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 .
Election/Restrictions
Applicant's election with traverse of cell penetrating peptide in the reply filed on December 17th, 2025 is acknowledged. The traversal is on the grounds that the technical feature does make a contribution in view of Weiner et al. (US2019151443A1) because the SEQ ID NO:2 of Weiner is 183 residues [0082-0086] and the present SEQ ID NO:11 is 32 residues. This is not found persuasive because the broadest reasonable interpretation of the applicant’s technical feature does not limit the number of residues present in the cell-penetrating peptide. The applicant uses the transitional phrase “has a structure represented by.” The MPEP states “The transitional term "comprising", which is synonymous with "including," "containing," or "characterized by," is inclusive or open-ended and does not exclude additional, unrecited elements or method steps” [2111.03]. The term ‘represented by’ is synonymous to ‘characterized by’ and is therefore inclusive. Additionally, the applicant’s use of the term ‘has’ does not limit the scope of the claim. The MPEP recites that the present participle form of has, ‘having,’ must be interpreted in light of the specification to determine whether open or closed claim, language is intended [MPEP 2111.03]. The applicant does not define the terms ‘represented by’ and ‘has’ in any manner that would indicate an exclusive intention when reciting. Therefore, the broadest reasonable interpretation of the cell-penetrating peptide includes any composition comprising of the instant sequence, like the one taught by Weiner et al.
The requirement is still deemed proper and is therefore made FINAL.
The restriction requirement filed October 17th, 2025 has been modified to include an election of species. During a telephone conversation with Attorney Robert Ward on March 18th, 2026 a provisional election was made to prosecute the invention of the cell penetrating peptide, SEQ ID NO:28, claims 23-35. Affirmation of this election must be made by applicant in replying to this Office action. Claims 24-28 and 36-42 are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
REQUIREMENT FOR UNITY OF INVENTION
As provided in 37 CFR 1.475(a), a national stage application shall relate to one invention only or to a group of inventions so linked as to form a single general inventive concept (“requirement of unity of invention”). Where a group of inventions is claimed in a national stage application, the requirement of unity of invention shall be fulfilled only when there is a technical relationship among those inventions involving one or more of the same or corresponding special technical features. The expression “special technical features” shall mean those technical features that define a contribution which each of the claimed inventions, considered as a whole, makes over the prior art.
The determination whether a group of inventions is so linked as to form a single general inventive concept shall be made without regard to whether the inventions are claimed in separate claims or as alternatives within a single claim. See 37 CFR 1.475(e).
When Claims Are Directed to Multiple Categories of Inventions:
As provided in 37 CFR 1.475 (b), a national stage application containing claims to different categories of invention will be considered to have unity of invention if the claims are drawn only to one of the following combinations of categories:
(1) A product and a process specially adapted for the manufacture of said product; or
(2) A product and a process of use of said product; or
(3) A product, a process specially adapted for the manufacture of the said product, and a use of the said product; or
(4) A process and an apparatus or means specifically designed for carrying out the said process; or
(5) A product, a process specially adapted for the manufacture of the said product, and an apparatus or means specifically designed for carrying out the said process.
Otherwise, unity of invention might not be present. See 37 CFR 1.475 (c).
This application contains claims directed to more than one species of the generic invention. These species are deemed to lack unity of invention because they are not so linked as to form a single general inventive concept under PCT Rule 13.1.
The species are as follows: a cell-penetrating peptide
A complete election of species must have (1) the exact sequence of the cell-penetrating peptide or truncate without any variable residues defined by a SEQ ID NO (e.g. SEQ ID 10-38)
Applicant is required, in reply to this action, to elect a single species to which the claims shall be restricted if no generic claim is finally held to be allowable. The reply must also identify the claims readable on the elected species, including any claims subsequently added. An argument that a claim is allowable or that all claims are generic is considered non-responsive unless accompanied by an election.
