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 .
Claims Status
Claims 1-13 are amended.
Claims 1-13 are pending.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 03/19/2024 is acknowledged. The submission is in compliance with the provision of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered.
Election/Restrictions
Applicant's election with traverse of Group 1 (claims 1-10) in the reply filed on 07/07/2026 is acknowledged. The traversal is on the ground(s) that the Applicant argues that the finding of lack of unity of invention is premature in the present application as a full search of the prior art has yet to have been conducted. This is not found persuasive since Groups 1-3 lack unity of invention because even though the inventions of these groups require the common technical feature of a solid support wherein a ribonucleic acid molecule containing at least one motif of UNAAAC nucleotide sequence is grafted onto a solid support or coupled to a capture ligand, this technical feature is not a special technical feature as it does not make a contribution over the prior art in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2626-2641; published online August 1, 2017). Touat-Todeschini et al. disclose a biotinylated RNA (5’Biot-GGAUCCUUAAACAGAUCU) that was added to a lysis extract and incubated at 1 hour at room temperature and added to a mixture of Dynabeads M280 Streptavidin (solid support; coupled to a capture ligand) (see RNA pull-down assay, pg. 2639).
Applicant's election with traverse of:
Species Group 1: SEQ ID NO: 9
Species Group 2: SEQ ID NO: 18
in the reply filed on 07/07/2026 is acknowledged. The traversal is on the ground(s) that the generic claims are not so broad as to place an undue burden on the Patent Office to search and examine the full scope of the claims. This is not found persuasive because each SEQ ID NO: is a distinct amino acid sequence/polypeptide requiring separate searches in databases and prior art literature.
The requirement is still deemed proper and is therefore made FINAL.
Claim 11-13 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention/subject matter, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 07/07/2026.
Specification
The disclosure is objected to because of the following informalities: The term phosphorothiate internucleotide bond is not known in the art (see specification line 31, pg. 9). The Examiner assumes that this may be a misspelling of the term phosphorothioate which is known in the art.
Appropriate correction is required.
Claim Objections
Claim 1 is objected to because of the following informalities:
Claim 1 recites “A method for purifying a protein of interest successively comprising..”. The language is awkward. Examiner suggests “protein of interest comprising successfully..” would be better language or leaving out as the steps appear to inherently comprise an order. 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.
Claims 1-10 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
With regards to claim 1 (and claims 2-10 dependent on), the claim recites “a protein of amino acid sequence having at least 90% sequence identity with the amino sequence of the protein Mm1 or of the fragment capable of binding”. It is unclear what the sequence of the Mmi1 is and therefore the claim is rendered indefinite. In the interest of compact prosecution, the Examiner is using the sequences of SEQ ID NO: 1 (Schizosaccharomyces pombe), SEQ ID NO: 3 (Schizosaccaromyces japonicus), SEQ ID NO: 5 (Schizosaccaromyces octosporus) and SEQ ID NO: 7 (Schizosaccharomyces cryophilus) as the sequences for the Schizosaccharomyces Mmi1 as described in the Specification (see specification. pg. 5, lines 5-22) to define sequences of the Mmi1 protein. Although the claims are examined in the light of the specification, the specification cannot be read into the claims, i.e., the limitation of the specification cannot be read into the claims (see MPEP 211 R-5).
With regards to claim 1 (and claim 2-10 dependent on), the claim recites “where appropriate, the brining into contact of the ribonucleic acid molecule coupled to a capture ligand with an affinity partner of the capture ligand onto a solid support”. It is unclear what defines the term “appropriate” in the claim and how one would determine when such a step is appropriate. In the interest of compact prosecution, the Examiner is interpreting this step as an optional step.
With regards to claim 7, the claim recites “at least one phosphorothiate internucleotide bond”. The phosophorothiate internucleotide bond is not known in the art thus the claim is rendered indefinite. The Examiner assumes that this is a misspelling of the term “phosphorothioate”. In the interest of compact prosecution, the Examiner is interpreting the term “phosphorothiate” recited in claim 7 as a “phosphorothioate” which is known in the art. Correction and clarification of spelling is needed.
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 5-6, and 8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164), hereinafter referred to as Touat-Todeschini.
With regards to claims 1, 5-6, and 8, Touat-Todeschini teaches a method of an RNA pull-down assay (affinity purification) in which His-Mmi1 wild type (has inherent ability to bind UNAAAC motif) was incubated with biotinylated RNA (5’Biot-GGAUCCUUAAACAGAUCU) and Dynabeads M280 Streptavidin (coupled to a capture ligand). Touat-Todeschini teaches that the beads were washed with lysis buffer and then eluted to recover the His-Mmi1 protein) (see pg. 2639). In this example, the Examiner is interpreting the His tag as the protein of interest in the His-Mmi1 fusion. Touat-Todeschini teaches that the Mmi1 protein is from Saccharomyces pombe (see pg. 2626 and pg. 2638).
