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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on August 14, 2025 has been entered.
Claim Objections
Claim 13 is objected to because of the following informalities: the claim is interrupted by a period, which would be more appropriately a comma, at the end of line 11. Appropriate correction is required.
Claim Rejections - 35 USC § 112
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 13 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.
Claim 13 line 5-6 recites the selectable marker is luc (luciferase) or sh-Ble (bleomycin resistance). The presence of the parentheticals makes unclear whether the selectable mark must be the particular genes recites (ie. luc or sh-Ble) or any luciferase or bleomycin resistance gene. For the purpose of compact prosecution, the claim is interpreted as comprising a selectable marker which is any luciferase or bleomycin resistance gene.
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 3-4, 7-8, 13, and 28-31 stand rejected under 35 U.S.C. 102(a)(1) as being anticipated by Mendez et al. (WO 2009/158658 A2; Published: Dec 30, 2009) as evidenced by Ferris et al. (Biochemistry. 40: 2978-2987; Published: Feb 10, 2001).
Mendez et al. teaches a method of increasing flocculation in Chlamydomonas reinhardtii by fusing the protein of interest to a glycomodule, GP1. Mendez et al. generate an expression cassette comprising the glycomodule, GP1, and lectin, the protein of interest; see Example 7 on page 31.
Regarding claims 3 and 28, back-translation of SEQ ID NO: 2 has 100% sequence identity with residues 980-1078 of SEQ ID NO: 13 and residues 1229-1327 of SEQ ID NO: 12 which are nucleic acids encoding a lectin fused to GP1 and incorporated into a construct (ie. a vector further comprising an expression cassette) for production by Chlamydomonas reinhardtii. Mendez et al. teaches that the expression cassette comprises a secretory signal peptide; see Figure 1 “Targeting signal” and paragraph 0015. Regarding claim 4, Mendez et al. teaches the expression cassette comprises a bleomycin resistance gene, or selectable marker; see Example 7 paragraph 00134.
Regarding claim 7, Mendez et al. teaches the expression cassette depicted in Figure 1E in which the selection marker (bleomycin resistance gene, 2A) and transgene (GP1-lectin coding regions) are physically linked in-frame, resulting in a chimeric single ORF. Figure 1E, shown below, shows that the targeting signal, or signal peptide, is between the selection marker and transgene, thus, also included in the single ORF. Additionally, two tags (MAT and FLAG) are located within the transgene, specifically between the GP1 and lectin (the flocculation protein or protein of interest), and are also included in the single ORF; see Example 7 on page 31.
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Regarding claim 8, the expression cassette taught by Mendez et al. further comprises a TEV protease recognition site between the GP1 and protein of interest’ see Example 7 on page 31.
Claim 13 recites several features, in the alternative, of the expression cassette including the regulatory nucleotide sequence. Mendez et al. teaches the expression cassette comprises a regulatory sequences called "Promoter/ 5' UTR" which is the C. reinhardtii HSP70 / rbcS2 5' UTR with introns; see Example 7 paragraph 00134.
Claims 29-31 recites a host cell, specifically, Chlamydomonas reinhardtii, comprising the vector; and the method of expressing a protein of interest comprising growing a microalga cell comprising a vector comprising the expression cassette of claim 3 and the method of expressing a protein of interest.
Mendez et al. teaches a vector comprising the expression cassette comprising the glycomodule and protein of interest and that to express the fusion Lectin-GP1 protein Chlamydomonas reinhardtii microalga cells were transformed via electroporation and grown on TAP agar plates containing 20ug/mL bleomycin; see Example 7 on page 31.
While Mendez et al. doesn’t explicitly state that GP1 is a glycoprotein or may be glycosylated, GP1 was previously characterized in Ferris et al. which teaches that the PPSPX domain, or the segment that aligns with instant SEQ ID NO: 2 and residues 980-1078 of Mendez et al. SEQ ID NO: 13 and residues 1229-1327 of Mendez et al. SEQ ID NO: 12, can be glycosylated. According to the definition on page 5 of the instant disclosure, GP1 as taught in Mendez et al. and as evidenced by Ferris et al. is a glycomodule motif.
