DETAILED ACTION
Notice of Pre-AIA or AIA Status
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. The Preliminary Amendment filed on November 7, 2024, has been received and entered.
Claim Disposition
3. Claims 9, 12-13 and 18 are cancelled. Claims 1-8, 10-11, 14-17 and 19-24 are pending and are under examination.
Information Disclosure Statement
4. The Information Disclosure Statements filed on May 12, 2025 and November 7, 2024, have been received and entered. The references cited on the PTO-1449 Form have been considered by the examiner and a copy is attached to the instant Office action. Note that a few references have been lined through because of an improper date citation.
Specification Objection
5. The specification is objected to for the following informalities:
The specification is objected to because the organism names are not consistently italicized throughout the specification see Moniliella pollinis on page 2 and see page 6, for example, ‘Ustilaginacceae’.
Appropriate correction is required.
Claim objection
6. Claims 1-8, 10-11, 14-17 and 19-24 are objected to for the following informalities:
For clarity and precision of claim language it is suggested that claim 1 is amended to recite “….yeast cell [[capable of producing]] that produces arabitol…. An exogenous polynucleotide sequence encoding…….arabitol [[2-dehydrogeanse]] 2-dehydrogenase…..”. See also claim 6 with similar language. The dependent claims hereto are also included.
Claim 3 is objected to because the organism name is consistently italicized see ‘Ustilaginacceae’.
For clarity it is suggested that claim 16 is amended to read, “A method for producing arabitol, [[the method]] comprising:…”, to remove redundancy. See also claim 17 with similar language.
Appropriate correction is required.
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.
7. Claims 1-8, 10-11, 14-17 and 19-24 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AlA), 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.
The claimed invention is directed to “a genetically engineered yeast cell capable of producing arabitol, the engineered yeast cell comprising:
an exogenous polynucleotide sequence encoding an arabitol 2-dehydrogenase enzyme (ARD2DH) comprising a sequence at least 80% identical to one of SEQ ID NOs: 1, 2, 3, 9 or 11. The claimed invention encompasses a large variable genus of enzymes that are not adequately described; and the invention encompasses a large variable genus of engineered yeast cells that are capable of producing arabitol, having an exogenous polynucleotide sequence that encodes the enzyme.
The art generally recognizes for example, several different genes can encode the same protein and there is an enormous amount of variability in the amino acid sequence. It is well-established in the art that a single amino acid change can be detrimental to the structure function relationship of a protein.
The specification at page 2 discloses that the yeast cell maybe of the subphylum Ustilaginomycotina and the engineered cell maybe a Moniliella pollinis cell. However, claim 1 is not limited to that embodiment. It is noted that claim 6 recites a genus of yeast and said yeast encompasses an exogenous polynucleotide sequence encoding an arabitol 2-dehydrogenase that is a least 85% identical to the aforementioned sequences (a very broad genus).
The claimed invention is also directed to a method for producing arabitol comprising the engineered yeast cell of claims 1 and 6 by contacting with a substrate. The method does not recite the specific substrate and the independent claims encompasses a genus of organisms and structures. Thus the claimed invention is overly broad and not commensurate in scope with the disclosure in the specification. Therefore, the claimed invention is not adequately described. No correlation is made between structure and function for the enzyme and coding sequence of the claimed invention, and does not demonstrate possession of the large genus. The specification fails to provide a representative number of species for the claimed genus to show that applicant was in possession of the claimed genus. A representative number of species means that the species, which are adequately described, are representative of the entire genus.
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, disclosure of drawings, or by disclosure of relevant identifying characteristics, for example, structure or other physical and/or chemical properties, by
functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. Vas-Cath Inc. v. Mahurkar, 935 F.2d 1555, 1563-64, 19 USPQ2d 1111, 1117 (Fed. Cir. 1991), states that "applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed" (See page 1117). The specification does not "clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed" (See Vas-Cath at page 1116). The skilled artisan cannot envision the detailed chemical structure of the encompassed genus, and therefore, conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993).
Therefore, for all these reasons the specification lacks adequate written description, and one of skill in the art cannot reasonably conclude that the applicant had possession of the claimed invention at the time the instant application was filed.
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.