Upon the allowance of a generic claim, applicant will be entitled to consideration of claims to additional species which are written in dependent form or otherwise require all the limitations of an allowed generic claim. Currently, the following claim(s) are generic 23
The groups of inventions listed above do not relate to a single general inventive concept under PCT Rule 13.1 because, under PCT Rule 13.2, they lack the same or corresponding special technical features for the following reasons:
The cell-penetrating peptides lack unity of invention because even though the inventions of these groups require the technical feature of Formula I, this technical feature is not a special technical feature as it does not make a contribution over the prior art in view of Weiner et al. (US2019151443A1: Published 2019).
Weiner teaches a hepatitis B viral core (HBV) protein used as part of a vaccine that transfects a cell in a mammalian host (Weiner, [126]). Weiner teaches that the HBV vaccine comprises a protein having the amino acid sequence of SEQ ID NO: 2 [claim 1]. SEQ ID NO: 2 comprises of SEQ ID NO: 11. Therefore, the common technical feature of the cell-penetrating peptide or truncate thereof of claim 23 does not constitute a special technical feature as it does not make a contribution over the prior art.
Nucleotide and/or Amino Acid Sequence Disclosures
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the specifications and claims are not identified by sequence identifiers in accordance with 37 CFR 1.821(d).
Formulas I-VII must have a corresponding SEQ ID Number.
Required response – Applicant must provide:
A substitute specification and claims in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers, consisting of:
A copy of the previously-submitted specifications and claims with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specifications and claims without markings (clean version); and
A statement that the substitute specifications and claims contain no new matter.
Claim Interpretation
The phrase “has a structure represented by’” is interpreted as open-ended, inclusive of any cell-penetrating peptide that comprises of the peptide or truncate defined by the claim. The MPEP states “the transitional term "comprising", which is synonymous with "including," "containing," or "characterized by," is inclusive or open-ended and does not exclude additional, unrecited elements or method steps” [2111.03]. The term ‘represented by’ is synonymous to ‘characterized by’ and is therefore inclusive. Additionally, the applicant’s use of the term ‘has’ does not limit the scope of the claim. The MPEP recites that the present participle form of has, ‘having,’ must be interpreted in light of the specification to determine whether open or closed claim, language is intended [MPEP 2111.03]. The applicant does not define the terms ‘represented by’ and ‘has’ in any manner that would indicate an exclusive intention when reciting. Therefore, claim 23 and its dependent claims are interpreted as a cell-penetrating peptide comprising of the formula used in the claim or the truncate defined by residues X11 to X26. If the applicant does not wish for the claim’s scope to be defined by open-ended language, they may remedy this by using exclusive language.
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.
Claim 29 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 29 includes the limitations of the claim it is dependent on, claim 23. Claim 23 states that compared to the cell-penetrating peptide, the truncate is truncated by 1-10 amino acid residues at the N-terminal resides and or truncated by 1-14 amino acids residues at the C-terminal. That means the broadest reasonable interpretation of the claimed sequence comprises a sequence of variable X11 to X26. As mentioned in to claim interpretation, since no exclusive language is used, the broadest reasonable interpretation of claim 29 is any cell-penetrating peptide comprising of the sequence from variable X-11 to X26- corresponding to SEQ ID NO 10-13, 15, 17-18, 20-21, 23-28, and 32-37. Presently, per the interpretion, SEQ ID NO:28 (elected species) lacks the written description requirement. The broadest reasonable embodiment of SEQ ID NO:28 is its truncate defined by claim 23 with a cell-penetrating peptide comprising the sequence SPRRRTPSPRRRRSQR. Inaptly, the residue corresponding to X-26 is R, is not supported by the variables listed in claim 23.
If the claim language of claim 23 is amended to be exclusive (e.g., utilizing the transitional phrase “consisting of”) which means that additional N- and C-terminal addition are excluded, claim 29 would still lack written description because . the last four residues (see in bold) of the full sequence of SEQ ID NO: 28 RRRGRSPRRRTPSPRRRRSQRREC are not supported by formula I in claim 23.Therefore, claim 29 lacks written description support from the claim it is dependent on, claim 23 because SEQ ID NO: 28 does not fall within Formula I. SEQ ID NOs: 10-13, 15, 17-18, 20-21, 23-27 and 32-37 do have written description support.
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.
