DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. 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 for the cited rejections 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.
3. Response to Election/Restriction filed on 4/26/2026 is acknowledged.
4. Claim filed on 10/30/2023 is acknowledged.
5. Claims 1-18 are pending in this application.
6. Claims 7-18 are withdrawn from consideration pursuant to 37 CFR 1.142(b), as being drawn to non-elected inventions, there being no allowable generic or linking claim.
7. Claims 1-6 are under examination.
Election/Restrictions
8. Applicant’s election without traverse of Group 1 (claims 1-6) and election of SEQ ID NO: 1 as species of cargo molecule transduction domain; EGFP-RMAD1 fusion protein (RMAD1 fused to the C-terminus of EGFP) as species of recombinant cargo molecule (for inventions 2 and 4); polynucleotide of SEQ ID NO: 12 as species of genetic construct (for invention 3); and pET28a vector comprising the genetic construct encoding EGFP-RMAD1 as species of expression vector (for invention 3) in the reply filed on 4/26/2026 is acknowledged. The requirement is made FINAL in this office action.
Please note: In view of Applicant’s election without traverse of Group 1, EGFP-RMAD1 fusion protein (RMAD1 fused to the C-terminus of EGFP) as the elected species of recombinant cargo molecule (for inventions 2 and 4); polynucleotide of SEQ ID NO: 12 as the elected species of genetic construct (for invention 3); and pET28a vector comprising the genetic construct encoding EGFP-RMAD1 as the elected species of expression vector (for invention 3) would not be searched and examined in the current office action.
Group 1 is drawn to a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, the cargo molecule transduction domain comprising: 1) a RMAD1 peptide consisting of SEQ ID NO: 1 derived from human ADARB2; or 2) a RMAD1 variant peptide consisting of 8 to 50 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide. A search was conducted on the elected species; and SEQ ID NO: 1 as the elected species of cargo molecule transduction domain appears to be free of prior art. A search was extended to the genus in claim 1; and prior art was found. Claims 1-6 are examined on the merits in this office action.
Claim Interpretations
9. With regards to the cargo molecule transduction domain recited in instant claims 1 and 6, in view of the RMAD1 variant can be any peptide/protein that is at least 8 amino acids in length, for the purpose of this examination, the Examiner is interpretating the recited cargo molecule transduction domain broadly includes any peptide/protein that is at least 8 amino acids in length.
With regards to the limitations recited in instant claims 2-5, the Examiner is interpreting instant claims 2-5 include all the limitations of instant claim 1 with further limitation of the RMAD1 variant recited in instant claim 1. Therefore, as an example, instant claim 2 is interpretated as the followings: A cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, the cargo molecule transduction domain comprising: 1) a RMAD1 peptide consisting of SEQ ID NO: 1 derived from human ADARB2; or 2) a RMAD1 variant peptide consisting of 8 to 50 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide, and wherein the amino acid substitution in the RMVAD1 variant peptide is a conservative amino acid substitution.
With regards to the limitation “in the form of a dimer or higher-order multimer” recited in instant claim 6, for the purpose of this examination, the Examiner is interpretating the term “higher-order multimer” means any multimer with more than two copies of the recited peptides.
Such interpretations apply to all the rejections set forth below.
Objections
10. The specification is objected to for containing/referring to sequences without also identifying them by the sequence identifier assigned to them in the sequence listing as required by 37 CFR 1.821(d). The specification discloses the amino acid sequence CKSKRRRRRRSKRKD on page 2, paragraph [9] of instant specification. However, it is missing the respective sequence identifier. Applicant is required to amend the specification to comply with 37 CFR 1.821(d).
11. The specification is objected to for the following minor informality: The specification recites “6R of 5 to 10 > substituted with” on page 27, Table 1 of instant specification. This appears to be a typo in this recitation. Applicant is required to correct this error.
Please note: The specification has not been checked to the extent necessary to determine the presence of all possible error. Applicant's cooperation is required in correcting any errors of which applicant may become aware in the specification (see MPEP § 608.01).
