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 .
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1-14 and 16-18 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural phenomenon without significantly more.
Independent claim 1 recites a method for prognosis and/or detection of a progerin-related aging pathology in a subject that comprises quantitating the concentration of progerin in in the sample. Independent claim 9 recites a method for determining the efficacy of a treatment for a progerin-related aging pathology that comprises determining the concentration of progerin in a pre-treatment sample from a subject. Independent claim 16 recites method for treatment of a progerin-related aging pathology in a subject that comprises quantitating the concentration of progerin in in the sample.
All the independent claims are directed to a relationship between progerin concentration and progerin-related aging pathology which is a natural correlation, which is a judicial exception.
These judicial exceptions are not integrated into a practical application, such as constituting an improvement in the technological field, or including steps recited in addition to the judicial exception that integrates detection of the natural phenomena into a particular treatment. The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exceptions because the additional elements fail to provide either an inventive concept or impose meaningful limits upon the method such that the invention does not preempt every observance of the natural phenomenon itself.
The claims are also directed at another judicial exception, the following abstract ideas, namely mental processes: “comparing the concentration of progerin in the sample with a progerin-related aging pathology-positive control” (claim 1), “comparing the pre-treatment concentration of progerin with the post-treatment concentration of progerin” (claim 9), and “comparing the concentration of progerin in the sample with a progerin-related aging pathology-positive control” (claim 16). “Comparing” is an abstract idea, namely a mental process that could be performed in a practitioner’s head, or with a practitioner with pen and paper.
Eligibility Step 1:
Claims 1-14 and 16-18 are directed to methods comprising measuring progerin to assess the status of a patient with HGPS. Methods are one of the eligible statutory categories for invention (STEP 1: YES). However, eligibility of the claims is not self-evident, and therefore analysis must proceed to Step 2.
Eligibility Step 2A, Prong One:
The natural relationships to which the claims are directed (i.e. the relation between the level of the biomarker progerin and progerin-related aging pathology) are laws of nature.
Eligibility Step 2A, Prong Two:
According to Step 2A, Prong Two, set forth in MPEP 2106.04 II A (2), the claims are next evaluated with respect to whether the judicial exception is integrated into a practical application. This analysis turns to the additional steps/elements recited within the claims. In independent claim 16, the additional steps are “if the subject has the pathology, administering to the subject a treatment for the pathology that lowers progerin concentration”.
Regarding the additional steps cited in claim 16, the “treatment for progerin-related aging pathology” is recited at a high level of generality and is not tied, for example to any particular treatment. The treatment or prophylaxis limitation must be “particular,” i.e., specifically identified so that it does not encompass all applications of the judicial exception(s). See MPEP 2106.04(d)(2).
Regarding claims 1-14 and 16-18, providing samples/controls and quantitating biomarker levels using methods with specific limits of quantitation are insufficient to integrate the judicial exception because the purpose is merely to obtain data. This does not go beyond insignificant presolution activity, i.e., a mere data gathering step necessary to use the correlation
There are no additional elements that reflect an actual improvement within the technical field. For example, there are no additional elements that apply the natural correlation/phenomena judicial exception to a particular treatment or which utilize a particular machine; there are no additional elements that effect a transformation; and, there are no additional elements that apply the judicial exception in some other meaningful way beyond generally linking it to a field, namely, progerin-related aging. In this way the claims, as drafted, do not integrate the judicial exception into a practical application that would overcome monopolizing the exception. (STEP 2A, Prong Two: NO).
Eligibility Step 2B:
Lastly, there are no additional elements of claims 1-14 and 16-18.
Therefore, the steps/elements recited in addition to the judicial exception do not add significantly more (STEP 2B: NO).
The claimed steps/elements recited in addition to the judicial exception, alone or in combination, do not make an inventive contribution over the methods that were known in the art prior to filing, and they amount to mere observation of the natural phenomenon itself, by any means known, with the words “apply it” in order to append it to the field of progerin-related aging pathology.
For all of these reasons, the claimed subject matter is ineligible under 35 U.S.C. 101 because the claims are directed to a natural phenomenon judicial exception without significantly more.
However, it is noted that claims 15, 19 and 20 do integrate the judicial exception into a practical application by tying the quantitation of progerin in a sample from a subject to treatment with a particular treatment, farnesyl transferase inhibitors.