Claim 29 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
The broadest reasonable embodiment of SEQ ID NO:28 in claim 29 is it is a truncate defined by claim 23 with a cell-penetrating peptide comprising the sequence SPRRRTPSPRRRRSQR. However, the residue corresponding to X-26 is R, is not supported by claim 23. Thereby, claim 29 is indefinite because the limitations of claim 23, the claim it is dependent from, do not apply. SEQ ID NO:28 cannot be distinctly claimed as a sequence derived from Formula I.
Claim Rejections - 35 USC § 101
Claims 23-33 are rejected under 35 U.S.C. 101 because the claimed composition is a product of nature without any markedly different characteristics from any naturally occurring counterparts:
Laws of nature and natural phenomena, as identified by the courts, include
naturally occurring principles/relations and nature-based products that are
naturally occurring or that do not have markedly different characteristics
compared to what occurs in nature. The courts have often described these
exceptions using other terms, including "physical phenomena," "scientific
principles", "natural laws," and "products of nature." [MPEP 2106.04(c)]
Regarding claim 23-29, claims 23-29 recite a cell-penetrating peptide that is able to perform transmembrane delivery. Such a peptides are a product of nature. See the analysis below
Step 1: Does the claim fall into a statutory category of invention?
Yes, the claim is directed to a composition of matter, which falls into a category of
invention.
Step 2A: Is the claim directed to a law of nature, a natural phenomenon
(product of nature) or an abstract idea?
Yes, the claims are directed to a product of nature because SEQ ID NOs 10-13 and 29, which read on the formulas of claims 23-29, can be derived from a core protein of the Hepatitis B virus (HBV) [Accession Number: V5JE82 · V5JE82_HBV]. SEQ ID NO:10 aligns with residues 2-35, SEQ ID NO:11 matches with residues 2-33, SEQ ID NO: 12 matches with residues 2-30, SEQ ID NO:13 matches with residues 2-28, and SEQ ID NO:29 matches with residues 7-35. SEQ ID NO:15, which also reads on the cell-penetrating peptides and truncates of claims 23-29, can also be derived from a core protein of the Hepatitis B virus (HBV) [Accession Number: V5JE87 · V5JE87_HBV]. SEQ ID NO:15 aligns with residues 2-37. Similarly, SEQ ID NO:17 can be derived from the capsid protein of the Hepatitis B virus (HBV) [Accession Number: L0CNB4 · L0CNB4_HBV], and aligns with residues 179 to 212. SEQ ID NO:20 can be derived from the external core antigen of the Horseshoe bat hepatitis B virus [Accession Number: U3M5R9· U3M5R9_9HEPA], and aligns with residues 178 to 217. SEQ ID NO:21 can be derived from the external core antigen of the Roundleaf bat hepatitis B virus [Accession Number: U3M5H3 · U3M5H3_9HEPA], and aligns with residues 178 to 217. SEQ ID NO:23 can be derived from the capsid protein of the Hepatitis B virus (HBV) [Accession Number: A0A1P7ZUM1 · A0A1P7ZUM1_HBV], and aligns with residues 150-183. SEQ ID NO:24 and 35 can be derived from the capsid protein of the Hepatitis B virus (HBV) [Accession Number: Q8AZ62 · Q8AZ62_HBV], and aligns with residues 150-181, and 155-181, respectively. SEQ ID NO:25 and 36 can be derived from the capsid protein of the Hepatitis B virus (HBV) [Accession Number: A0A0D3MP40 · A0A0D3MP40_HBV], and align with residues 150-178, and 155-178, respectively. SEQ ID NO:26 and 37 can be derived from a core protein of the Hepatitis B virus (HBV) [Accession Number: U5JHF0 · U5JHF0_HBV]. SEQ ID NO:26 aligns with residues 150-176 and SEQ ID: 37 aligns with 155-176.
Truncates of the previous sequences and following sequence, according to the parameters of independent claim 23, are also products of nature. Truncate of SEQ ID NO:27, residues of 1-20, align with a core protein of the Hepatitis B virus (HBV) [Accession Number: V5JE82 · V5JE82_HBV], residues 2-21.
