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 .
Status of the claims
The amendment filed 08/21/25 is acknowledged and has been entered. Claims 1, 4, 6, 22 and 24 have been amended. Claims 2-3, 5, 9-11, 13-15, 18-19 and 26 were previously canceled. Accordingly, claims 1, 4, 6-8, 12, 16-17, 20-25 and 27-29 are under examination.
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, 4, 6-8, 12, 16-17 and 20-21 are rejected under 35 U.S.C. 101 because the claimed invention is directed to abstract ideas and/or to laws of nature/natural phenomena without significantly more.
The U.S. Patent and Trademark Office recently revised the MPEP with regard to § 101 (see the MPEP at 2106). Regarding the MPEP at 2106, in determining what concept the claim is “directed to,” we first look to whether the claim recites:
(1) any judicial exceptions, including certain groupings of abstract ideas (i.e., mathematical concepts, certain methods of organizing human activity such as a fundamental economic practice, or mental processes); and
(2) additional elements that integrate the judicial exception into a practical application (see MPEP § 2106.05(a)-(c), (e)-(h)).
Only if a claim (1) recites a judicial exception and (2) does not integrate that exception into a practical application, do we then look to whether the claim contains an “‘inventive concept’ sufficient to ‘transform’” the claimed judicial exception into a patent-eligible application of the judicial exception. Alice, 573 U.S. at 221 (quoting Mayo, 566 U.S. at 82). In so doing, we thus consider whether the claim:
(3) adds a specific limitation beyond the judicial exception that is not “well-understood, routine, conventional” in the field (see MPEP § 2106.05(d)); or
(4) simply appends well-understood, routine, conventional activities previously known to the industry, specified at a high level of generality, to the judicial exception.
See MPEP 2106.
ELIGIBILITY STEP 2A: WHETHER A CLAIM IS DIRECTED TO A JUDICIAL EXCEPTION
Step 2A, Prong 1
The claims are directed to a naturally occurring correlation between the presence of PLIN1 autoantibodies in a subject having autoimmune-related lipodystrophy.
Step 2A, Prong 2
The additional elements of contacting a sample with a peptide that comprises 24 consecutive amino acids that are at least 90% identical to 24 consecutive amino acids of any one of SEQ ID NOS: 2 to 6 and detecting antibodies in the sample that bind to the peptide does not apply, rely on, or use the judicial exception in a manner that imposes a meaningful limit on the judicial exception.
Also, with respect to the recitations “wherein detecting such antibodies in the sample in step (c) constitutes evidence that the subject is experiencing or is at risk of developing the autoimmune-related lipodystrophy” and “wherein detecting such antibodies in the sample in step (c) is diagnostic for autoimmune-related lipodystrophy”. The “wherein” statements at best articulates the judicial exception, amounting only to a general instruction to apply or use the judicial exception. This could read on mental activity being performed solely in a practitioner’ head, e.g. A mental appreciation of the presence of autoantibodies bound to the peptide being correlated with autoimmune related lipodystrophy. No active method steps are invoked or clearly required; the “wherein” statements do not include any activity that would constitute a practical application, i.e. steps that apply, rely on or use the natural principle in a manner such that the claims amount to significantly more that the natural principal itself.
ELIGIBILITY STEP 2B: WHETHER THE ADDITIONAL ELEMENTS CONTRIBUTE AN "INVENTIVE CONCEPT"
Further, the additional elements of the claims are recited with a high level of generality and do not apply, rely on, or use the judicial exception in a manner that imposes a meaningful limit on the judicial exception. (the active method steps/limitations recited in addition to the judicial exceptions themselves) and do not add significantly more to the judicial exception(s).
As shown by Corvillo et al (Frontiers Immunology, Vol 9, Article 2142, September 2018, pages 1-13) (submitted in the IDS filed 07/13/23) it is well known routine and conventional in the art to obtain a sample from a subject and to contact the sample with a peptide that comprises 24 consecutive amino acids that are at least 90% identical to 24 consecutive amino acids of any one of SEQ ID NOS: 2 to 6 (e.g. page 4).