8. Claims 20 and 23-24 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 8 is indefinite for the recitation of “a yeast cell capable of producing arabitol at titer of at least 0.2 when used in a fermentation process in the presence of dextrose…”, because there are no indicia in the claim of the specific yeast and said yeast is recited as “capable of producing arabitol”, however, the titer is given a specific measurement with unknown variables.
Claims 20 and 23-24 are indefinite for the recitation of the phrase “reduced relative to an equivalent” because the amount of reduction is unknown the comparison organism is unknown and the specific polynucleotide is unknown, thus the claim language is highly ambiguous.
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.
9. 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.
10. Claim(s) 1-8, 10-11, 14-17 and 19-24 is/are rejected under 35 U.S.C. 103 as being unpatentable over WO 2020/168407 (of record in the application) in view of Blaesing et al. (AXE81702 (Aug. 2009, see below alignment), CN 101 899 454 (of record in the application), Kobayashi et al. (of record in the application) and Kordowska-Wiater (of record in the application).
The primary reference teaches recombinant host cells, capable of producing ribitol, wherein the recombinant microorganism is a yeast of a genus selected from Yarrowia, Candida, Saccharomyces, Pichia, Hansenula, Kluyveromyces, Issatchenkia,
Zygosaccharomyces, Debaryomyces, Schizosaccharomyces, Pachysolen,
Cryptococcus, Trichosporon, Rhodotorula, and Myxozyma. SEQ ID NO: 180 is a
Candida tropicalis D-arabitol-dehydrogenase that has 94.3 % identity (99.6 %
similarity) over 282 positions in a common overlap (range (q:s): 1-282:1-282)
with SEQ ID NO: 11 of the present application. The primary reference discloses D-arabitol-dehydrogenase and the instant claims recite arabitol 2-dehydrogenase, however the art generally recognizes that the compounds refer to the same general class of enzymes that catalyze the oxidation of the sugar alcohol D-arabitol but represent different levels of naming specificity. The primary reference does not teach a structure that is at least 80% identical to the recited sequences. However, Blaesing et al. teaches the structure of SEQ ID NO:1 with at least 81% sequence identity (see below alignment. The tertiary reference discloses a 2-D-arabitol dehydrogenase protein (AZG74784) from Pichia stipitis that is 100% identical with SEQ ID NO: 2 and the recombinant expression of said enzyme in E.coli for preparing D-arabitol. The fourth reference discloses the use of the yeast Moniliella for the production of the sugar alcohol erythritol. The fifty reference discusses research on native yeasts from the genera Candida, Pichia, Debaryomyces and Zygosaccharomyces as well as genetically modified strains of Saccharomyces cerevisiae, which are able to utilize biomass hydrolysates to effectively produce L- or D-arabitol.
According to the disclosure in the specification, candidate D-arabitol 2-dehydrogenase (ARD2DH) enzyme sequences were selected from the Uniprot database and analyzed (paragraph [0067], i.e. the enzymes of SEQ ID NOs: 1-3, 9 and 11 per se were already known in the art). The instant claims 1 (and 2) refer to a genetically engineered yeast cell capable of producing arabitol, the engineered yeast cell comprising an exogenous polynucleotide sequence encoding an arabitol 2-dehydrogenase (ARD2DH) enzyme or having at least 80% identity with at least one of SEQ ID NOs: 1, 2, 3, 9 or 11 of the present application.
As the enzyme disclosed in the primary reference has 67.7 % identity with SEQ ID NO: 11 of the present application and is expressed in yeast that are specified as, for example, Yarrowia, Candida, or Pichia, said disclosure is considered to render the claimed invention as obvious (pertaining to instant claims 1-4). Instant claims 5-6 refers to a yeast cell of the Moniliella genus. The use of the yeast Moniliella for the production of sugar alcohols is disclosed in the tertiary reference. Given that the recombinant yeast of claim 1 is known in the art, the use of an alternative host (that is already known in the art for this purpose) is considered a workshop modification that is obvious. Consequently, dependent claims 7-8, 10-11, 16-17 are obvious.
Regarding claim 19 which refers to common fermentation conditions that lie within the normal ability of a person skilled in the art and cannot render the claimed method as non-obvious. The same argumentation applies to claims 20-24, which refer to production rates during the fermentation process.