Thus, claims 3-4, 7-8, 13, and 28-31 are anticipated by Mendez et al.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
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 5-6 stand rejected under 35 U.S.C. 103 as being unpatentable over Mendez et al. (WO 2009/158658 A2; Published: Dec 30, 2009), as evidenced by Ferris et al. (Biochemistry. 40: 2978-2987; Published: Feb 10, 2001), as applied to claim(s) 3-4, 7-8, 13, and 28-31 above, and in view of Kieliszewski (US 2005/0074838 A1; Published: Apr 7, 2005) and Ramos-Martinez et al. (Plant Biotechnology Journal. 15(9): 1214-1224; Published: Feb 16, 2017). and Goodenough et al. (The Journal of Cell Biology. 101: 1550-1568; Published: October 1985).
The teachings of Mendez et al. as evidenced by Ferris et al., as related to claim(s) 3-4, 7-8, 13, and 28-31, from which these claims depend are given previously in this Office action and are fully incorporated here.
Mendez et al. teaches an expression cassette comprising a fusion protein comprising GP1. The expression cassette taught by Mendez et al. comprises the selectable marker, GP1, and the protein of interest in the same open reading frame; see Example 7 on page 31 and Figure 1E.
Mendez et al. does not teach an expression cassette where the glycomodule precedes the protein of interest.
Kieliszewski teaches an expression cassette for use in plants, which is broadly defined in paragraph 0144 to include Chlamydomonas, wherein the synthetic glycomodule, SP32, precedes the protein of interest, EGFP; see paragraph 0189. Kieliszewski noted that the absence of the glycomodule resulted in lower levels of secreted protein of interest; see paragraph 0485.
Given that Mendez et al. and Kieliszewski teach expression cassettes which comprise glycomodule motifs and can be used in Chlamydomonas for recombinant protein expression, it would have been obvious to one of ordinary skill in that art and one would have a reasonable expectation of success to modify the expression cassette taught by Mendez et al., wherein the 5’ to 3’ order is protein of interest, then glycomodule, to the 5’ to 3’ order taught by Kieliszewski, of selectable marker peptide, glycomodule, then protein of interest.
This expectation of success is further supported by the teachings of Ramos-Martinez et al. which teach that proteolytic degradation in is a challenge for recombinant protein expression in Chlamydomonas which can be addressed by adding a glycomodule, which is known to be resistant to proteolytic degradation, to the expression cassette; see pages 1214, 1215, and 1219. Further, Ferris et al. teaches that the domain of GP1 wherein SEQ ID NO: 2 is a subsequence is glycosylated and, thereby resistant to proteases; see page 2985 left column. Ramos-Martinez et al., in providing a proposed mechanism for how the synthetic glycomodule motif tested increased yield of secreted recombinant protein, draws parallels to the glycosylation of naturally occurring hydroxyproline-rich glycoproteins (HRGPs) in Chlamydomonas, which includes GP1; see page 1220 last sentence. Since Kieliszewski which teaches the 5’ to 3’ order of glycomodule, then protein of interest, also teaches that the absence of the glycomodule decreased the yield of the protein of interest, and since Mendez et al., as evidenced by Ferris et al., teaches an expression cassette comprising the fusion of the glycoprotein, GP1, to the protein of interest, but in the 5’ to 3’ order of protein of interest, then glycomodule, the modification of the order of the glycomodule and protein of interest in the expression cassette taught by Mendez et al. to the order taught by Kieliszewski would have been obvious to one of ordinary skill in the art and one would have had a reasonable expectation of success that such a modification would result in increased expression and secretion of a recombinant protein in Chlamydomonas.
Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art
before the effective filing date of the application, as evidenced by the references.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) 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 www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 3-5, 13, 28, and 29 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 53-56, 61, 64-68, and 72 of copending Application No. 19/168,527 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding instant claim 3, copending claims 64-66 and 72 teach a method of producing an antibody recombinantly and a polynucleotide encoding an antibody, or protein of interest, comprising a glycomodule motif comprising SEQ ID NO: 2 which is 100% identical to instant SEQ ID NO: 2. The antibody is encoded by a polynucleotide which comprises a secretory signal peptide. Regarding instant claim 13, copending claim 66 teaches that the signal peptide is CAH, ARS, or gametolysin.
Regarding instant claims 28 and 29, copending claims 67 and 68 teach a vector comprising the polynucleotide sequence of claim 64 and a host cell comprising the vector.
Regarding instant claim 4, the antibody comprises a tag according to copending claim 61. Regarding instant claim 5, the antibody comprises the glycomodule motif in the N-terminal position; see copending claim 54.