It does not appear to be the case that the active steps recited, which are performed in order to gather the data or perform the assay, are steps recited or performed in an unconventional or non-routine way, such to provide an inventive concept under step 2B.
The claimed limitations as currently presented fail to recite limitations that add a feature that is more than well understood, conventional or routine in the field of diagnostics and biochemical assay methodologies.
For all of these reasons, the claims fail to include additional elements that are sufficient to either integrate the judicial exception(s) into practical application(s) thereof, or amount to significantly more than the judicial exception(s).
Claim Rejections - 35 USC § 112
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.
Written Description
Claims 1, 6-8, 12, 16-17, 20-25 and 27-29 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 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claims 1, 22 and 24 are directed to contacting the sample with a peptide that comprises 24 consecutive amino acids that are at least 90% identical to 24 consecutive amino acids of any one of SEQ ID NO:s 2 to 6.
Claims 1, 22 and 24 as a whole therefore encompasses a genus of polypeptides and peptides for detecting the presence of antibodies associated with lipodystrophy. Thus, the peptides are defined by reference to a desired functional characteristic, namely the capacity to bind to an antibody associated with lipodystrophy.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus.
Although the recitation “24 consecutive amino acids that are at least 90 % identity to 24 consecutive amino acids..” may appear somewhat limited, however, the number of amino acid sequences comprising a deletion, substitution and/or addition of is actually enormous. The specification does not disclose any and all 24 consecutive amino acids, or provide an example of any and all possible consecutive amino acids. For example, current SEQ ID NO:2 is 49 amino acid residues in length, and the claimed genus includes changes at any given position in the sequence as long as there are 24 consecutive amino acids, there is no disclosure of a precise epitope or precise consecutive amino acids that must be retained in order to achieve binding (e.g. to still bind and detect the presence of “antibodies associated with autoimmune-related lipodystrophy.
Thus, the genera encompassed by the claims are of large size and substantial variability. As a result, the number of species meeting the structural requirements of the claim is exceedingly large and characterized by substantial variability; in that any polypeptide having 90% identity be encompassed. As stated above the number of amino acid sequences comprising a deletion, substitution and/or addition of is actually enormous and also allows a diverse number of amino acids added to, deleted or substituted in any combination. It is not apparent that the identities of all such species could be determined even with the aid of a computer.
Furthermore, only those sequences meeting the structural and functional requirements of the genus are encompassed by the claim. Therefore, the claims encompass all of the sequences meeting the structural requirements that are also able to bind to an autoantibody. In this case, however, it cannot be envisioned based on the specification what sequences would possess such binding properties.
Comparing the claim scope with the scope of the description, it is noted that the specification as filed discloses on page 4 discloses polypeptides comprising SEQ IS NO.’s 1-6. Page 37 discloses 5 fragments which have the unique capability of binding to PLIN1 autoantibodies associated with lipodystropy. As shown in Table 1 these fragments are fragments 1-2, 11 and 4-5 which consist of SEQ ID NO.’s 2-6, all of which have 49 amino acids. Thus, the specification is disclosing that fragments 3 and 6-10 did not possess this unique capability. As shown by the Affidavit submitted by Mark S. Anderson on 08/25/26 The entire 522 amino acid sequence of PLIN1 (SEQ ID NO: 1) was surveyed by using fragments that were 49 amino acids in length, overlapping each other by 24 amino acids: specifically, SEQ ID NOS 2 to 23 (para 0069) (see page 2 of the declaration). Mark Anderson on page 4 of the declaration indicates that if five amino acids in a 49-amino acid peptide are mutated, the reactivity will remain, because most of the clones will bind specifically to a sub-epitope in the target peptide. Anderson further states that “peptides that are 90% identical to immunogenic fragments of PLIN1 will almost always capture enough autoantibodies in the patient’s polyclonal response to give a positive test. Thus, the specification and the declaration are showing that 49 amino acids are minimal. Although the fragments that were 49 amino acids in length, may have 24 amino acids that are overlapping each other. The specification does not disclose any and all consecutive 24 amino acids or provide what the 24 amino acids are or any additions, mutations etc that may occur and still provide the essential function of binding to the recited antibodies. While the specification and the Affidavit provide support for the written description of a “peptide that comprises at least 49 consecutive amino acids that are at least 90% identical to any one of SEQ ID NOS: 2 to 6 (such as recited in claims 4), does not provide support for any and all 24 consecutive amino acids as currently recited (e.g. claims 1, 22 and 24).