Claims 1, 6, 14 and 15 refer to yeast cells, wherein the arabitol 2-dehydrogenase
enzyme has a sequence at least 80, 85% and 90% identical to SEQ ID NOs: 1/ 2, 3, 9
and/or 11. The problem to be solved could be formulated as the provision of recombinant cells for the production of arabitol. The solution are yeast cells expressing an arabitol 2-dehydrogenase enzyme having a sequence at least 85%/ 90%
identical to SEQ ID NOs: 2, 3, 9 and/or 11.
The current application has shown that Moniliella strains transformed with the
polynucleotide sequence encoding the arabitol 2-dehydrogenase of SEQ ID
NOs: 2, 3, 9 and/or 11 produce significant amounts of arabitol upon culture in
shake flask fermentations. However, insofar as claims 14 and 15 refer to any
yeast as a host cell, it is not credible that the problem is solved over the whole
scope of the claims.
In contrast, Examples 3 (Table 5) and 4 (Table 7) of the application show that
the specific strains "1-3" (a-f), "1-4" (a-f), "1-10" (a-h) and "1-12" (a-g), i.e.
Moniliella pollinis strains transformed with the polynucleotide sequences
encoding SEQ ID NOs: 2, 3, 9 and 11, indeed produce significant amounts of
arabitol. This is considered an unexpected and advantageous finding, however, the invention as claimed has unreasonable broadening and thus rendered obvious via the cited references.
Therefore, it would have been obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to arrive at the claimed invention as a whole because the combined teaching of the references render the claimed invention as obvious. One of ordinary skill in the art would be motivated to combine the references because they are analogous art.
Moreover, the Supreme Court pointed out in KSR, “a patent composed of several elements is not proved obvious merely by demonstrating that each of its elements was, independently, known in the prior art.” KSR, 127 S. Ct. at 1741. The Court thus reasoned that the analysis under 35 U.S.C. 103 "need not seek out precise teachings directed to the specific subject matter of the challenged claim, for a court can take account of the “inferences and creative steps that a person of ordinary skill in the art would employ.” Id. at 1741. The Court further advised that “[a] person of ordinary skill is…a person of ordinary creativity, not an automation.” Id. at 1742. Therefore, the claimed invention was obvious to make and use at the time the invention was made and was prima facie obvious.
RESULT 2
AXE81702
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
ID AXE81702 standard; DNA; 1038 BP.
XX
AC AXE81702;
XX
DT 20-AUG-2009 (first entry)
XX
DE Gibberella zeae PH-1 derived DNA SEQ 1611.
XX
KW plant; agriculture; transgenic plant; plant identification;
KW plant breeding; genetic marker; crop improvement; protein production;
KW abiotic stress tolerance; cold tolerance; heat tolerance;
KW drought resistance; freezing tolerance; salt tolerance; coding sequence;
KW ds.
XX
OS Gibberella zeae PH-1.
XX
CC PN WO2009077611-A2.
XX
CC PD 25-JUN-2009.
XX
CC PF 19-DEC-2008; 2008WO-EP067960.
XX
PR 19-DEC-2007; 2007EP-00150175.
XX
CC PA (BADI ) BASF PLANT SCI GMBH.
XX
CC PI Blaesing O, Henkes S, Kollipara K, Kulkarni R, Reuzeau C;
CC PI Thimm O, Wesley B;
XX
DR WPI; 2009-K61871/43.
DR P-PSDB; AXE81703.
DR PC:NCBI; gi46128266.
DR PC_ENCPRO:NCBI; gi46128267.
XX
CC PT Producing a plant with increased yield as compared to a corresponding
CC PT wild type plant, comprises increasing or generating in a plant or its
CC PT part one or more activities.
XX
CC PS Claim 2; SEQ ID NO 1611; 255pp; English.