Claim Rejections - 35 USC § 102
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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
1. Claims 1, 2 and 4 are rejected under 35 U.S.C. 102(a)(1) as being anticipate
McClintock et al. teaches a method for prognosis of Hutchinson-Gilford progeria syndrome (a progerin-related aging pathology) in a subject, comprising:
providing a sample from a subject;
quantitating the concentration of progerin in in the sample with a quantitative
immunoassay, wherein the quantitative immunoassay detects progerin but does not detect
wildtype lamin A protein; and
comparing the concentration of progerin in the sample with an HGPS-positive
control, wherein a concentration of progerin in the sample that is below the concentration
of progerin in the HGPS-positive control indicates an increased life expectancy in the subject (see, e.g., sample from a subject – p. 1, under “Abstract”: “Screening 150 skin biopsies”; quantitating the concentration of progerin in in the sample with a quantitative immunoassay, wherein the assay does not detect wildtype lamin A protein– p. 3, col. 1, para. 2: “The serum of rabbit 972 specifically recognized progerin protein and gave no signal with A-type lamin including pre-lamin A”, and p. 2, under “Figure 1.”, panel “C”, and p. 5, under “Figure 3.”; comparing the concentration of progerin in the sample with an HGPS-positive control – p. 2, under “Figure 1.”). The applicant’s specification identifies immunofluorescent histochemistry as an immunoassay that can be used with methods (see, p. 9, lines 21-23).
I.) As noted above, McClintock et al. teaches all the elements of claim 1.
Therefore, McClintock et al. anticipates claim 1.
II.) Regarding applicant’s claim 2, as noted above McClintock et al, anticipates claim 1 from which claim 2 depends.
Claim 2 recites that the sample is a liquid sample selected from plasma, serum, urine, cell extract, and saliva.
McClintock et al. teaches analyzing progerin in cells. (Introduction)
Therefore, McClintock et al. anticipates claim 2.
III.) Regarding applicant’s claim 4, as noted above McClintock et al, anticipates claim 1 from which claim 4 depends.
Claim 4 recites that the control is from the same subject at an earlier time point.
McClintock et al. teaches that the control is from the same subject at an earlier time point, as in claim 4 (see, e.g., p. 4, col. 1, para. 1: “fibroblast culture DR118 established from an 86 year-old female was monitored by indirect immunofluorescence with anti-progerin mAb and exhibited an average of 0.4% of progerin-positive cells in young cultures. That average increased to 0.8% in late cultures (PPDs 30 to 35)”).
Therefore, McClintock et al. anticipates claim 4.
2. Claims 9-11 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Cao et al. (“Rapamycin Reverses Cellular Phenotypes and Enhances Mutant Protein Clearance in Hutchinson-Gilford Progeria Syndrome Cells”, Science Translational Medicine, 29 June 2011 Vol 3 Issue 89).
Cao et al. teaches a method for determining the efficacy of a treatment for Hutchinson-Gilford progeria syndrome (a progerin-related aging pathology), comprising:
providing a pre-treatment sample from a subject, that is taken prior to
administration of a treatment for HGPS;
determining the concentration of progerin in the pre-treatment sample with a
quantitative immunoassay, wherein the quantitative immunoassay detects progerin but
does not detect wildtype lamin A protein;
providing a post-treatment sample from the subject, that is taken during or after
administration of a treatment for HGPS;
determining the concentration of progerin in the post-treatment sample with the
quantitative immunoassay; and
comparing the pre-treatment concentration of progerin with the post-treatment
concentration of progerin, wherein a significant decrease in progerin concentration in the
post-treatment sample indicates that the treatment is effective (see, e.g., p. 3, col. 1, para. 1: “we generated a custom antibody against progerin using a peptide located at the cryptic splicing junction as an antigen (anti-progerin). This antibody specifically recognized progerin, but not lamin A or C in Western (immuno) blotting and immunofluorescence analyses (fig. S4). When normalized with a β-actin control, quantification of protein by Western blot revealed a ~50% reduction in progerin amounts in rapamycin-treated HGPS cells on day 60 of treatment relative to mock-treated cells”, and p. 4, under “Fig. 2.”, panels “A.” and “B.”).
I.) As noted above, Cao et al. teaches all the limitations of claim 9.
Therefore, Cao et al. anticipates claim 9.
II.) Regarding applicant’s claim 10, as noted above Cao et al. anticipates claim 9 from which claim 10 depends.
Claim 10 recites that pre-treatment sample and the post treatment sample are a liquid sample selected from plasma, serum, cell extract, urine, and saliva.
Cao et al. teaches analyzing progerin in cells. (Title)
Therefore, Cao et al. anticipates claim 10.