12. The drawings are objected to for the following minor informality:
Figures 2A and 2B: The legend of Y-axis is missing.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
13. Claim 1 is objected to for the following minor informality: Claim 1 contains the acronym “ADARB2”. An acronym in the first instance of claims should be expanded upon/spelled out with the acronym indicated in parentheses, for example, double-stranded RNA-specific editase B2 (ADARB2). The abbreviation can be used thereafter.
Furthermore, Applicant is suggested to amend claim 1 as “A cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, wherein the cargo molecule transduction domain comprises: 1) a RMAD1 peptide consisting of SEQ ID NO: 1 derived from human double-stranded RNA-specific editase B2 (ADARB2); or 2) a RMAD1 variant peptide…”.
14. Claim 2 is objected to for the following minor informality: Applicant is suggested to amend claim 2 as “…wherein the amino acid substitution of the RMAD1 peptide is conservative amino acid substitution”.
15. Claim 3 is objected to for the following minor informality: Applicant is suggested to amend claim 3 as “The cargo molecule transduction domain of claim 1, wherein the RMAD1 variant peptide is a sequence in which a lysine residue of SEQ ID NO: 1 is independently substituted with an arginine residue and/or an arginine residue of SEQ ID NO: 1 is independently substituted with a lysine residue”.
16. Claim 4 is objected to for the following minor informality: Applicant is suggested to amend claim 4 as “…wherein the RMAD1 variant peptide is a sequence in which one to six lysine residues and arginine residues of SEQ ID NO: 1 are deleted”.
17. Claim 5 is objected to for the following minor informality: Applicant is suggested to amend claim 5 as “…wherein the RMAD1 variant peptide is a sequence in which at least one amino acid is deleted or added to SEQ ID NO: 1”.
18. Claim 6 is objected to for the following minor informality: Applicant is suggested to amend claim 6 as “The cargo molecule transduction domain of claim 1, wherein the cargo molecule transduction domain is in the form of multimer”.
Rejections
Claim Rejections - 35 U.S.C. § 101
19. 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.
20. Claims 1-6 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. Claims 1-6 are directed to a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, the cargo molecule transduction domain comprising: 1) a RMAD1 peptide consisting of SEQ ID NO: 1 derived from human ADARB2; or 2) a RMAD1 variant peptide consisting of 8 to 50 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide.
As evidenced by instant specification, the RMAD1 peptide consisting of instant SEQ ID NO: 1 is a fragment of the naturally occurring protein human ADARB2 (see pages 2-3, paragraph [9] of instant specification). Therefore, human ADARB2 protein (comprising a RMAD1 peptide consisting of instant SEQ ID NO: 1) meets all the structural limitations of the cargo molecule transduction domain recited in instant claims 1-5.
Furthermore, as evidenced by Verly et al (Sci. Rep., 2017, 7, pages 1-13), the naturally occurring homodimeric antibiotic peptide homotarsinin is a dimer of peptide consisting of the amino acid sequence NLVSDIIGSKKHMEKLISIIKKCR-NH2 (a RMAD1 variant consisting of 24 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide of instant SEQ ID NO: 1), for example, the paragraph bridging pages 1-2. In comparison to the RMAD1 peptide of SEQ ID NO: 1 consisting of the amino acid sequence CKSKRRRRRRSKRKD, the amino acid sequence NLVSDIIGSKKHMEKLISIIKKCR-NH2 is a variant that has a conservative substitution such as Arg at position 5 of instant SEQ ID NO: 1 is substituted with Lys (a conservative substitution recited in instant claim 2). Therefore, the homodimeric antibiotic peptide homotarsinin in Verly et al meets all the structural limitations of the cargo molecule transduction domain recited in instant claims 1, 2 and 6.
And since the human ADARB2 protein and/or the homodimeric antibiotic peptide homotarsinin meets all the structural limitations of the cargo molecule transduction domain recited in instant claim 1, the human ADARB2 protein and/or the homodimeric antibiotic peptide homotarsinin would inherently have the same properties and functionality of the peptide recited in instant claim 1. Therefore, the human ADARB2 protein and/or the homodimeric antibiotic peptide homotarsinin is a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues. And the MPEP states: “Products of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990) (see MPEP § 2112.01 II). Since the USPTO lacks the experimental facilities to make a further determination, the burden is on the Applicant to prove the otherwise.
