC class II comprises all or part of a human MHC II HLA-DR, HLA-DQ, or HLA-DP, wherein the effective amount of the said complex must possess the functional property of expanding any generic antipathogenic autoreactive T cells in vivo in the subject and wherein the NS must treat any generic autoimmune disease or disorder except for the case of T1D that is recited in dependent claim 31 (and wherein the definition in the specification for treating also comprises preventing). In addition, the peptide that is derived from human IGRP must possess the functional property of binding to an HLA-DR, HLA-DQ, or HLA-DP molecule and visa versa.
The specification does not disclose a representative number of species of such IGRP-derived peptide antigen- HLA-DR, HLA-DQ, or HLA-DP complexes, nor sufficient relevant identifying characteristics in the form of structure or functional characteristics coupled with a known or disclosed correlation between structure and function.
In the instant case, Applicant’s elected species of antigen from which a peptide that binds to a class II MHC molecule can derive is IGRP, a protein relevant to type 1 diabetes (T1D). The specification discloses a few peptide epitopes from IGRP that bind to the human HLA-A*0201 MHC class I molecule (e.g., at [0097] and the Table shown on page 30) and one peptide from IGRP that binds to a murine MHC class II molecule ([0197]). The specification does not disclose any species of peptide derived from human IGRP that possesses the functional property of binding to an HLA-DR, HLA-DQ, or HLA-DP molecule, nor wherein the complex thereof has the functional property of expanding antipathogenic autoreactive T cells. The functional property of ‘expanding antipathogenic autoreactive T cells in the subject’ is dependent on the presence of such T cells in vivo (the T cell repertoire in different subjects) that possess a TCR that is cognate for one of the recited complexes and if present, the functional property of binding of the peptide/MHC II complex to a cognate TCR and visa versa.
Given this consideration, the breadth and structural diversity (i.e., the primary amino acid sequence) of the genus of human IGRP peptides (including those relevant to any autoimmune disease or condition), it is clear that the genus of such NS-human IGRP/ HLA-DR, HLA-DQ, or HLA-DP complexes administered in the claimed method is much broader than that disclosed in the specification (since none are disclosed). There is no evidence of record for a representative number of such peptide/MHCII complexes relevant to the genus of autoimmune diseases or disorders that can expand antipathogenic autoreactive T cells in a subject in need thereof, for IGRP or the breadth of the genus of autoantigen epitopes.
In addition evidentiary reference HLA Nomenclature 2023 (2 pages, of record) teaches that there are over 10,700 different HLA class II molecules alone (i.e., human MHC II molecules that include HLA-DR, HLA-DQ, or HLA-DP molecules) (see entire reference, especially the Numbers of HLA Alleles section). There is no evidence of record for a correlation between the primary amino acid sequence of a MHC binding peptide (i.e, the structure) and the functional ability to expand antipathogenic T cells in a subject.
Therefore, it appears that the instant specification does not adequately disclose the breadth of the NS/pMHCII complexes in the administered pharmaceutical composition comprising them recited in the instant claims. In light of this, a skilled artisan would reasonably conclude that Applicant was not in possession of the genus of all such NS-human IGRP/ HLA-DR, HLA-DQ, or HLA-DP MHCII complexes and pharmaceutical compositions thereof, and hence was not in possession of the method that administers them to treat an autoimmune disease or disorder at the time the instant application was filed.
Applicant’s arguments of record in the amendment and response filed 3/24/26 on page 6 at section E have been fully considered but are not persuasive for the reasons enunciated therein.
7. Claims 23, 28 and 30-34 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
This is a new ground of rejection necessitated by Applicant’s amendment filed 3/24/26, as Applicant has amended the claims to add new claim limitations that have necessitated changes to the prior rejection of record.
“To be enabling, the specification of a patent must teach those skilled in the art how to make and use the full scope of the claimed invention without ‘undue experimentation.’” Genentech, Inc. v. Novo Nordisk, A/S, 108F.3d 1361, 1365, 42 USPQ2d 1001, 1004 (Fed. Cir. 1997) (quoting In re Wright, 999F2d 1557, 1561, 27 USPQ2d 1510, 1513 (Fed. Cir. 1993)). In In re Wands 8 USPQ2d 1400 (CAFC 1988), a number of factors are set forth which a court may consider in determining whether a disclosure would require undue experimentation. These factors were set forth as follows: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims. All the factors need not be reviewed when determining whether a disclosure is enabling. Amgen, Inc. v. Chugai Pharm. Co., Ltd., 927F2.d 1200, 1213, 18 USPQ2d 1016, 1027 (Fed. Cir. 1991) (noting that the Wands factors “are illustrative, not mandatory. What is relevant depends upon the facts.”).