III.) Regarding applicant’s claim 11, as noted above Cao et al. anticipates claim 10 from which claim 11 depends.
Claim 11 recites providing one or more additional post-treatment samples that are taken from the subject at time points subsequent to the initial post-treatment sample, and wherein a continued or further decrease in progerin concentration indicates continued efficacy of the treatment.
Cao et al. teaches providing one or more additional post-treatment samples that are taken from the subject at time points subsequent to the initial post-treatment sample, and wherein a continued or further decrease in progerin concentration indicates continued efficacy of the treatment (see, e.g., p. 6, under “Fig. 4.”, panel “A.”).
Therefore, Cao et al. anticipates claim 11.
Claim Rejections - 35 USC § 103
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.
3. Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over McClintock et al. as applied to claims 1 and 4 above, and further in view of Todd et al. (“Ultrasensitive Flow-based Immunoassays Using Single-Molecule Counting”, Clinical Chemistry 53, No.11, 2007).
I.) Regarding applicant’s claim 3, as noted above McClintock et al. anticipates claim 1 from which claim 3 depends.
Claim 3 recites that the quantitative immunoassay comprises:
contacting the sample with a capture antibody that binds to both wildtype lamin A
and progerin, resulting in a mixture of captured lamin A and captured progerin;
separating the mixture of captured lamin A and captured progerin from the
sample;
contacting the mixture of captured lamin A and captured progerin with a progerin specific detection antibody comprising a detectable label, thereby binding the captured
progerin but not the captured lamin A with the detection antibody;
separating the detectable label from the mixture with captured lamin A; and
detecting the detectable label, and thereby quantitating the amount of progerin in
the sample.
McClintock et al. does not teach that the quantitative immunoassay comprises:
contacting the sample with a capture antibody that binds to both wildtype lamin A
and progerin, resulting in a mixture of captured lamin A and captured progerin;
separating the mixture of captured lamin A and captured progerin from the
sample;
contacting the mixture of captured lamin A and captured progerin with a progerin specific detection antibody comprising a detectable label, thereby binding the captured
progerin but not the captured lamin A with the detection antibody;
separating the detectable label from the mixture with captured lamin A; and
detecting the detectable label, and thereby quantitating the amount of progerin in
the sample.
Todd et al. teaches an assay method wherein the quantitative immunoassay comprises:
contacting the sample with a capture antibody that binds to the target;
separating the mixture of target from the sample;
contacting the mixture of target with a specific detection antibody comprising a detectable label, thereby binding the captured target with the detection antibody;
separating the detectable label from the mixture; and
detecting the detectable label, and thereby quantitating the amount of target in
the sample, as in claim 3 (see, e.g., p. 1991, col. 1, under “ERRENA IAs”: “Samples or calibrators (in volumes of 50–100 L) were diluted with assay buffer containing capture antibody-coated MPs (e.g., in 150 L) and incubated in a 96-well plate for 1–2 h at 25 °C with shaking. All plasma or serum samples were tested undiluted without pretreatment. MPs were separated using a magnetic bed (Ambion). Supernatant was removed, MPs were washed once, and then 20 L detection antibody (50–500 mg/L diluted in assay buffer) was added and incubated for 60 min at 25 °C with shaking. The MPs were again magnetically separated and washed 6 times using Tris-buffered saline with 0.5 mL Triton X-100/L. After removal of residual wash buffer, 20 L elution buffer (4 mol/L urea) was added. This reagent disrupted antibody–analyte interactions and resulted in the release of detection antibody from the MPs. The solution in each 96-well plate was then transferred to a 384-well filter plate (0.2 m, AcroPrep cat. no. 5070, Pall) and centrifuged at 1200g for 3 min to separate detection antibody in elution buffer from MPs. The eluted and filtered material in the 384-well plate was then placed into the Erenna Immunoassay System”).
McClintock et al. and Todd et al. are analogous to the field of the claimed invention because they are both in the field of immunoassays for scarce proteins.
It would have been obvious to one of ordinary skill in the art before applicant’s effective filing date to use the quantitative immunoassay of Todd et al. in the methods of McClintock et al. An artisan would have been motivated to do so because Todd et al. discloses, “the Erenna Immunoassay System builds single-molecule detection combined with MP IA technology to provide highly sensitive IAs. This system also provides a broad dynamic reporting range and flexible sample volume requirements. The flexibility of sample volume may allow determination of multiple quantifications from a small sample or to conserve samples” (see, Todd et al., p. 1994, col. 2, para. 4). An artisan would have had a reasonable expectation of success based on the given disclosures.