The claims 1-6 do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the claimed cargo molecule transduction domain in instant claims 1-6 does not recite features or steps demonstrating a marked difference from what exists in nature; and the claimed cargo molecule transduction domain in instant claims 1-6 does not recite meaningful limitations that add something of significance to the judicial exception. Therefore, the claimed cargo molecule transduction domain in instant claims 1-6 is not significantly different than a judicial exception (natural product).
Claim Rejections - 35 U.S.C. § 112 paragraph (b)
21. 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.
22. Claim 4 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 pre-AIA the applicant regards as the invention.
23. Claim 4 recite “The cargo molecule transduction domain of claim 1, wherein, in a peptide sequence in which one or more amino acids are deleted from the RMAD1 variant peptide, one to six lysine residues and arginine residues among the amino acids of the RMAD1 peptide are deleted”. It is unclear what the recited “in a peptide sequence in which one or more amino acids are deleted from the RMAD1 variant peptide, one to six lysine residues and arginine residues among the amino acids of the RMAD1 peptide are deleted” is, in that whether the recitation means in addition to one to six lysine residues and arginine residues of the RMAD1 peptide are deleted, one or more amino acids are deleted from the RMAD1 variant peptide as well or not. Therefore, the metes and bounds of instant claim 4 is vague and indefinite.
Furthermore, in view of the disclosure of instant specification, the Examiner is interpretating claim 4 as “The cargo molecule transduction domain of claim 1, wherein the RMAD1 variant peptide is a sequence in which one to six lysine residues and arginine residues of SEQ ID NO: 1 are deleted”. Therefore, claim 4 would not be rejected under 35 U.S.C. 112(d) or 35 U.S.C. 112 (pre-AIA ), 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim Rejections - 35 U.S.C. § 112 paragraph (a)
Written Description
24. The following is a quotation 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 35 U.S.C. 112 (pre-AIA ), first paragraph:
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.
25. Claims 1-6 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.
The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient” (MPEP § 2163).
A claimed genus may be satisfied through sufficient description of a representative number of species or disclosure of relevant, identifying characteristics such as functional characteristics coupled with a known or disclosed correlation between function and structure (MPEP § 2163(3)a(II)). The number of species that describe the genus must be adequate to describe the entire genus; if there is substantial variability, a large number of species must be described.
The analysis for adequate written description considers (a) actual reduction to practice, (b) disclosure of drawings or structural chemical formulas, (c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure, and (d) representative number of samples.
In the instant case, claims 1-6 recite a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, the cargo molecule transduction domain comprising: 1) a RMAD1 peptide consisting of SEQ ID NO: 1 derived from human ADARB2; or 2) a RMAD1 variant peptide consisting of 8 to 50 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide. Claims 2-5 further limit the RMAD1 variant peptide; and claim 6 limits the cargo molecule transduction domain to be in the form of a multimer.
The genus of instant claimed peptide is extremely broad, including any peptide/protein that is at least 8 amino acids in length.
The instant specification discloses that RMAD1 peptide of instant SEQ ID NO: 1 as a cargo molecule transduction domain; and peptides of instant SEQ ID NOs: 2-11 as variants of RMAD1 peptide of instant SEQ ID NO: 1.
The issue at question is whether a person of ordinary skilled in the art would be able to determine what structural feature/amino acid sequence is required for the instant claimed peptide to have the functional characteristics of being a cargo molecule transduction domain or not.
(a) actual reduction to practice and (b) disclosure of drawings or structural chemical formulas:
In the instant case, the instant specification discloses that RMAD1 peptide of instant SEQ ID NO: 1 as a cargo molecule transduction domain; and peptides of instant SEQ ID NOs: 2-11 as variants of RMAD1 peptide of instant SEQ ID NO: 1.
Furthermore, peptides of instant SEQ ID NOs: 1-3 and 5-11 are tested in the working examples in instant specification.
Taken all these together, other than the limited examples, the instant specification fails to disclose the effect of either altering the amino acid sequence or the length of the RMAD1 peptide of instant SEQ ID NO: 1 on the functional characteristics of being a cargo molecule transduction domain. The instant specification does not describe a general correlation between structure and function for the claimed genus of peptide comprising any one amino acid sequence that is at least 8 amino acids in length to be a cargo molecule transduction domain.