It was known in the prior art that small changes in antigen structure profoundly affect antibody-antigen interactions. Harlow & Lane (Harlow, E. and Lane, D., Antibodies: A Laboratory Manual (1988) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pages 23-26) discuss how even small changes in antigen structure can profoundly affect the strength of an antibody-antigen interaction. See entire selection, in particular page 26, first full paragraph. In particular, the loss of a single hydrogen bond can reduce the strength of interaction by 1000-fold (ibid).
Many other researchers have reported similar findings to those of Harlow & Lane. For example, Lederman et al. ("A single amino acid substitution in a common African allele of the CD4 molecule ablates binding of the monoclonal antibody, OKT4" Mol Immunol. 1991 Nov;28(11):1171-81) found that a single amino acid substitution on the antigen CD4 ablated binding of a monoclonal antibody (see title and abstract). Similarly, Colman et al. (Research in Immunology, 1994; 145(1): 33-36) teach that amino acid changes in an antigen can effectively abolish antibody antigen binding entirely (see entire document, particularly pages 33-34).
As noted above, the variability among the peptides encompassed by the claims is also enormous; and would encompass changes much more substantial than the loss of a single hydrogen bond or the mutation of a single amino acid; yet even such minor changes as these were known to dramatically affect function.
Given the unpredictability associated with making even minor changes to antigen structure while preserving function, with limited exception it is not possible to predict which, out of the enormous number of peptides encompassed by the claims, would be capable of binding to an immunoglobulin and/or an immunoglobulin complex.
For all of these reasons, the skilled artisan would not reasonably conclude that the inventor(s), at the time the application was filed, had possession of the full scope of the claimed invention.
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.
Claims 1, 4, 6-8, 12, 16-17 and 20-21 are 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.
Claim 1, lines 9-10 the recitation “constitutes evidence that the subject is experiencing or is at risk for developing auto-immune-related lipodystrophy.” Causes confusion because the sentence ends with a period and then is followed up by reciting “wherein detecting such antibodies in the sample in step (c) is diagnostic for autoimmune-related lipodystrophy”. This causes confusion as to if the method comprises both the constitution of evidence that subject is experiencing or is at risk for developing autoimmune-related lipodystrophy and is diagnostic for autoimmune-related lipodystrophy or if the applicant intends that only one of the scenarios is achieved. Also. by the recitation ending in a period and then starting the next sentence with a lower case “wherein” adds to the confusion as to if the applicant intended the sentence to end or not. Please clarify.
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.
Claims 1, 4, 6, 8, 12, 16-17 and 20 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Corvillo et al (Frontiers in Immunology, Vol 9, Article 2142, Sept. 2018, pages 1-13) (submitted in the IDS filed 07/13/23).
Corvillo et al discloses detecting autoimmune-related acquired generalized liposystrophy comprising collecting serum or plasma samples from a subject (e.g. pg 2) and contacting the sample with a recombinant PLIN1 and detecting binding of autoantibodies to the recombinant PLIN1) (e.g. pg 4). Corvillo et al discloses the detection is by ELISA (e.g. pg 4). Corvillo et al discloses that the subject can have an autoimmune disease such as dermatomyositis (e.g. page 1). Corvillo et al discloses that patients with detecting autoimmune-related acquired generalized liposystrophy show the presence of the autoantibodies (e.g. abstract, pgs 6-8). Corvillo et al discloses the subject can show fat loss (e.g. page 2) (early sign of lipodyatrophy).