Regarding claims 30 and 31, HBV proteins found in nature encompass a fusion protein comprising a cell-penetrating peptide covalently linked to a peptide of interest because the broadest reasonable interpretation of the peptide of interest encompasses the remaining sequence not defined by Formula I.
Regarding claims 32 and 33, HBV proteins found in nature can be interpreted as a conjugate comprising of a a cell-penetrating peptide covalently linked to a molecule of interest because the broadest reasonable interpretation of the molecule of interest encompasses the remaining sequence not defined by Formula I.
Regarding claims 34 and 35, the HBV protein self-assembled to form an icosahedral capsid with 240 copies of capsid protein [Information found L0CNB4 · L0CNB4_HBV}. Therefore, a multimer and a complex comprising of a multimer and a component (like a water molecule), exist in nature.
SEQ ID NO: 28 and 32-34 are not natural products because the sequences are not found naturally occurring in any proteins.
Step 2A Prong One: Does the claim recite an abstract idea, law of nature, or
natural phenomenon?
In the present case, the answer is yes because when a nature-based product is
derived from a naturally occurring thing, then the naturally occurring thing is the
counterpart. Section 2106.04 (b) recites:
When a law of nature or natural phenomenon is claimed as a physical product, the courts have often referred to the exception as a "product of nature". For example, the isolated DNA of Myriad and the primers of Ambry Genetics were described as products of nature by the courts. Ass’n for Molecular Pathology v. Myriad Genetics, Inc., 569 U.S. 576, 580, 106 USPQ2d 1972, 1975 (2013); University of Utah Research Foundation v. Ambry Genetics, 774 F.3d 755, 758-59, 113 USPQ2d 1241, 1243 (Fed. Cir. 2014). As explained in those decisions, products of nature are considered to be an exception because they tie up the use of naturally occurring things, but they have been labeled as both laws of nature and natural phenomena. See Myriad Genetics, Inc., 569 U.S. at 590- 91, 106 USPQ2d at 1979 (claims to isolated DNA held ineligible because they claim “naturally occurring phenomena" and are "squarely within the law of nature exception")
Step 2A Prong Two: Does the claim recite additional elements that integrate
the judicial exception into a practical application?
Because the markedly different characteristics analysis is based on comparing the
characteristics of the claimed nature-based product and its counterpart, the second step
in the analysis is used to identify appropriate characteristics to compare. Appropriate
characteristics must be possessed by the claimed product, because it is the claim that
must define the invention to be patented. In the present case, each component found in
nature is unmodified by a non-naturally occurring quality. For example, being able to perform transmembrane delivery is a naturally-occurring quality that a peptide derived from a virus has.
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 23-29 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Riedl et al. (Riedl, P., Reimann, J., & Schirmbeck, R. (2006). Complexes of DNA vaccines with cationic, antigenic peptides are potent, polyvalent CD8(+) T-cell-stimulating immunogens. Methods in molecular medicine, 127, 159–169.).
Regarding claims 23, 24 and 29, Riedl et al. discloses the peptide HBc150–183. Riedl et al. discloses this peptide is a cell-penetrating peptide. See [1.2]. The HBc150–183 peptide has the amino acid sequence RRRGRSPRRRTPSPRRRRSQSPRRRRSQSRES which is the same length and amino acid sequence as the claimed SEQ ID NO: 10, where X6 is R, X7 is R, X8 is R, X9 is G, X10 is R, X11 is S, X16 is T, X17 is P, X18 is S, X24 is S, X26 is S, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S of Formula I [Table 1].
Regarding claim 25, the cationic peptide HBc150–183, taught by Riedl et al, reads on a truncate of Formula II, where X6 is R, X7 is R, X8 is R, X9 is G, X11 is S, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S [Table 1].
Regarding claim 26, the cationic peptide HBc150–183, taught by Riedl et al, reads on a truncate of Formula III, where X6 is R, X7 is R, X8 is R, X9 is G, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S [Table 1].