4. Claims 7 and 8 are rejected under 35 U.S.C. 103 as being unpatentable over McClintock et al. as applied to claims 1 and 4 above, and further in view of Cao et al. and Gordon et al. (“Association of Lonafarnib Treatment vs No Treatment With Mortality Rate in Patients With Hutchinson-Gilford Progeria Syndrome”, American Medical Association 2018).
I.) Regarding applicant’s claim 7, as noted above McClintock et al. anticipates claim 1 from which claim 7 depends.
Claim 7 recites repeating the method one or more times after the subject undergoes a treatment for HGPS, wherein a decrease in progerin concentration following the treatment indicates a positive prognosis.
McClintock et al does not teach repeating the method one or more times after the subject undergoes a treatment for HGPS, wherein a decrease in progerin concentration following the treatment indicates a positive prognosis.
Cao et al. teaches repeating the measurement of progerin after treatment for HGPS, wherein the decrease in progerin following treatment is 50%, as in claims 7-9 (see, e.g., p. 3, col. 1, para. 1: “we generated a custom antibody against progerin using a peptide located at the cryptic splicing junction as an antigen (anti-progerin). This antibody specifically recognized progerin, but not lamin A or C in Western (immuno) blotting and immunofluorescence analyses (fig. S4). When normalized with a β-actin control, quantification of protein by Western blot revealed a ~50% reduction in progerin amounts in rapamycin-treated HGPS cells on day 60 of treatment relative to mock-treated cells”, and p. 4, under “Fig. 2.”, panels “A.” and “B.”, and p. 1, under abstract: “Our findings suggest an additional mechanism for the beneficial effects of rapamycin on longevity and encourage the hypothesis that rapamycin treatment could provide clinical benefit for children with HGPS”).
Furthermore, Gordon et al. teaches increased life expectancy following treatment of HGPS, as in claims 7-9 (see, e.g., p. 1687, under “CONCLUSIONS AND RELEVANCE”: “Among patients with HGPS, lonafarnib monotherapy, compared with no treatment, was associated with a lower mortality rate after 2.2 years of follow-up”).
McClintock et al., Cao et al., and Gordon et al. are analogous to the field of the claimed invention because they are all in the field of HGPS.
It would have been obvious to one of ordinary skill in the art before applicant’s effective filing date to repeat the measurements of McClintock et al. after treatment because Cao et al. discloses that progerin decreases after HGPS treatment and increases longevity (see, Cao et al., p. 1, under abstract: “Our findings suggest an additional mechanism for the beneficial effects of rapamycin on longevity and encourage the hypothesis that rapamycin treatment could provide clinical benefit for children with HGPS”) and Gordon et al. discloses, “Among patients with HGPS, lonafarnib monotherapy, compared with no treatment, was associated with a lower mortality rate after 2.2 years of follow-up” (see, Gordon et al., p. 1687, under “CONCLUSIONS AND RELEVANCE”). An artisan would have had a reasonable expectation of success based on the given disclosures.
Therefore, McClintock et al. in view of Cao et al. and Gordon et al. renders claim 7 obvious.
II.) Regarding applicant’s claim 8, as noted above McClintock et al. in view of Cao et al. and Gordon et al. renders claim 7 obvious from which claim 8 depends.
Claim 8 recites that a greater decrease in progerin concentration indicates a greater increase in life expectancy.
As noted above, Gordon et al. discloses, “Among patients with HGPS, lonafarnib monotherapy, compared with no treatment, was associated with a lower mortality rate after 2.2 years of follow-up” (see, Gordon et al., p. 1687, under “CONCLUSIONS AND RELEVANCE”). An artisan would have had a reasonable expectation of success based on the given disclosures.
Therefore, McClintock et al. in view of Cao et al. and Gordon et al. renders claim 8 obvious.
5. Claim 12 is rejected under 35 U.S.C. 103 as being unpatentable over Cao et al. as applied to claim 10 above, and further in view of Todd et al.
Claim 12 recites contacting the sample with a capture antibody that binds to both wildtype lamin A and progerin, resulting in a mixture of captured lamin A and captured progerin; separating the mixture of captured lamin A and captured progerin from the sample; contacting the mixture of captured lamin A and captured progerin with a progerin-specific detection antibody comprising a detectable label, thereby binding captured progerin but not captured lamin A with the detection antibody; separating the detectable label from the mixture with captured lamin A; detecting the detectable label, and thereby quantitating the amount of progerin in the sample.