The specification does not disclose how to use the instant invention, a method of treating an autoimmune disorder or disease comprising administering to a subject in need thereof a pharmaceutical composition comprising an effective amount of a composition comprising a plurality of nanosphere complexes, wherein each nanosphere complex comprises: a biocompatible bioabsorbable nanosphere (NS) metal core composed of iron (III) oxide, wherein the diameter of the metal core is between 5-15 nm, a biodegradable coating comprising dextran and PEG; and a peptide/MHC class II protein complex covalently coupled to the metal core via an N-maleimide linker, wherein the peptide is derived from human IGRP and wherein the MHC comprises all or part of a HLA-DR, HLA-DQ, or HLA-DP, wherein each dose of the pharmaceutical composition comprises from 0.24 to 6.08 mg, wherein the effective amount is sufficient to expand antipathogenic autoreactive T cells in the subject, and including the limitations of the dependent claims.
As is stated in the claim interpretation above in this office action, the specification discloses at [0064] that the term “treating” or “treatment” means treatment of a disease or condition in a patient including preventing or protecting against the condition, inhibiting the disease or condition (i.e., arresting or suppressing the development of clinical symptoms, and/or relieving the disease or condition (i.e., causing the regression of clinical symptoms.
The specification has not enabled the breadth of the claimed invention because: (1) the claims encompass a method of prevention and treatment of any autoimmune disorder or disease by administering the recited nanospheres that comprise a human IGRP peptide complexed with a human MHC class II molecule that is one of allele products of HLA-DR, HLA-DQ, or HLA-DP, wherein practicing the method is unpredictable because of the prevention aspect of the definition in the specification for “treatment” for any autoimmune disorder or disease including T1D (type 1 diabetes), (2) because of the treatment aspect of treating any autoimmune disorder or disease (that is not T1D) with an IRGP/human class II MHC complex, and (3) because there is no evidence of record for a genus of IGRP derived peptides that bind to [the over 10,700 different] human HLA class II molecules that are alleles of HLA-DR, HLA-DQ, or HLA-DP that can be administered coupled to a nanosphere in the claimed method.
The state of the art is such that it is unpredictable in the absence of appropriate evidence whether the claimed method can be practiced without undue experimentation.
Applicant’s elected species of antigen from which a peptide that binds to a class II MHC molecule can derive is IGRP, a protein relevant to type 1 diabetes (T1D). The specification discloses a few peptide epitopes from IGRP that bind to the human HLA-A*0201 MHC class I molecule (e.g., at [0097], [0008], and the Table shown on page 30) and one peptide from IGRP that binds to a murine MHC class II molecule ([0197]). There is no evidence of record that any of these peptides bind to a human MHC class II molecule. There is no disclosure of any peptides from human IGRP that bind to any of the human MHC class II molecules encompassed by HLA-DR, HLA-DQ, or HLA-DP. The specification discloses at [0005] that T1D in mice is associated with autoreactive CD8+ T cells (i.e., T cells that recognize class I MHC, not class II MHC).
Expanding antipathogenic autoreactive T cells in the subject is dependent on the presence of such T cells in vivo that possess a TCR that is cognate for one in the broad genus of such peptide-MHCII complexes (i.e., it is dependent upon the T cell repertoire in different subjects).
The specification also discloses a variety of MHC class I peptide antigens (not MHC class II peptide antigens) for T1D [0019], as well as for other autoimmune diseases. The specification discloses a non-limiting laundry list of such autoimmune diseases or conditions at e.g., at [0022].
It is clear that the breadth of the genus of an autoimmune disease or disorder and the MHC class II binding epitope peptides relevant to such diseases or disorders is much broader than the disclosure in the specification or relevant disclosure in the art, particularly since no human IGRP peptides relevant to binding to human MHC class II molecules such as the genus of allele products of HLA-DR, HLA-DQ, or HLA-DP are disclosed in the specification or made of record in the instant application, and particularly as human IGRP peptides would be expected to be potentially relevant to treating T1D.
Evidentiary reference Miller, Frederick W. (Curr. Opin. In Immunol. 2023, 80: 102266, 9 pages, of record) teaches “Autoimmunity is characterized by self-reactive immune components and autoimmune disease by autoimmunity plus pathology” (abstract). Frederick further teaches that “Although proposals have been made regarding approaches to define autoimmunity and specific autoimmune diseases, there are still no commonly agreed-upon general criteria for these…This lack of consensus in autoimmune disease definitions, and even agreement on which specific illnesses constitute the autoimmune diseases, impede research and clinical care” (introduction section). See entire reference.