Regarding claim 27, the cationic peptide HBc150–183, taught by Riedl et al, reads on a Formula I truncated by five residues from the N-terminus and three residues from C-terminus. X6 is R, X7 is R, X8 is R, X9 is G, X10 is R, X11 is S, X16 is T, X17 is P, X18 is S, X24 is S, X26 is S, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S [Table 1].
Regarding claim 28, the cationic peptide HBc150–183, taught by Riedl et al, comprises or consists of Formulas IV-VII, where X6 is R, X7 is R, X8 is R, X9 is G, X10 is R, X11 is S, X16 is T, X17 is P, X18 is S, X24 is S, X26 is S, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S [Table 1].
Claims 23-33 and 35 are also rejected under 35 U.S.C. 102(a)(1) as being anticipated by Chen et al (Chen HL, Su PY, Chang YS, Wu SY, Liao YD, et al. (2013) Identification of a Novel Antimicrobial Peptide from Human Hepatitis B Virus Core Protein Arginine-Rich Domain (ARD). PLOS Pathogens 9(6): e1003425).
Regarding claims 23—24 and 29, Chen et al. demonstrates that the HBc 147-183 peptide [Fig 1] can penetrate through the cell membrane [pg 11 pgh 5]. Therefore, a cell-penetrating membrane is anticipated because HBc 147-183 comprises of Formulas I- XII, where X6 is R, X7 is R, X8 is R, X9 is G, X10 is R, X11 is S, X16 is T, X17 is P, X18 is S, X24 is S, X26 is S, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S.
Regarding claim 25, the HBc 147-183 peptide reads on a truncate of Formula II, where X6 is R, X7 is R, X8 is R, X9 is G, X11 is S, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S [Table 1].
Regarding claim 26, the HBc 147-183 peptide reads on a truncate of Formula III, where X6 is R, X7 is R, X8 is R, X9 is G, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S [Table 1].
Regarding claim 27, the HBc 147-183 peptide, taught by Chen et al, reads on a Formula I truncated by five residues from the N-terminus and three residues from C-terminus. X6 is R, X7 is R, X8 is R, X9 is G, X10 is R, X11 is S, X16 is T, X17 is P, X18 is S, X24 is S, X26 is S, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S [Table 1].
Regarding claim 28, the HBc 147-183 peptide comprises of Formulas IV-VII, where X6 is R, X7 is R, X8 is R, X9 is G, X10 is R, X11 is S, X16 is T, X17 is P, X18 is S, X24 is S, X26 is S, X32 is S, X33 is Q, X34 is S, X35 is R, X36 is E, and X37 is S [Table 1].
Regarding claim 29, the HBc 147-183 peptide comprises of SEQ ID NO:10.
Regarding claims 30 and 31, the HBc 147-183 peptide can be considered a fusion protein as (i) the cell-penetrating peptide corresponds to the part of the sequence that has the same amino acid residues as instant SEQ ID NO:10 and the broadest reasonable interpretation can be used to interpret the first three residues, not predicted by Formula I, as a peptide of interest covalently linked to a truncate of Formula I.
Regarding claims 32 and 33, the HBc 147-183 peptide can be considered a conjugate characterized by (i) the cell-penetrating peptide with same sequence as instant SEQ ID NO:10 and (ii) the molecule of interest, which by the broadest reasonable interpretation can be deciphered as first three residues, not predicted by Formula I, as a molecule of interest covalently linked to a truncate of Formula I.
Regarding claim 35, Chen et al teaches that the HBc 147-183 peptide can enter the cytoplasm of S. aureus [pg 11 pgh 4]. The broadest reasonable interpretation of the word ‘complex’ includes the cytosol of the cytoplasm, unless otherwise defined by applicant. Since it has been established that the HBc 147-183 peptide can be considered a fusion protein (see claim 30 and 31 rejection), Chen et al anticipates a fusion protein HBc 147-183 complexed with cytosol.
Claim 34 is rejected under 35 U.S.C. 102(a)(1) as being unpatentable over UniProt (Accession Number L0CNB4 · L0CNB4_HBV; entry 22-APR-2020).