Cao et al. does not teach contacting the sample with a capture antibody that binds to both wildtype lamin A and progerin, resulting in a mixture of captured lamin A and captured progerin; separating the mixture of captured lamin A and captured progerin from the sample; contacting the mixture of captured lamin A and captured progerin with a progerin-specific detection antibody comprising a detectable label, thereby binding captured progerin but not captured lamin A with the detection antibody; separating the detectable label from the mixture with captured lamin A; detecting the detectable label, and thereby quantitating the amount of progerin in the sample.
Todd et al. teaches an assay method wherein the quantitative immunoassay comprises:
contacting the sample with a capture antibody that binds to the target;
separating the mixture of target from the sample;
contacting the mixture of target with a specific detection antibody comprising a detectable label, thereby binding the captured target with the detection antibody;
separating the detectable label from the mixture; and
detecting the detectable label, and thereby quantitating the amount of target in
the sample, as in claim 13 (see, e.g., p. 1991, col. 1, under “ERRENA IAs”: “Samples or calibrators (in volumes of 50–100 L) were diluted with assay buffer containing capture antibody-coated MPs (e.g., in 150 L) and incubated in a 96-well plate for 1–2 h at 25 °C with shaking. All plasma or serum samples were tested undiluted without pretreatment. MPs were separated using a magnetic bed (Ambion). Supernatant was removed, MPs were washed once, and then 20 L detection antibody (50–500 mg/L diluted in assay buffer) was added and incubated for 60 min at 25 °C with shaking. The MPs were again magnetically separated and washed 6 times using Tris-buffered saline with 0.5 mL Triton X-100/L. After removal of residual wash buffer, 20 L elution buffer (4 mol/L urea) was added. This reagent disrupted antibody–analyte interactions and resulted in the release of detection antibody from the MPs. The solution in each 96-well plate was then transferred to a 384-well filter plate (0.2 m, AcroPrep cat. no. 5070, Pall) and centrifuged at 1200g for 3 min to separate detection antibody in elution buffer from MPs. The eluted and filtered material in the 384-well plate was then placed into the Erenna Immunoassay System”).
Cao et al. and Todd et al. are analogous to the field of the claimed invention because they are both in the field of immunoassays for scarce proteins.
It would have been obvious to one of ordinary skill in the art before applicant’s effective filing date to use the quantitative immunoassay of Todd et al. in the methods of Cao et al. An artisan would have been motivated to do so because Todd et al. discloses, “the Erenna Immunoassay System builds single-molecule detection combined with MP IA technology to provide highly sensitive IAs. This system also provides a broad dynamic reporting range and flexible sample volume requirements. The flexibility of sample volume may allow determination of multiple quantifications from a small sample or to conserve samples” (see, Todd et al., p. 1994, col. 2, para. 4). An artisan would have had a reasonable expectation of success based on the given disclosures.
6. Claims 15 is rejected under 35 U.S.C. 103 as being unpatentable over Cao et al. as applied to claim 10 above, and further in view of Gordon et al.
I.) Regarding applicant’s claim 15, as noted above Cao et al. anticipates claim 10 from which claim 15 depends.
Claim 15 recites that the treatment comprises a farnesyl transferase inhibitor.
Cao et al. does not teach that the treatment comprises a farnesyl transferase inhibitor.
Gordon et al. teaches treating HGPS patients with lonafarnib monotherapy, as in claims 16-17 (see, e.g., p. 1687, under “CONCLUSIONS AND RELEVANCE”: “Among patients with HGPS, lonafarnib monotherapy, compared with no treatment, was associated with a lower mortality rate after 2.2 years of follow-up”).
Cao et al. and Gordon et al. are analogous to the field of the claimed invention because they are both in the field of HGPS.
It would have been obvious to one of ordinary skill in the art before applicant’s effective filing date to use the treatment of Gordon et al. in the method of Cao et al. An artisan would have been motivated to do so because Gordon et al. teaches “Among patients with HGPS, lonafarnib monotherapy, compared with no treatment, was associated with a lower mortality rate after 2.2 years of follow-up” (see, p. 1687, under “CONCLUSIONS AND RELEVANCE”). An artisan would have understood the benefit of lonafarnib treatment, mainly the lower mortality rate. An artisan would have had a reasonable expectation of success based on the given disclosures.