XX
CC The present invention relates to a novel method of producing a plant with
CC increased yield as compared to a corresponding wild type plant. The
CC method comprises: increasing or generating in a plant or a part one or
CC more activities of polypeptides associated with abiotic stress responses
CC and abiotic stress tolerance in plants, selected from 30S ribosomal
CC protein S11, 60S ribosomal protein, adaptin medium chain homolog APM2,
CC B0252-protein, BRICK1-like protein, Cav1 protein, chloroplast chaperonin,
CC DNA polymerase, flagellar protein, G2/mitotic-specific cyclin, GRE1-
CC protein (hydrophilin), and membrane protein. The methods, transformed
CC wild type plant, isolated nucleic acid molecule, nucleic acid construct,
CC vector, polypeptide, antibody, plant cell nucleus, plant cell, plant
CC tissue, propagation material, pollen, progeny, and harvested material are
CC useful for producing a transgenic plant with increased yield as compared
CC to a corresponding non-transgenic plant; for producing a polypeptide; for
CC identifying a compound conferring increased yield as compared to the
CC corresponding non-transformed wild type plant cell; for producing an
CC agricultural composition; and for identifying the plant with the
CC increased yield; also, the nucleic acids of the invention are useful for
CC preparing the plant with increased yield as compared to the corresponding
CC non-transformed wild type plant; as markers for identification or
CC selection of the plant with increased yield as compared to the
CC corresponding non-transformed wild type plant; and as markers for
CC detection of yield increase in plants or plant cells. The method produces
CC plant that shows an improved yield-related trait, nutrient use efficiency
CC and/or abiotic stress tolerance, salt stress, heat stress, drought stress
CC and low temperature stress, while low temperature stress refers to
CC chilling tolerance and/or freezing tolerance, increased low temperature
CC tolerance, and increase of harvestable yield. The present sequence
CC represents the Gibberella zeae PH-1 derived DNA sequence which was useful
CC during the method of the invention for producing a plant with increased
CC tolerance to environmental stress and/or increased yield.
CC
CC Revised record issued on 06-AUG-2009 : Enhanced with precomputed
CC information from BOND.
XX
SQ Sequence 1038 BP; 233 A; 290 C; 256 G; 259 T; 0 U; 0 Other;
Alignment Scores:
Length: 1038
Score: 1293.00 Matches: 246
Percent Similarity: 81.3% Conservative: 46
Best Local Similarity: 68.5% Mismatches: 45
Query Match: 69.7% Indels: 22
Gaps: 3
US-18-863-705-1 (1-361) x AXE81702 (1-1038)
Qy 7 ProIleValArgThrAlaThrArgArgCysAlaAlaAla---------ArgMetCysGln 23
||| :::||| |||||| ||||||::: ||| |||
Db 13 CCTTCTTTGCGTCTCTGTGTGCGGCGTGTTGCTGCTTCACCTGCTATTCGCCCCTGTTTC 72
Qy 24 SerLeuValAlaLeuArgAlaLeuHisAspGlyProProArgArgAsnLysProGlySer 43
::: ||| ||| ||||||::: |||||||||::::::|||||||||
Db 73 ACTTTTACTGCTGCGCGAAAGCTTCACAATGTCCCTCCCCGACAGGACAAACCAGGAAAA 132
Qy 44 HisSerGlnThrAspSerAspIleGluIleProPheProProGluAspGluLeuPro--- 62
::::::||||||||| ||||||::: :::||| ::: |||||||||
Db 133 TATGCCCAGACCGATCCCCAGATCGAGGTTGAGTACCCAGAAGATCATGAGCTCCCTAGC 192