Evidentiary reference Rose, Noel R. (Amer. J. Epidemiol., 2016, 183(5): 403-406, of record) teaches “individual cells, animals, and humans differ in an almost infinite number of characteristics representing their biologic individuality” and “most autoimmune diseases develop over a long period of time, during which the patients are clinically asymptomatic…Unfortunately…biological signs (of autoimmunity) do not become diagnostically apparent until irreversible tissue damage has occurred. Treatment of autoimmune disease today still focuses on compensating for or repairing damage already inflicted rather than curing the patient” (page 404 at the first three full paragraphs). Rose also states that it has long been possible to prevent many autoimmune diseases in models of autoimmune disease in inbred genetically homogenous animals housed under standard conditions (prevention section). Human patients do not fit these criteria as Rose teaches “Humans, however, are far from homogenous. This exemplifies the major problem in directly applying the results of reductionist experimental findings to human populations. It has become axiomatic that all of the experiments done on a single inbred strain of mice correspond to research on a single human individual (first full paragraph on page 406). See entire reference.
There is insufficient guidance in the specification as to how to use the instant invention. Undue experimentation would be required of one skilled in the art to practice the instant invention. See In re Wands 8 USPQ2d 1400 (CAFC 1988).
Applicant’s arguments of record in the amendment and response filed 3/24/26 on page 6 at section ”F” have been fully considered but are not persuasive for the reasons enunciated therein.
8. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 38 and 30-34 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.
9. The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
10. Claim 28 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
This is a new ground of rejection necessitated by Applicant’s amendment filed 3/24/26. Applicant has presently amended instant base claim 23 to recite “wherein the peptide is derived from human IGRP and the MHC comprises all or part of a HLA-DR, HLA-DQ, or HLA-DP”.
Claim 28 recites the limitation “wherein the peptide comprises an epitope derived from an antigen selected from the group consisting of PPI, IGRP, GAD, and pro-insulin, and the MHCII comprises HLA-DR”. This limitation lacks antecedent basis in instant base claim 23 because the said base claim presently recites “wherein the peptide is derived from human IGRP”. Dependent claim 28 recites that the peptide comprises an epitope derived from other than human IGRP (i.e., peptides derived from PPI, GAD and pro-insulin are not human IGRP derived peptides, nor are peptides derived from IGRP necessarily human IGRP derived peptides, “IGRP” being broader than “human IGRP”).
11. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 under pre-AIA 35 U.S.C. 103(a) as being unpatentable over WO2012/041968 A1 (IDS reference) in view of Pfister and Morbidelli (J. Contr. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has amended instant base claim 23 to delete the limitation that constituted new matter. In light of this, the primary art reference cited in this rejection is no longer available as prior art. In addition, Applicant has also amended the claims to introduce limitations that are not taught by the art references, i.e., “wherein the peptide is derived from human IGRP and the MHC comprises all or part of a HLA-DR, HLA-DQ, or HLA-DP”.
12. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 under 35 U.S.C. 103 as being unpatentable over US 2025/0121043 A1 (PgPub of application serial no. 18/638,077, with priority to at least 3/7/08) in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has amended instant base claim 23 to delete the limitation that constituted new matter. In light of this, the WO2012 reference cited in this rejection is no longer available as prior art. In addition, Applicant has also amended the claims to introduce limitations that are not taught by the art references, particularly human IGRP derived peptides that bind to HLA-DR, HLA-DQ, or HLA-DP. The primary art reference discloses (e.g., at [0010]) that IGRP has been recently identified as being of potential relevance in human T1D and that two HLA-A*0201 (class I MHC, not class II MHC that is recited in the instant claims) binding epitopes of human IGRP are recognized by islet-associated CD8+ T cells (that recognize class I MHC, not class II MHC) from murine MHC I deficient NOD mice expressing an HLA-A*0201 transgene.
13. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 under 35 U.S.C. 103 as being unpatentable over US 10,080,808 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has amended instant base claim 23 to delete the limitation that constituted new matter. In light of this, the US 10,080,808 and WO2012 references cited in this rejection are no longer available as prior art. In addition, Applicant has also amended the claims to introduce limitations that are not taught by the art references, particularly human IGRP derived peptides that bind to HLA-DR, HLA-DQ, or HLA-DP.
14. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 under 35 U.S.C. 103 as being unpatentable over US 9,603,948 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has amended instant base claim 23 to delete the limitation that constituted new matter. In light of this, the US 9,603,948 and WO2012 references cited in this rejection are no longer available as prior art. In addition, Applicant has also amended the claims to introduce limitations that are not taught by the art references, particularly human IGRP derived peptide that binds to HLA-DR, HLA-DQ, or HLA-DP.
15. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 under 35 U.S.C. 103 as being unpatentable over U.S. Patent No. 8,354,110 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has amended instant base claim 23 to delete the limitation that constituted new matter. In light of this the WO2012 reference cited in this rejection is no longer available as prior art.
16. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 as rejected on the ground of nonstatutory double patenting as being unpatentable over claims 137-156 of copending Application No. 18/645,030 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has amended the claims to delete recitation of the limitation that constitutes new matter. Accordingly, the WO2012 and Pfister and Morbidelli references are no longer available as prior art references. However, for completeness of the record, Applicant’s arguments (spanning pages 11-12 of the amendment and response filed 3/24/26) that the claims of 18/645,030 are drawn to a product are not persuasive, as the claim set of ‘030 comprises a method of treating an autoimmune disease with the product. In addition, Applicant’s arguments pertaining to patentable distinction between product and method claims is not persuasive, as only divisional applications of the instant application are entitled to the 35 U.S.C. 121 safe harbor provision. 18/645,030 was not filed as a divisional of the instant application.
17. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 as provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 47-63 of copending Application No. 18/638,077 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has amended the claims to delete recitation of the limitation that constitutes new matter. Accordingly, the WO2012 and Pfister and Morbidelli references are no longer available as prior art references.
18. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 as provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 2, 5, 7, 8, 10-18, 20-36 of copending Application No. 17/661,873 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has amended the claims to delete recitation of the limitation that constitutes new matter. Accordingly, the WO2012 and Pfister and Morbidelli references are no longer available as prior art references.
19. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 as provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 38, 39, 40, 42, 44, 46, 48, 52-56, 62, 63, 66, 69 and 71-73 of 17/532,584.
Applicant has amended the claims to include recitation of a peptide from human IGRP and an HLA-DR, HLA-DQ, or HLA-DP molecule, limitations that the claims of 17/532,584 do not recite. In addition, the claims of 17/532,584 recite treating a hepatic disease, which is not relevant to IGRP as is presently recited in instant base claim 23.
20. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 as rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. 12,397,038 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has amended the claims to delete recitation of the limitation that constitutes new matter. Accordingly, the WO2012 and Pfister and Morbidelli references are no longer available as prior art. In addition, the claims of US 12,397,038 administer MHC class II binding peptides from PDC-E2 antigen of primary biliary cirrhosis (PBC), rather than a human IGRP peptide as is presently recited in instant base claim 23.
21. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 30 and 32-34 as rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 10,080,808 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has deleted recitation of the limitation that constitutes new matter. Accordingly, the WO2012 and Pfister and Morbidelli references are no longer available as prior art. In addition, the method of the claims of US 10,080,808 recite administering MHCII/peptide-NPs with the peptide being MS-related, not related to IGRP as is presently recited in instant base claim 23.
22. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 30 and 32-34 as rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. 9,603,948 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contro. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has deleted recitation of the limitation that constitutes new matter. Accordingly, the WO2012 and Pfister and Morbidelli references are no longer available as prior art. In addition, the claims of US 9,603,948 do not recite that the antigen peptide is from human IGRP, as is presently recited in instant base claim 23.
23. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 28 and 30-34 on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 6-21 of U.S. Patent No. 8,354,110 in view of WO2012/041968 A1 (IDS reference), Pfister and Morbidelli (J. Contr. Release, 2014, 180: 134-149, IDS reference), and Cochran et al (Immunity, 2000, 12: 241-250, IDS reference).
Applicant has deleted recitation of the limitation that constitutes new matter. Accordingly, the WO2012 and Pfister and Morbidelli references are no longer available as prior art.
24. Applicant’s amendment filed 3/24/26 has overcome the prior rejection of record of claims 23, 30 and 32-34 on the ground of nonstatutory double patenting as being unpatentable over claims 1-8 of U.S. Patent No.12,011,480 in view of WO2012/041968 A1 (IDS reference).
Applicant has deleted recitation of the limitation that constitutes new matter. Accordingly, the WO2012 reference is no longer available as prior art, nor do the claims of US 12,011,480 recite IGRP peptide as is presently recited in instant base claim 23.
25. No claim is allowed.
26. 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.
27. Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARIANNE DIBRINO whose telephone number is (571)272-0842. The examiner can normally be reached on M, T, Th, F.
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/Marianne DiBrino/
Marianne DiBrino, Ph.D.
Patent Examiner
Group 1640
Technology Center 1600
/MISOOK YU/Supervisory Patent Examiner, Art Unit 1641
Prosecution Insights