With respect the recitation “a peptide that comprises 24 consecutive amino acids are at least 90% identical to 24 consecutive amino acids of any one of SEQ ID NOS 2 to 6” as recited in claims 1, 22 and 24. The instantly recited claims are not limited to the recited sequences but utilizes open language in reciting “a peptide that comprises…” Thus, given its broadest reasonable interpretation any peptide or protein comprising the SEQ ID NO: 2 to 6 would have this peptide and would be 90% identical. Corvillo et al teaches the antigen can be recombinant PLIN1 (OriGene). As evidenced by OriGene product datasheet for TP306292L (pages 1-2, obtained 04/16/2025) the recombinant protein is a human recombinant protein which comprises SEQ ID NO: 3 which begins at the 49th amino acid discloses on the first page of the datasheet. Also, SEQ ID NO: 1 comprises SEQ ID: NO’s 2-6 and therefore it is deemed that the recombinant PLIN1 in the modified method of Corvillo et al reads on the open language of “comprising” and “that comprises” and therefore comprises 24 consecutive amino acids that are at least 90% identical to 24 consecutive amino acids of any one of SEQ ID NOS: 2 to 6. Thus, for the reasons stated above Corvillo reads on the instantly recited claims.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 7 and 21 are rejected under 35 U.S.C. 103 as being unpatentable over Corvillo et al in view of Jehl et al (Diabetes Care, Vol 42, October 2019, pages 2008-2010).
See above for the teachings of Corvillo et al.
Corvillo et al differs from the instant invention in failing to teach the subject has history of treatment with an immune checkpoint inhibitor therapy.
Jehl et al teaches that it is known and conventional in the art that patients receiving nivolumab (checkpoint inhibitor) is associated with acquired generalized lipodystrophy (e.g. abstract, pgs 2008, 2010). Jehl et al discloses the subject has cancer and insulin resistance (e.g. page 1)
It would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to incorporate subjects that have been treated with a checkpoint inhibitor such as taught by Jehl et al because Jehl et al shows that patients receiving a checkpoint inhibitor have a correlation with generalized lipodystrophy. Thus, one of ordinary skill in the art would have a reasonable expectation of success incorporating subject receiving a checkpoint inhibitor such as taught by Jehl into the method of Corvillo et al.
Claims 22-25 are 27-29 are rejected under 35 U.S.C. 103 as being unpatentable over Corvillo et al in view of Bolan et al (The Journal of Clinical Endocrinology & Metabolism, 87 (1), pages 380-384, 2002).
See above for the teachings of Corvillo et al.
Corvillo et al differs from the instant invention in failing to teach administering an immunosuppressive therapy to the subject.
Bolan et al teaches that it is known and conventional to administer plasma exchange (immunosuppressive therapy) to subjects having acquired generalized lipoatrophy (lipodystrophy) and teaches that provides for dramatic improvement in the subject (e.g. abstract, pgs 382-384).
It would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to incorporate plasma exchange therapy such as taught by Bolan et al for the subject in the modified method of Corvillo et al because Bolan et al shows that it is known and conventional in the art and provides for dramatic improvement of the subject. Thus, one of ordinary skill in the art would have a reasonable expectation of success incorporating plasma exchange therapy such as taught by Bolan et al for the subject in the modified method of Corvillo et al.
Response to Arguments
Applicant's arguments filed 08/21/26 and the Affidavit by Mark S. Anderson filed 08/25/26 have been fully considered but they are not persuasive.
101 Rejections:
Applicant argues that the use of target peptides identical or at least 90% identical to SEQ ID NOS:2 to 6 improves the diagnostic power of the assay, because the presence of antibodies specific for any one of SEQ ID NOS:2 to 6 is more predictive of lipodystrophy. This constitutes an inventive concept.