Qy 63 SerAspProValArgArgAlaGlyGlyGlnTyrValLysProThrLeuGlnThrPheSer 82
|||:::|||||| |||||||||||||||||||||||||||||| ||||||:::
Db 193 AGTGAGCCTGTCTCTGGCGCTGGTGGCCAGTATGTGAAGCCAACTCTGCCCACCTTTACA 252
Qy 83 LeuAspLysLysValGlyLeuValThrGlyGlyAlaArgGlyLeuGlyLeuValIleAla 102
|||||| ||||||:::|||||||||||||||||||||||||||||||||:::
Db 253 CTCGACGGTCATGTTGGCATCGTCACCGGTGGTGCACGTGGGTTGGGTCTTGTTATGGGT 312
Qy 103 GlnGlyMetValTyrSerGlyAlaAspValAlaLeuValAspMetAsnSerLysLeuThr 122
||||||||||||:::||||||:::::::::||||||||||||||||||
Db 313 CAAGGAATGGTATTCTCTGGATCCAACCTTGCTCTTGTTGATATGAAT------------ 360
Qy 123 GlnLysLeuGlyGlySerPheThrSerAlaAspIleProThrGluGluGluAlaGluLys 142
:::|||||||||||||||
Db 361 ------------------------------------------AAGGAAGAAGCAGAGAAG 378
Qy 143 GlnThrLysAsnLeuValLysAlaPheMetArgGluAsnProAsnAlaAlaArgValPro 162
|||||| ::::::::: ||| :::||||||||| ||| |||:::|||
Db 379 CAGACTAGCTTGATCATTGAAGAGTTCAAAAAGGAGAACCCTCGAGCCCGACGAATCCCA 438
Qy 163 LysValThrAlaHisPheSerAspValSerAspProAlaSerValAspAlaCysIleAla 182
|||||||||||||||::::::||||||||||||||| ||||||:::||||||:::|||
Db 439 AAGGTCACTGCCCATTATGCTGATGTATCTGATCCTGAATCTGTCGAGGCTTGTGTAGCC 498
Qy 183 GluValIleGluGlnHisGlyLysIleAspAsnLeuValThrSerAlaGlyPheThrGlu 202
||||||:::::::::|||||||||||||||||||||||||||||||||||||||||||||
Db 499 GAGGTTGTTAAGGAGCACGGAAAGATCGACAACCTGGTCACCTCAGCTGGCTTCACGGAG 558
Qy 203 AsnTyrGluAlaValAsnTyrProIleAspArgLeuArgLysLeuTrpAlaValAsnIle 222
|||:::|||||||||||||||||||||||||||||||||||||||||||||||||||:::
Db 559 AACTTCGAAGCCGTTAACTACCCCATCGACCGTCTCCGTAAGCTTTGGGCTGTTAACGTT 618
Qy 223 AspGlyThrTyrLeuPheAlaThrSerValAlaArgHisLeuMetGluArgLysAlaPro 242
|||||||||||||||||||||||||||||||||||||||||||||:::||||||||||||
Db 619 GACGGTACATATCTCTTTGCAACATCAGTCGCCAGGCACTTGATGCAAAGAAAGGCTCCT 678
Qy 243 GlySerMetValLeuIleGlySerMetSerGlySerIleValAsnValProGlnProGln 262
||||||:::|||:::|||||||||||||||||||||||||||||||||||||||||||||
Db 679 GGTAGCATCGTCATGATTGGTAGCATGTCCGGATCCATTGTCAACGTTCCTCAGCCTCAG 738
Qy 263 ThrProTyrAsnValSerLysAlaGlyValArgHisLeuAlaSerSerLeuAlaValGlu 282
||||||||| :::||||||||||||||||||||||||:::|||||||||||||||
Db 739 GCTCCCTATAATGCCGCCAAAGCCGGTGTGCGCCATCTCGCTGCTTCCTTGGCCGTCGAA 798
Qy 283 TrpAlaAspAlaAsnIleArgValAsnCysLeuSerProGlyTyrMetMetThrAlaLeu 302
|||||| |||||||||||||||||||||:::|||||||||||||||:::|||||||||
Db 799 TGGGCTCAGGCAAACATCCGAGTCAACTGCATCTCTCCCGGTTACATGTTGACTGCACTC 858
Qy 303 ThrAlaLysIleLeuAspGluAsnProGluLeuLysLysLysTrpValSerLeuIlePro 322
||| ||||||||||||:::||||||:::|||||| |||||| ||||||||||||
Db 859 ACTCAGAAGATTCTTGACGACAACCCGGATCTCAAGGCCAAGTGGACTTCCCTTATCCCC 918
Qy 323 MetGlyLysMetGlyAspProGlyAspLeuMetGlyProValIlePheLeuLeuSerGlu 342
|||||||||||| ||| |||||||||||||||||| ||||||||||||:::
Db 919 CAGGGCAAAATGGGACAACCACAGGACCTCATGGGGCCCGTGGCATTCCTCCTATCAGAT 978
Qy 343 AsnSerLysTyrValAsnGlyIleAspLeuArgValAspGlyGlyTyrThrLeuThr 361
||| |||||| ||| |||:::|||||||||||||||||||||:::|||
Db 979 GCTTCTTCGTATGTGACTGGTGCCGACATCCGAGTCGATGGCGGCTACACCGTTACC 1035
SEQ ID NO:2
RESULT 1
Z46866
LOCUS Z46866 1157 bp mRNA linear PLN 12-JUN-2006
DEFINITION P.stipitis ARDH gene encoding D-arabitol dehydrogenase.
ACCESSION Z46866
VERSION Z46866.1
KEYWORDS D-arabitol dehydrogenase.