(c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure:
As discussed above, in the instant case, based on the disclosure of instant specification, other than the limited examples, a person of ordinary skilled in the art would not be able to determine the effect of either altering the amino acid sequence or the length of the RMAD1 peptide of instant SEQ ID NO: 1 on the functional characteristics of being a cargo molecule transduction domain.
With regards to the instant claimed peptide being a cargo molecule transduction domain, Du et al (J. Peptide Res., 1998, 51, pages 235-243) teach peptide r-SA2 with the amino acid sequence NYKKPKLAAAPALLALLVAPLLAVAA, for example, page 236, Figure 1. The peptide r-SA2 in Du et al is a variant of the RMAD1 peptide of instant SEQ ID NO: 1. However, it is not a cargo molecule transduction domain (see page 240, Figure 4A; and Section “Other topological requirements for cell-permeable peptide functions”).
Furthermore, it is well known in the peptide/protein art that even single amino acid changes or differences in the amino acid sequence of a protein can have dramatic effects on the protein’s function. As an example of the unpredictable effects of mutations on protein function, Drumm et al (Annu. Rev. Pathol. Mech. Dis., 2012, 7, pages 267-282) teach cystic fibrosis is an autosomal recessive disorder caused by mutations in the CFTR (cystic fibrosis transmembrane conductance regulator) gene, for example, page 268, Section “CYSTIC FIBROSIS”. Drumm et al further teach several mutations can cause cystic fibrosis, including two mutations G551D and G551S; and clinical consequences are quite different for these two changes, as the G551D variant has virtually no detectable activity, and consequently a classic, severe phenotype is associated; G551S, however, has reduced but clearly detectable function and is associated with a much milder presentation of CF, for example page 269, left column, the last paragraph. Drumm et al also teach that in the most common cystic fibrosis mutation ΔF508 (the absence of amino acid 508 of the normally 1,480-amino acid protein) gives rise to the cystic fibrosis phenotype, for example, page 268, right column, the 2nd paragraph. Thus, even the substitution or deletion of a single amino acid can have dramatic and unpredictable effects on the function of the protein. The unpredictability of the effect of amino acid substitution on the function and/or property of peptide/protein is further confirmed and discussed in Yampolsky et al (Genetics, 2005, 170, pages 1459-1472). Yampolsky et al teach even conservative substitution can significantly affect the function of the protein/peptide, for example, page 1465, Table 3. Although the disclosures of Drumm et al and Yampolsky et al are directed to proteins/peptides other than cargo molecule transduction domain, they illustrate the inherent unpredictability with respect to the biological activity of a given protein/peptide after even minor changes to the primary amino acid sequence.
Therefore, based on the state of art, a person of ordinary skilled in the art would not be able to determine the effect of either altering the amino acid sequence or the length of the RMAD1 peptide of instant SEQ ID NO: 1 on the functional characteristics of being a cargo molecule transduction domain.
(d) representative number of samples:
In the instant case, the genus of instant claimed peptide is extremely broad, including any peptide/protein that is at least 8 amino acids in length.
And, as discussed in (a) and (b) above, the instant specification discloses that RMAD1 peptide of instant SEQ ID NO: 1 as a cargo molecule transduction domain; and peptides of instant SEQ ID NOs: 2-11 as variants of RMAD1 peptide of instant SEQ ID NO: 1.
Furthermore, peptides of instant SEQ ID NOs: 1-3 and 5-11 are tested in the working examples in instant specification.
Considering the broadness of the genus of instant claimed peptide, the instant specification fails to provide sufficient examples to describe the entire genus of peptide that is at least 8 amino acids in length to be a cargo molecule transduction domain claimed.
Taken all these together, considering the state of the art and the disclosure in instant specification, it is deemed that the instant specification fails to provide adequate written description for the claimed genus of peptide that is at least 8 amino acids in length being a cargo molecule transduction domain; and does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention.
Claim Rejections - 35 U.S.C. § 102(a)(1)
26. 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.