Copending claims 53-56, 61, 64-68, and 72 read on instant claims 3-5, 13, 28, and 29 in an anticipatory manner.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 6-8 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 53-56, 61, 64-68, and 72 of copending Application No. 19/168,527 in view of
The teachings of Application No. 19/168,527 as related to claim(s) 3-5, 13, 28, and 29, from which these claims depend are given previously in this Office action and are fully incorporated here.
While the copending claims teach a tag and a cleavage site, the copending claims are silent reading the reading frame, a second tag, a selectable marker, and a regulatory sequence.
Regarding instants claims 6 and 7, Mendez et al. teaches the expression cassette depicted in Figure 1E in which the selection marker (bleomycin resistance gene, 2A) and transgene (GP1-lectin coding regions) are physically linked in-frame, resulting in a chimeric single ORF. Figure 1E, shown below, shows that the targeting signal, or signal peptide, is between the selection marker and transgene, thus, also included in the single ORF. Additionally, two tags (MAT and FLAG) are located within the transgene, specifically between the GP1 and lectin (the flocculation protein or protein of interest), and are also included in the single ORF; see Example 7 on page 31.
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Regarding instant claim 8, the expression cassette taught by Mendez et al. further comprises a TEV protease recognition site between the GP1 and protein of interest’ see Example 7 on page 31.
Regarding instant claim 6, given that Mendez et al. teaches recombinant protein expression of a fusion protein comprising SEQ ID NO: 2 with a selectable marker in the open reading frame, it would have been obvious to one of ordinary skill in the art and one would have had a reasonable expectation of success to add a selectable marker in the same open reading frame as SEQ ID NO: 2 and the protein of interest, or antibody as taught in the copending claims. One would have been motivated to add the selectable marker in order to the select for host cells comprising the expression cassette or polynucleotide encoding the antibody – SEQ ID NO: 2 fusion protein and to guarantee co-expression of both the selectable marker gene and the fusion protein.
Regarding instant claims 7 and 8, given that Mendez et al. teaches recombinant protein expression of a fusion protein comprising SEQ ID NO: 2 with a selectable marker, two tags, a protease site in the open reading frame, it would have been obvious to one of ordinary skill in the art and one would have had a reasonable expectation of success to add these elements in the same open reading frame as SEQ ID NO: 2 and the protein of interest, or antibody as taught in the copending claims. One would have been motivated to add the two tags in order to isolate the antibody, or protein of interest, from the glycomodule sequence, selectable marker, and other regulatory elements translated. One would have been motivated to add the selectable marker in order to the select for host cells comprising the expression cassette or polynucleotide encoding the antibody – SEQ ID NO: 2 fusion protein and to guarantee co-expression of both the selectable marker gene and the fusion protein. One would have been motivated to add the protease cleavage site between the tag and protein of interest in order remove the tag from the antibody following antibody isolation.
Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art
before the effective filing date of the application, as evidenced by the references.
This is a provisional nonstatutory double patenting rejection.
Claims 30 and 31 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 53-56, 61, 64-68, and 72 of copending Application No. 19/168,527 in view of Mayfield et al. (Vaccine 23: 1828-1832; Published: November 19, 2004).
The teachings of Application No. 19/168,527 as related to claim(s) 3-5, 13, 28, and 29, from which these claims depend are given previously in this Office action and are fully incorporated here.
While the copending claims teach the recombinant production of an antibody comprising instant SEQ ID NO: 2 which is native to Chlamydomonas, as evidenced by the instant Specification page 32, the copending claims do not teach producing the antibody in Chlamydomonas reinhardtii.
Mayfield et al. teaches that Chlamydomonas reinhardtii, a microalgae, can be used to recombinantly produce antibodies with high yield; see whole document and page 1831 in particular.
It would have been obvious to one of ordinary skill in the art and one would have had a reasonable expectation of success to recombinantly produce the antibody, a protein of interest, in Chlamydomonas reinhardtii by the method taught by the copending claims because it is similar to the method discussed in Mayfield et al. which resulted in a high yield of antibody.
Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art
before the effective filing date of the application, as evidenced by the references.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant’s amendments filed August 14, 2025 are acknowledged.
Applicant's arguments filed August 14, 2025 have been fully considered but they are not persuasive.
Regarding the rejection under 35 U.S.C. 102(a)(1) as being anticipated by Mendez et al. as evidenced by Ferris et al., Applicant alleges that Mendez et al. does not teach all elements of amended claim 3 because the consisting essentially of and consists of language excludes GP1 sequences which beyond the exact sequence of SEQ ID NO: 2.