SOURCE Scheffersomyces stipitis (Enteroramus dimorphus)
ORGANISM Scheffersomyces stipitis
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Pichiomycetes; Debaryomycetaceae; Scheffersomyces.
REFERENCE 1 (bases 1 to 1157)
AUTHORS Hallborn,J., Walfridsson,M., Penttila,M., Keranen,S. and
Hahn-Hagerdal,B.
TITLE A short-chain dehydrogenase gene from Pichia stipitis having
D-arabinitol dehydrogenase activity
JOURNAL Yeast 11 (9), 839-847 (1995)
PUBMED 7483848
REFERENCE 2 (bases 1 to 1157)
AUTHORS Hallborn,J.
TITLE Direct Submission
JOURNAL Submitted (30-NOV-1994) Johan Hallborn, Applied Microbiology, Lund
Institute of, Technology, Chemical center, Getingevagen 60, Lund,
S-221 00, Sweden
FEATURES Location/Qualifiers
source 1..1157
/organism="Scheffersomyces stipitis"
/mol_type="mRNA"
/strain="CBS 6054"
/db_xref="taxon:4924"
gene 1..1157
/gene="ARDH"
CDS 191..1027
/gene="ARDH"
/function="NAD dependent, oxidises D-arabitol to
D-ribulose"
/experiment="experimental evidence, no additional details
recorded"
/codon_start=1
/transl_table=12
/product="D-arabitol dehydrogenase"
/protein_id="CAA86939.1"
/db_xref="GOA:P50167"
/db_xref="InterPro:IPR002198"
/db_xref="InterPro:IPR002347"
/db_xref="InterPro:IPR016040"
/db_xref="InterPro:IPR020904"
/db_xref="UniProtKB/Swiss-Prot:P50167"
/translation="MDYSYANVVPNFRLDGRLAIITGGSGGLAAVISRALLAQGADVA
LIDMNLERTKSAAKEVLGWGEETLKGEHASAIGQVSAWSCNIGDAEAVDATFSSINEH
HGKIADLLINTAGYCENFPAETYPATNAESIMKVNGLGSFYVSQSFARPLIQNNLRGS
IILIGSMSGTIVNDPQPQCMYNMSKAGVIHLVRSLACEWAKYNIRVNTLSPGYILTPL
TRNVISGHTEMKEAWESKIPMKRMAEPKEFVGSILYLASETASSYTTGHNLVVDGGYE
CW"
ORIGIN
Alignment Scores:
Length: 1157
Score: 1442.00 Matches: 278
Percent Similarity: 100.0% Conservative: 0
Best Local Similarity: 100.0% Mismatches: 0
Query Match: 100.0% Indels: 0
Gaps: 0
US-18-863-705-2 (1-278) x Z46866 (1-1157)
Qy 1 MetAspTyrSerTyrAlaAsnValValProAsnPheArgLeuAspGlyArgLeuAlaIle 20
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 191 ATGGACTACTCATACGCTAACGTTGTTCCCAACTTCAGATTGGACGGAAGATTGGCTATT 250
Qy 21 IleThrGlyGlySerGlyGlyLeuAlaAlaValIleSerArgAlaLeuLeuAlaGlnGly 40
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 251 ATTACCGGAGGTTCTGGTGGTTTGGCCGCAGTCATTTCGCGTGCCTTGTTGGCCCAGGGC 310
Qy 41 AlaAspValAlaLeuIleAspMetAsnLeuGluArgThrLysSerAlaAlaLysGluVal 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 311 GCTGATGTTGCTCTCATTGACATGAACTTGGAAAGAACCAAGTCCGCTGCCAAAGAAGTT 370
Qy 61 LeuGlyTrpGlyGluGluThrLeuLysGlyGluHisAlaSerAlaIleGlyGlnValSer 80
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 371 TTGGGCTGGGGTGAAGAGACGTTGAAGGGTGAACACGCTTCAGCCATCGGCCAAGTTTCC 430
Qy 81 AlaTrpSerCysAsnIleGlyAspAlaGluAlaValAspAlaThrPheSerSerIleAsn 100
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 431 GCCTGGTCCTGCAACATTGGGGATGCTGAGGCAGTAGACGCTACTTTCAGCTCCATCAAC 490
Qy 101 GluHisHisGlyLysIleAlaAspLeuLeuIleAsnThrAlaGlyTyrCysGluAsnPhe 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 491 GAACACCACGGCAAGATCGCTGACTTGTTGATTAACACCGCTGGATACTGTGAAAACTTC 550
Qy 121 ProAlaGluThrTyrProAlaThrAsnAlaGluSerIleMetLysValAsnGlyLeuGly 140
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 551 CCTGCCGAAACGTACCCGGCTACTAACGCTGAAAGCATCATGAAGGTGAACGGTTTGGGC 610
Qy 141 SerPheTyrValSerGlnSerPheAlaArgProLeuIleGlnAsnAsnLeuArgGlySer 160
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 611 TCATTCTACGTTTCGCAATCGTTCGCTAGACCATTGATCCAGAACAACTTGAGAGGCTCT 670
Qy 161 IleIleLeuIleGlySerMetSerGlyThrIleValAsnAspProGlnProGlnCysMet 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 671 ATCATCTTGATTGGCTCAATGTCTGGAACAATTGTCAACGACCCACAACCCCAATGTATG 730