The argument is not found persuasive because claim itself does not reflect the disclosed improvement in the technology. The current claim does not provide a step of medical intervention which applies the judicial exception in a manner which adds more to the claim. The current claims are not acting or using a practical application but are coming up with information of the naturally occurring correlation between the presence of PLIN1 autoantibodies in a subject having autoimmune-related lipodystrophy. The claims do not have a step of using this presence in a manner that imposes a meaningful limit. Thus, the current steps are not acting on or using the judicial exception in a practical application and that the steps are merely coming up with information but not applying that information with medical intervention.
112 (a) Written Description:
Applicant argues that the claimed subject matter in the patents at issue in Amgen is different the situation here in two ways: (1) it is not a particular monoclonal antibody being claimed here - it is the target peptide being used to test for the presence of an autoantibody; (2) the autoantibody present in a patient's serum against PLIN1 is inevitably polyclonal, not monoclonal. A modest degree of variation in the target peptide will not change the effectiveness of the peptide in capturing antibodies from a polyclonal response.
Dr. Anderson explains it this way in his declaration: "Rather than just a single antibody molecule with a single antigen combining site, the patient makes a pool of different antibodies, each with its own antigen binding site with its own specificity. For a protein as large as PLIN1, the patient will react against several different epitopes in the autoantigen for each epitope, there will be dozens or hundreds of different antibody clones in a patient's immune response that will each bind to the same epitope in a different way."
Dr. Anderson concludes that a variation of five amino acids in a peptide that is 49 amino acids in length is unlikely to render the peptide completely unable to capture any of the antibody clones in the response. Peptides that are 90% identical to immunogenic fragments of PLIN1 will almost always capture at least enough autoantibodies in the patent's polyclonal response to give a positive test result.
The office is respectfully reminded that there is no requirement that all of the species within a claimed genus be equally effective - only that species that are effective be adequately represented in the disclosure, with other species being identifiable without undue experimentation.
For reasons stated previously and herein, there is a substantial latitude of sequence variation in SEQ ID NO:2 to 6 that would be effective in detecting antibodies that are diagnostic of lipodystrophy in the claimed assay method. SEQ. ID NOs:2 to 6 used in the working examples are representative of the genus of 90% identical peptides being claimed. Variants falling within the genus can readily be assessed for efficacy using the assay systems provided in the disclosure.
These arguments and the Declaration of Dr. Anderson have been fully considered and are not found persuasive and are insufficient for the following reasons: (1) the instant written description is not limited to Amgen and in fact never mentions Amgen and thus the argument is not on point. Further, even though Amgen may be directed to a monoclonal antibody and the instant rejection is based on a peptide, Amgen would be relevant because both are directed to binding molecules that have capability of binding specifically to desired antigen/antibody of interest. Also, as pointed out by the Applicant Amgen is concerned with enablement issues which are completely different than written description issues. (2) While the argument and Declaration are sufficient for providing support for a peptide that comprises at least 49 consecutive amino acids that are at least 90% identical to any one of SEQ ID NOS: 2 to 6 as recited in claim 4 does not provide support for any and all peptides that comprises 24 consecutive amino acids that are at least 90% identical to 24 consecutive amino acids of any one of SEQ ID NO:s 2 to 6. As shown by the Affidavit submitted by Mark S. Anderson on 08/25/26 The entire 522 amino acid sequence of PLIN1 (SEQ ID NO: 1) was surveyed by using fragments that were 49 amino acids in length, overlapping each other by 24 amino acids: specifically, SEQ ID NOS 2 to 23 (para 0069) (see page 2 of the declaration). Mark Anderson on page 4 of the declaration indicates that if five amino acids in a 49-amino acid peptide are mutated, the reactivity will remain, because most of the clones will bind specifically to a sub-epitope in the target peptide. Anderson further states that “peptides that are 90% identical to immunogenic fragments of PLIN1 will almost always capture enough autoantibodies in the patient’s polyclonal response to give a positive test. Thus, the specification and the declaration are showing that 49 amino acids are minimal. Although the fragments that were 49 amino acids in length, may have 24 amino acids that are overlapping each other. The specification does not disclose any and all consecutive 24 amino acids or provide what the 24 amino acids are or any additions, mutations etc that may occur and still provide the essential function of binding to the recited antibodies. While the specification and the Affidavit provide support for the written description of a “peptide that comprises at least 49 consecutive amino acids that are at least 90% identical to any one of SEQ ID NOS: 2 to 6 (such as recited in claims 4), does not provide support for any and all 24 consecutive amino acids as currently recited (e.g. claims 1, 22 and 24).