UniProt states that “Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins” [Function section]. The HBV capsid protein comprises of a truncate of Formula I, from residues 179 to 212. The HBV capsid protein forms a multimer and can be interpreted as a fusion protein comprising of the cell -penetrating Formula I and a peptide of interest (the remaining sequence). Thus, UniProt anticipates a multimer comprising the cell-penetrating truncate and peptide of interest because it was known, prior to filing, that the HBV protein forms a multimer.
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.
Claims 30-33 and 35 are rejected under 35 U.S.C. 103 as being unpatentable over Riedl et al, as previously applied to claims 23-29.
Riedl et al developed a vaccination strategy to use synthetic, cationic and antigenic peptides complexed to anionic nucleic acids [Abstract]. These cationic peptide motifs are “cell-penetrating peptides” [1.2]. Of the natural sources of antigenic, cationic peptides introduced, the cationic peptide HBc150–183 from the HBcAg protein has the same sequence and length as instant SEQ ID NO:10 [Table 1].
Regarding claims 30-31, Riedl teaches complexes of plasmid DNA with cationic peptides in which a CD8+ T-cell-stimulating epitope peptide was fused to a cationic domain [1.3]. Riedl et al. does not explicitly show that the HBc150–183 peptide can be fused to the CD8−+ T-cell epitope and only shows an N-terminal CD8−+ T-cell epitope fused to cationic tat domain [Fig 1]. However, it would have been obvious to an artisan of ordinary skill that the HBc150–183 peptide, which is a truncate of instant Formula I, can be used as a cationic peptide in place of Tat50-97 because Riedl et al presents the HBc150–183 peptide as a potential cationic peptide, fit for being used as a delivery system for peptide or DNA into the cytosol [1.2 and Table 1]. Prior to the effective filing date, one of ordinary skill could expect reasonable success of making a fusion protein comprising of HBc150–183, a cell-penetrating truncate of Formula I covalently linked to a peptide of interest (CD8−+ T-cell epitope).
Regarding claim 32 and 33, the broadest reasonable interpretation allows the designation of the CD8−+ T-cell epitope as a molecule of interest. It would have been obvious, according to Riedl et al’s teachings, that a molecule of interest can be covalently linked to HBc150–183 peptide, in place of Tat50-97, because Riedl et al presents the HBc150–183 peptide as a potential cationic peptide [1.2 and Table 1]. Prior to the effective filing date, one of ordinary skill could expect reasonable success of making a fusion protein comprising of HBc150-183, a cell-penetrating truncate of Formula I covalently linked to a molecule of interest,
Regarding claim 35, Riedl et al. also teaches that cationic peptides work well with DNA vaccines because the “Cationic, R-rich peptides interact with their guanidino head groups through H-bonds with the phosphate backbone of RNA or DNA molecules “ [1.2]. Riedl introduced HBc150-183 as a natural source of cationic peptides, along with Tat50-97 [Table 1]. Since Riedl demonstrated that Tat50-97 fuses with CD8−+ T-cell epitope T404–412, to form a T404–412-tat peptide and the peptide forms a complex with pCI/S plasmid/DNA, it is obvious that HBc150-183 could do the same [Fig 1]. Therefore, a person of ordinary skill would have learned from Riedl et al, prior to the effective filing date, to make a complex comprising a (1) fusion protein of cell-penetrating HBc150–183, and the CD8+ T-cell-stimulating epitope peptide and (2) pCl/S plasmid DNA non-covalently complexed with.
Therefore, the claims were prima facie obvious at the time before the effective filing date of the claimed invention.
Claim Summary
Claim 29 is rejected under 35 U.S.C. 112(a) and 112(b). Claims 23-34 are rejected under 35 U.S.C. 101. Claims 23-35 are rejected under 35 U.S.C. 102(a)(1). Claims 30-33 and 35 are rejected under 35 U.S.C. 103.
Correspondence
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SACHI JAUHARI whose telephone number is (571)272-3769. The examiner can normally be reached Mon-Fri 9-4.
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, Lianko Garyu can be reached at (571) 270-7367. 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.
/SACHI JAUHARI/Examiner, Art Unit 1654 /LIANKO G GARYU/ Supervisory Patent Examiner, Art Unit 1654
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