Qy 181 TyrAsnMetSerLysAlaGlyValIleHisLeuValArgSerLeuAlaCysGluTrpAla 200
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 731 TACAACATGTCCAAGGCTGGAGTGATCCACTTGGTCAGATCGTTGGCCTGCGAATGGGCC 790
Qy 201 LysTyrAsnIleArgValAsnThrLeuSerProGlyTyrIleLeuThrProLeuThrArg 220
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 791 AAGTACAACATCAGAGTCAACACCTTATCACCAGGCTATATTTTGACTCCTTTAACCAGA 850
Qy 221 AsnValIleSerGlyHisThrGluMetLysGluAlaTrpGluSerLysIleProMetLys 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 851 AACGTGATTTCTGGCCACACAGAGATGAAGGAAGCCTGGGAATCCAAGATCCCCATGAAG 910
Qy 241 ArgMetAlaGluProLysGluPheValGlySerIleLeuTyrLeuAlaSerGluThrAla 260
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 911 AGAATGGCCGAACCCAAGGAATTCGTGGGGTCCATCTTATACTTGGCAAGCGAGACTGCT 970
Qy 261 SerSerTyrThrThrGlyHisAsnLeuValValAspGlyGlyTyrGluCysTrp 278
||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 971 TCTTCCTACACTACGGGCCACAATTTGGTTGTGGACGGAGGATATGAATGCTGG 1024
Basis For NonStatutory Double Patenting
11. 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. See 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) may be used to overcome an actual or provisional rejection based on a nonstatutory double patenting ground provided the conflicting application or patent is shown to be commonly owned with this application. See 37 CFR 1.130(b).
Effective January 1, 1994, a registered attorney or agent of record may sign a terminal disclaimer. A terminal disclaimer signed by the assignee must fully comply with 37 CFR 3.73(b).
12. Claims 1-8, 10-11, 14-17 and 19-24 are rejected under the judicially created doctrine of obviousness-type double patenting as being unpatentable over claims 1, 3-6, 8, 11-17 and 20-26 of U.S. Application No. 18/663,710. An obvious-type double patenting rejection is appropriate where the conflicting claims are not identical, but an examined application claim is not patentably distinct from the reference claim(s) because the examined claim is either anticipated by, or would have been obvious over, the reference claim(s). See In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); and In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985). Although the conflicting claims are not identical, they are not patentably distinct from each other.
The instant application claims are directed to a genetically engineered yeast cell capable of producing arabitol, the engineered yeast cell….an exogenous polynucleotide sequence encoding an arabitol 2-dehydrogenase……at least 80% identical to at least one of SEQ ID NOs:1, 2, 3, 9 or 11. The copending application claims are drawn to a genetically engineered yeast cell capable of producing arabitol, the engineered yeast cell comprising: an exogenous polynucleotide sequence encoding an arabitol-phosphate dehydrogenase (APDH) enzyme comprising a sequence at least 80% identical to SEQ ID NO: 11. Although the scope of the two sets of claims differs, the two sets of claims are an obvious variation of each other, thus prima facie obvious. This is a provisional obvious type double patenting rejection.
Conclusion
13. No claims are presently allowable.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to HOPE A ROBINSON whose telephone number is (571) 272-0957. The examiner can normally be reached 9-5pm on Monday to Friday.
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/HOPE A ROBINSON/Primary Examiner, Art Unit 1652
Prosecution Insights