MPEP 2111.03 III states: For the purposes of searching for and applying prior art under 35 U.S.C. 102 and 103, absent a clear indication in the specification or claims of what the basic and novel characteristics actually are, “consisting essentially of” will be construed as equivalent to “comprising.”
There is no clear indication in the specification or claims of what the basic and novel characteristics actually are, thus “consisting essentially of” has been construed as equivalent to “comprising.” Recall that the use of "consists of" in the body of the claims does not limit the open-ended "comprising" language in claim 3; and, thus, the transition phrase "consists of" does not limit the claim to only the recited subsequence of GP1 (SEQ ID NO: 2) and the transition language ‘comprising’ allows the claims to cover the entire GP1, as long as the glycomodule motif contained the specific subsequence of SEQ ID NO: 2 recited by the claim; see MPEP 2111.03.II.
Further, Applicant argues that the entire GP1 sequence would materially affect the function/property of the construct, resulting in a membrane bound fusion protein, in contrast with an expressed protein secreted into the media. However, claim 3 does not recite any functional language limiting the construct to expressed proteins secreted in the media.
Claims 5-6 recite the order of the 5’ to 3’ of the glycomodule and protein of interest and the presence of a selectable marker within the open reading frame. In response to the rejection of claims 5 and 6 under 35 U.S.C. 103, Applicant argues that amended claim 3 excludes GP1 sequences which comprise more than SEQ ID NO: 2. This is addressed above.
Applicant argues that one would not have been motivated to use the full GP1 sequence in a fusion protein as taught by Mendez et al. to improve recombinant protein secretion as taught by Kieliszewski and Ramos-Martinez et al. because the full length GP1 of Mendez et al. would result in a membrane bound recombinant protein.
Claim 5 recites that the glycomodule motif precedes the protein of interest in 5’ to 3’ order. GP1 comprises a c-terminal head which embeds into the outermost layer of the cell wall – not membrane; see Goodenough et al. (The Journal of Cell Biology. 101: 1550-1568; Published: October 1985). The construct of Mendez et al. modified with the 5’ to 3’ order of glycomodule then protein of interest, would still comprise the TEV protease recognition site between the GP1 and protein of interest; see Mendez et al. Example 7 on page 31. Once cleaved, the protein of interest would be liberated or secreted into the media.
Applicant points to Figures 2A and Figure 3 and states that glycomodule motifs not derived from GP1 (ie. SEQ ID NOs: 1, 3, and 5) did not result in expression of recombinant protein, while SEQ ID NO: 2 results in higher expression of recombinant protein. Neither Mendez et al., Kieliszewski, nor Ramos-Martinez et al. teach SEQ ID NOs: 1, 3, or 5 and claims 5 and 6 do not recite them. Ferris et al. teaches that the domain of GP1 wherein SEQ ID NO: 2 is a subsequence is glycosylated and, thereby resistant to proteases; see page 2985 left column. Ramos-Martinez et al., in providing a proposed mechanism for how the synthetic glycomodule motif tested increased yield of secreted recombinant protein by reducing protease degradation, draws parallels to the glycosylation of naturally occurring hydroxyproline-rich glycoproteins (HRGPs) in Chlamydomonas, which includes GP1; see page 1220 last sentence. Thus, one of ordinary skill in the art would have had a reasonable expectation of success to improve recombinant protein yields using the GP1 sequence taught by Mendez et al.
On page 10, Applicant alleges that Mendez et al. and Ferris et al. teach away from a glycomodule sequence consisting of SEQ ID NO: 2 for improving production and secretion of recombinant proteins, but does not elaborate further.
The rejection of claims 5 and 6 under 35 U.S.C. 103 is maintained.
Conclusion
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Molino et al. (PLOS One. 13(2): e0192433; Published: Feb 6, 2018) teaches several secretory peptides for use in Chlamydomonas reinhardtii.
Huang et al. (Applied Biochemistry and Microbiology. 53(5): 513-517; Published: Sep 14, 2017) teaches producing EGF in Chlamydomonas reinhardtii.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to KATHERINE ANN HOLTZMAN whose telephone number is (571)270-0252. The examiner can normally be reached Monday - Friday 7:30am - 5:00pm.
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/KATHERINE ANN HOLTZMAN/Examiner, Art Unit 1646
/JULIET C SWITZER/Primary Examiner, Art Unit 1682