102 Rejections:
Applicant argues that Corvillo does not teach or suggest using PLIN1 autoantibodies as a diagnostic aid. The article is focused entirely on the underlying causes of the condition. The title of the article is: Autoantibodies Against Perilipin 1 as a Cause of Acquired Generalized Lipodystrophy. The abstract concludes:
These autoantibodies altered the ability of perilipin to regulate lipolysis in cultured preadipocytes causing abnormal, significantly elevate basal lipolysis. Our data provide strong support for the conclusion that perilipin 1 autoantibodies are a cause of generalized lipodystrophy in these patients.
This argument is not found persuasive because the abstract also specifically discloses that anti-adipocyte antibodies have been previously reported in patients with acquired generalized lipodystrophy (AGL) and that their approach identified IgG autoantibodies in the serum of patients with AGL. Further, Corvillo discloses that the finding of anti-PLIN1 autoantibodies in patients with AGL sheds light on the pathophysiology of the disease, provides a target for its difficult diagnosis and opens the possibility for novel therapeutic strategies (e.g. page 11). Further, one would recognize that a subject with AGL having these antibodies is at risk of developing the disease or has the disease.
Applicant argues that he claims refer specifically to detecting antibodies that bind to peptides at least 90% identical to one of SEQ ID NOS:2 to 6. As shown in the working examples, use of these selected peptides improves the diagnostic utility of the test, and are superior to other fragments of PLIN1. None of the references teach or suggest the value and effectiveness of focusing on these five particular peptides.
This argument is not found persuasive because (1) the instant claims are not limited to the five particular peptides as argued but the claim used comprising language and allows for the full length PLIN1 (SEQ ID NO:1) which would comprises these peptides and the claim also allows for any and all peptides that comprises 24 consecutive amino acids that are at least 90% identical to 24 consecutive amino acids of any one of SEQ ID NOS:2 to 6; (2) Corvillo et al teaches the same peptides and antibodies as currently recited correlated with the same disease as currently recited and therefore the peptides of Corvillo et al would provide diagnostic utility and superiority as argued.
Applicant argues that he claimed invention is an important advance in the art that fills a long-felt need. Rebuttal evidence against an obviousness rejection may include evidence of "secondary considerations," such as "commercial success, long felt but unsolved needs, [and] failure of others." Graham V. John Deere Co., 383 U.S. 1, 148 USPQ 4459, 467, cited in MPEP § 2145 3.
Applicant states that Dr. Anderson explains in his declaration that before this invention was made, there was no blood marker or other definitive test to assess autoimmune related lipodystrophy in a patient. The diagnostic test described in this application enables the clinician to screen for the condition early in a patient's differential diagnosis, with virtually no false negatives.
This argument and the Declaration by Dr. Anderson have been fully considered but is not sufficient and not persuasive because applicant does not identify evidence to support that others in the art recognized a need to solve the specific problem (see Ex Parte Mathew Howard Myles, PTAB Appeal 2019-004771, at pp. 16-18 (Dec. 28, 2020). Also, as shown by Corvillo et al the use of the currently recited peptides for the detection of antibodies to these peptides in patients with lipodystrophy were known prior to this invention. Thus, the long-felt need was satisfied by another before the invention of the current application.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to GARY W COUNTS whose telephone number is (571)272-0817. The examiner can normally be reached M-F 7:00-4:00.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Gregory Emch can be reached at 571-272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/GARY COUNTS/ Primary Examiner, Art Unit 1678
Prosecution Insights