27. Claims 1, 2 and 6 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Verly et al (Sci. Rep., 2017, 7, pages 1-13).
The instant claims 1, 2 and 6 are drawn to a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, the cargo molecule transduction domain comprising: 1) a RMAD1 peptide consisting of SEQ ID NO: 1 derived from human ADARB2; or 2) a RMAD1 variant peptide consisting of 8 to 50 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide.
Verly et al, throughout the literature, teach a homodimeric antibiotic peptide homotarsinin, which is a dimer of the peptide consisting of the amino acid sequence NLVSDIIGSKKHMEKLISIIKKCR-NH2 (a RMAD1 variant consisting of 24 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide of instant SEQ ID NO: 1), for example, the paragraph bridging pages 1-2. In comparison to the RMAD1 peptide of instant SEQ ID NO: 1 consisting of the amino acid sequence CKSKRRRRRRSKRKD, the amino acid sequence NLVSDIIGSKKHMEKLISII KKCR-NH2 is a variant that has a conservative substitution such as Arg at position 5 of instant SEQ ID NO: 1 is substituted with Lys (as recited in instant claim 2). Therefore, the homodimeric antibiotic peptide homotarsinin in Verly et al meets all the structural limitations of the cargo molecule transduction domain recited in instant claims 1, 2 and 6.
With regards to the limitation “a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues” recited in instant claim 1, since the homodimeric antibiotic peptide homotarsinin in Verly et al meets all the structural limitations of the cargo molecule transduction domain recited in instant claim 1, the homodimeric antibiotic peptide homotarsinin in Verly et al would inherently have the same properties and functionality of the peptide recited in instant claim 1. Therefore, the homodimeric antibiotic peptide homotarsinin in Verly et al is a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues. And the MPEP states: “Products of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990) (see MPEP § 2112.01 II). Since the USPTO lacks the experimental facilities to make a further determination, the burden is on the Applicant to prove the otherwise.
Since the reference teaches all the limitations of instant claims 1, 2 and 6; the reference anticipates instant claims 1, 2 and 6.
28. Claims 1-5 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Tang et al (WO 01/57188 A2).
The instant claims 1-5 are drawn to a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, the cargo molecule transduction domain comprising: 1) a RMAD1 peptide consisting of SEQ ID NO: 1 derived from human ADARB2; or 2) a RMAD1 variant peptide consisting of 8 to 50 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide.
Tang et al teach peptide of SEQ ID NO: 2641, which is 154 amino acids in length and consists of the amino acid sequence RTIRETERRSALSCSVLKSEPLPGLQPQASQ QRRRRLPGRRQVQVQEGGGSGLRAWVLAMASVLGSGRGSGGLSSQLKCKSKRRRRRRSKRKDKVSILSTFLAPFKHLSPGITNTEDDDTLSTSSAEVKENRNVGNLAARPPPSGDRARGGATR (comprising the amino acid sequence of instant SEQ ID NO: 1, underlined), for example, page 322, SEQ ID NO: 2641. It meets all the structural limitations of the cargo molecule transduction domain recited in instant claims 1-5.
With regards to the limitation “a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues” recited in instant claim 1, since the peptide of SEQ ID NO: 2641 in Tang et al meets all the structural limitations of the cargo molecule transduction domain recited in instant claim 1, the peptide of SEQ ID NO: 2641 in Tang et al would inherently have the same properties and functionality of the peptide recited in instant claim 1. Therefore, the peptide of SEQ ID NO: 2641 in Tang et al is a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues. And the MPEP states: “Products of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990) (see MPEP § 2112.01 II). Since the USPTO lacks the experimental facilities to make a further determination, the burden is on the Applicant to prove the otherwise.
Furthermore, the MPEP states the following: “A genus does not always anticipate a claim to a species within the genus. However, when the species is clearly named, the species claim is anticipated no matter how many other species are additionally named. See Ex parte A, 17 USPQ2d 1716 (Bd. Pat. App. & Inter. 1990)” (see MPEP § 2131.02).
Since the reference teaches all the limitations of instant claims 1-5; the reference anticipates instant claims 1-5.