7. Claims 16, 19 and 20 are rejected under 35 U.S.C. 103 as being unpatentable over McClintock et al. in view of Gordon et al.
As noted above, McClintock et al. teaches as set forth above, including providing a sample from a subject;
quantitating the concentration of progerin in in the sample with a quantitative
immunoassay, wherein the quantitative immunoassay detects progerin but does not detect
wildtype lamin A protein;
comparing the concentration of progerin in the sample with an HGPS-positive
control, wherein if the concentration of progerin in the sample indicates that the subject
has HGPS, as in claim 18 (see, e.g., sample from a subject – p. 1, under “Abstract”: “Screening 150 skin biopsies”; quantitating the concentration of progerin in in the sample with a quantitative immunoassay, wherein the assay does not detect wildtype lamin A protein– p. 3, col. 1, para. 2: “The serum of rabbit 972 specifically recognized progerin protein and gave no signal with A-type lamin including pre-lamin A”, and p. 2, under “Figure 1.”, panel “C”, and p. 5, under “Figure 3.”; comparing the concentration of progerin in the sample with an HGPS-positive control – p. 2, under “Figure 1.”). The applicant’s specification identifies immunofluorescent histochemistry as an immunoassay that can be used with methods (see, p. 9, lines 21-23).
McClintock et al. does not teach a method for treatment of Hutchinson-Gilford progeria syndrome (HGPS) in a subject, comprising:
if the subject has HGPS, administering to the subject a treatment for HGPS that
lowers progerin concentration.
McClintock et al. also fails to teach the treatment comprises a farnesyl transferase inhibitor, specifically lonafarnib.
Gordon et al. teaches treating HGPS patients with lonafarnib monotherapy, (see, e.g., p. 1687, under “CONCLUSIONS AND RELEVANCE”: “Among patients with HGPS, lonafarnib monotherapy, compared with no treatment, was associated with a lower mortality rate after 2.2 years of follow-up”).
McClintock et al. and Gordon et al. are analogous to the field of the claimed invention because they are both in the field of HGPS.
It would have been obvious to one of ordinary skill in the art before applicant’s effective filing date to use the treatment of Gordon et al. in the method of McClintock et al. An artisan would have been motivated to do so because Gordon et al. teaches “Among patients with HGPS, lonafarnib monotherapy, compared with no treatment, was associated with a lower mortality rate after 2.2 years of follow-up” (see, p. 1687, under “CONCLUSIONS AND RELEVANCE”). An artisan would have understood the benefit of lonafarnib treatment, mainly the lower mortality rate. An artisan would have had a reasonable expectation of success based on the given disclosures.
Therefore, McClintock et al. in view of Gordon et al. renders claim 16 obvious.
II.) Regarding applicant’s claim 19, as noted above McClintock et al. in view of Gordon et al. renders claim 16 obvious from which claim 19 depends.
Claim 19 recites that the treatment for the pathology comprises administering a farnesyl transferase inhibitor to the subject.
Gordon et al. teaches lonafarnib as noted in the title.
Therefore, McClintock et al. in view of Gordon et al. renders claim 19 obvious.
III.) Regarding applicant’s claim 20, as noted above McClintock et al. in view of Gordon et al. renders claim 19 obvious from which claim 20 depends.
Claim 20 recites that the farnesyl transferase inhibitor is lonafarnib.
Gordon et al. teaches lonafarnib as noted in the title.
Therefore, McClintock et al. in view of Gordon et al. renders claim 20 obvious.
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.
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Claims 1, 3-9, and 11-20 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-10, 12-22 of U.S. Patent Application No. 18/723,433 (hereafter referred to as ‘433).
Although the claims at issue are not identical, they are not patentably distinct from each other because the only difference is that a progerin-related aging pathology is substituted with “HGPS” in ‘433. HGPS is a dominant progerin-related aging pathology. The name for the protein progerin comes from the Hutchinson-Gilford progeria syndrome.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claims are allowed.
While claims 5, 6, 13, 14, 17 and 18 are free of the prior art, the claims are rejected under 35 U.S.C. 101, and for non-statutory double patenting.
While McClintock et al., Cao et al. and Gordon et al. teach as set forth above, they all fail to teach the lower limit of quantitation of the quantitative immunoassay is 59 pg/ml and the upper limit of quantitation of the quantitative immunoassay is 30,000 pg/ml, as in claims 5, 6, 13, 14, 17 and 18.
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/MICHAEL STANLEY GZYBOWSKI/Examiner, Art Unit 1798
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