Obviousness Double Patenting
29. 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 claims at issue 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); and 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 a nonstatutory double patenting ground provided the reference application or patent either is shown to be commonly owned with this application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO internet Web site contains terminal disclaimer forms which may be used. Please visit http://www.uspto.gov/forms/. The filing date of the application will determine what form should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to http://www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
30. Claims 1, 2 and 6 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-11, 14, 15, 18, and 19 of co-pending application No. 18/290570.
31. Instant claims 1, 2 and 6 are drawn to a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, the cargo molecule transduction domain comprising: 1) a RMAD1 peptide consisting of SEQ ID NO: 1 derived from human ADARB2; or 2) a RMAD1 variant peptide consisting of 8 to 50 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide.
32. Claims 1-11, 14, 15, 18, and 19 of co-pending application No. 18/290570 are drawn to a cargo molecule transduction domain that has cell-penetrating ability and binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, the cargo molecule transduction domain comprising: 1) a RMMR1 peptide consisting of SEQ ID NO: 1 derived from human MRPL15; or 2) a RMMR1 variant peptide consisting of 5 to 50 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMMR1 peptide; recombinant cargo molecule comprising such cargo molecule transduction domain; pharmaceutical composition and/or cosmetics comprising such recombinant cargo molecule; and method of using such cargo molecule transduction domain.
The RMMR1 peptide of SEQ ID NO: 1 in claims of co-pending application No. 18/290570 consists of the amino acid sequence ERRPRGRRRGRKC, which is a RMAD1 variant recited in instant claims 1 and 2. And a multimer of the RMMR1 peptide of SEQ ID NO: 1 in claim 11 of co-pending application No. 18/290570 meets the limitations of instant claim 6.
This is a provisional obviousness-type double patenting rejections because the conflicting claims have not in fact been patented.
33. Claims 1 and 2 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-3 and 8-19 of co-pending application No. 18/266540.
34. Instant claims 1 and 2 are drawn to a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues, the cargo molecule transduction domain comprising: 1) a RMAD1 peptide consisting of SEQ ID NO: 1 derived from human ADARB2; or 2) a RMAD1 variant peptide consisting of 8 to 50 amino acids in which one or more amino acids are deleted, substituted, and/or added to the RMAD1 peptide.
35. Claims 1-3 and 8-19 of co-pending application No. 18/266540 are drawn to a peptide consisting of the amino acid sequence of SEQ ID NO: 2 or an amino acid sequence showing 95% or more sequence homology thereto; a vaccine comprising such peptide; a pharmaceutical composition comprising such peptide; and methods of using such peptide.
The peptide of SEQ ID NO: 2 or 3 in claims of co-pending application No. 18/266540 is a RMAD1 variant recited in instant claims 1 and 2, which meets all the structural limitations of the cargo molecule transduction domain recited in instant claims 1 and 2.
With regards to the limitation “a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues” recited in instant claim 1, since the peptide of SEQ ID NO: 2 or 3 in claims of co-pending application No. 18/266540 meets all the structural limitations of the cargo molecule transduction domain recited in instant claim 1, the peptide of SEQ ID NO: 2 or 3 in claims of co-pending application No. 18/266540 would inherently have the same properties and functionality of the peptide recited in instant claim 1. Therefore, the peptide of SEQ ID NO: 2 or 3 in claims of co-pending application No. 18/266540 is a cargo molecule transduction domain that binds to cargo molecules and transports the cargo molecules into mammalian cells or tissues. And the MPEP states: “Products of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990) (see § MPEP 2112.01 II). Since the USPTO lacks the experimental facilities to make a further determination, the burden is on the Applicant to prove the otherwise.
This is a provisional obviousness-type double patenting rejections because the conflicting claims have not in fact been patented.
36. For the same/similar reasoning/rational as the rejection set forth in Sections 33-35 above, instant claims 1 and 2 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-19 of co-pending Application No. 18/290572; claims 1-15 of co-pending Application No. 18/867016; and claims 16-19 and 24-35 of co-pending Application No. 18/873183.
These are all provisional obviousness-type double patenting rejections because the conflicting claims have not in fact been patented.
Conclusion
No claim is allowed.
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/LI N KOMATSU/Primary Examiner, Art Unit 1658
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