Therefore, claims 1, 5-6, and 8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164), hereinafter referred to as Touat-Todeschini.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-2, 5-6, and 8 are rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569), hereinafter referred to as Xie, in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164), hereinafter referred to as Touat-Todeschini.
With regards to claims 1-2, 5-6, and 8, Xie teaches a method of protein purification of GST-Mmi1YTH (comprises at least the 173 C-terminal amino acids; has the inherent ability to bind to UNAAAC motif) fusion (see Protein expression and purification, pg. 13). Xie teaches that the Mmi1 protein is from Schizosaccharomyces pombe and that the GST-Mmi1YTH was subcloned from a Mmi1YTH-p28 construct to a modified PGEex-4T1 vector with a TEV protease cleavage site (Tev4T1) (see Protein expression and purification, pg. 2). Xie teaches that the GST tagged proteins were purified by glutathione sepharose (see Protein expression and purification, pg. 13). Xie teaches that the proteins were further purified by size-exclusion chromatography (indicates that the GST-mmi1 fusion protein was separated from the glutathione sepharose column in the previous step). Xie does not teach that the GST-Mmi1 fusion protein was brought into contact with a ribonucleic acid molecule containing at least one motif of UNAAAC nucleotide sequence so as to allow the affinity binding of the protein tag with the ribonucleic acid molecule, the ribonucleic acid molecule being grafted onto a solid support or coupled to a capture ligand.
However, Touat-Todeschini teaches a method of an RNA pull-down assay (affinity purification) in which His-Mmi1 wild type (has inherent ability to bind UNAAAC otif) was incubated with biotinylated RNA (5’Biot-GGAUCCUUAAACAGAUCU) and Dynabeads M280 Streptavidin (coupled to a capture ligand). Touat-Todeschini teaches that the beads were washed with lysis buffer and then eluted to recover the His-Mmi1 protein) (see pg. 2639).
It would have been obvious to one of ordinary skill in the art of protein expression and purification before the effective filing date of the current instant application to modify the method for purifying a protein of interest taught by Xie by replacing the glutathione sepharose column with the Dynabeads M280 Streptavidin taught by Touat-Todeschini, incubating the GST(protein of interest)-Mmi1 fusion protein with biotinylated RNA (5’Biot-GGAUCCUUAAACAGAUCU), and bringing into contact with the Dynabeads M280 Streptavidin (coupled with capture ligand), and then eluting the column to capture the protein of interest. In this case, the GST would be considered the protein of interest. One of ordinary skill in the art would be motivated to do so since both Xie and Touat-Todeschini teach that the Mmi1 protein has affinity for binding the UNAAAC nucleotide motif. One would then be motivated to apply a GST (protein of interest)-MMi1 protein taught by Xie to the Dynabeads M280 Streptavidin and incubated with biotinylated RNA (5’Biot-GGAUCCUUAAACAGAUCU) (coupled to a capture ligand) taught by Touat-Todeschini to achieve a method of affinity purification of the GST (protein of interest)-mmi1 fusion protein. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Xie and Touat-Todeschini who provide all the teachings, reagents, and methods needed to do so.
Therefore, claims 1-2, 5-6, and 8 are rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569) in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164).
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569), hereinafter referred to as Xie, in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164), hereinafter referred to as Touat-Todeschini, as applied to claim 1 above, and further in view of Raran-Kurussi et al. (Methods Mol. Biol. Vol. 1586; pg. 221-230, published 2017), hereinafter referred to as Raran-Kurussi.
The teachings of Xie and Touat-Todeschini as applied to claim 1 are summarized above.
Neither Xie or Touat-Todeschini teach that the separation of the protein of interest from the solid support is carried out by cleavage at the enzymatic cleavage site.
However, Raran-Kurussi teaches that although affinity tags are highly effective tools for the expression and purification of recombinant proteins, they generally need to be removed prior to structural and functional studies. Raran-Kurusi teaches the use of a stable variant of tobacco etch (TEV) protease in E. coli as a reagent for removing affinity tags from recombinant proteins by site-specific endoproteoolysis (see Abstract, pg. 221).
It would have been obvious to one of ordinary skill in the art of protein expression and purification before the effective filing date of the current instant application to use the TEV protease reagent taught by Raran-Kurussi to remove the GST (protein of interest) from the solid support in the modified purification method taught by Xie and Touat-Todeschini since Xie teaches the GST-Mmi1 fusion protein contains a TEV cleavage site. One of ordinary skill in the art would be motivated to do so since Raran-Kurussi teaches that it is generally needed to remove affinity tags from proteins of interest before functional and/or structural studies and using TEV protease would be effective in removing the protein of interest (GST) from the solid support by specifically targeting the TEV cleavage site of the fusion protein. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Xie, Touat-Todeschini, and Raran-Kurussi who provide all the teachings, reagents, and methods needed to do so.
Therefore, claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569) in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164) as applied to claim 1 above, and further in view of Raran-Kurussi et al. (Methods Mol. Biol. Vol. 1586; pg. 221-230, published 2017).
Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569), hereinafter referred to as Xie, in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164), hereinafter referred to as Touat-Todeschini, as applied to claim 1 above, and further in view of Bogyo et al. (US Patent No.: 8,314,215 B2; published November 20, 2012), hereinafter referred to as Bogyo.
The teachings of Xie and Touat-Todeschini as applied to claim 1 are summarized above.
Neither Xie or Touat-Todeschini teach a method of purifying a protein of interest in which a cleavage site is inserted between the ribonucleic acid molecule containing at least one motif of UNAAAC nucleotide sequence and the solid support
However, Bogyo teaches a linker system that is provided where a small molecule reactive group (probe that binds to certain enzymes at the active site) is linked through an aryl diazo linker to an affinity molecule such as biotin (see Abstract). Bogyo teaches that the reactive group may comprise a number of functionalities known to react with a specific target to be studied. Bogyo teaches that this enables the probe to be exposed to the analyte such as proteins and bind specifically to them to form a complex having an affinity molecule allowing immobilization of the bound analyte on an affinity column or other support (e.g. with streptavidin) (see Abstract). Bogyo teaches that the linker is cleaved without causing removal of the affinity group or dissociation of the probe from the analyte. Bogyo then teaches that the linker is cleaved under mild reducing conditions such as dithionite (see Abstract).
It would have been obvious to one of ordinary skill in the art of protein expression and biochemistry before the effective filing date of the current instant application to modify the method for purifying a protein of interest taught by Xie and Touat-Todeschini by inserting a cleavage site such as an aryl diazo linker between the UNAAAC nucleotide motif and an affinity molecule such as biotin. One of ordinary skill in the art would be motivated to do so by the teachings of Bogyo in order to achieve separation of the protein of interest from the solid support using mild reducing agents to achieve cleavage and obtain the protein of interest. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Xie, Touat-Todeschini, and Bogyo who provide all the teachings, reagents, and methods needed to do so.
Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569) in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164) as applied to claim 1 above, and further in view of Bogyo et al. (US Patent No.: 8,314,215 B2; published November 20, 2012).
Claim 7 is rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569), hereinafter referred to as Xie, in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164), hereinafter referred to as Touat-Todeschini, as applied to claim 1 above, and further in view of Xu et al. (Nucleic Acids Research, Vol. 24, pg. 3643-3644; published 1996), hereinafter referred to as Xu.
The teachings of Xie and Touat-Todeschini as applied to claim 1 are summarized above.
Neither, Xie or Touat-Todeschini teach that in the method for purifying a protein of interest, the ribonucleic acid molecule comprises at least one chemically modified nucleotide and/or at least one locked nucleic acid and/or at least one phosphorothiate internucleotide bond. (Note the Examiner is assuming the term recited in claim 7 “phosphorothiate” (which is not known in the art) is a misspelling of the term “phosphorothioate” which is known in the art. In the interest of compact prosecution, the Examiner is referring to the term “phosphorothioate” as the proper spelling. See above 112b rejection.
However, Xu teaches that phosphorothioate-containing nucleic acids have found wide-spread use in molecular biology. Xu teaches that the increased resistance to nuclease digestion that is displayed by sulfur-containing backbone analogues has prompted the consideration of these molecules for medical purposes (pg. 3643). Xu further teaches that backbone modifications, including phosphorothioate substitutions are also being explored as an approach for increasing the nuclease resistance. Xu teaches that the introduction of phosphorothioates into RNA can be achieved in several ways and teaches that oligoribonucleotide hexamers containing a phosphorothioate diester at every position were prepared with the EDITH protocol (see pg. 3643). Xu teaches that the new sulfurizing agent EDITH is a highly effective sulfurization agent for incorporating single or multiple phosphorothioate linkages into RNA oligomers (see last paragraph, pg. 3644).
It would have been obvious to one for ordinary skill in the art of protein engineering and purification before the effective filing date of the current instant application to modify the method for purifying a protein of interest from the combined teachings of Xie and Touat-Todeschini by incorporating at least one phosphorothioate internucleotide bond into the UNAAAC nucleotide sequence using the sulfurizing EDITH reagent taught by Xu. One of ordinary skill in the art would be motivated to do so by the teachings of Xu in order to provide nuclease digestion resistance to the UNAAAC nucleotide motif used in the method for purifying a protein of interest from the combined teachings of Xie and Touat-Todeschini which would avoid potential issues of degradation of the UNAAAC nucleotide and to provide a stable affinity molecule to achieve a robust affinity purification method. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Xie, Touat-Todeschini, and Xu who provide all the teachings, reagents, and methods needed to so so.
Therefore, claim 7 is rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569) in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164) as applied to claim 1 above, and further in view of Xu et al. (Nucleic Acids Research, Vol. 24, pg. 3643-3644; published 1996).
Claims 8-10 are rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569), hereinafter referred to as Xie in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164), hereinafter referred to as Touat-Todeschini as applied to claim 1 above, and further in view of UniProt Database entry (MMI1_SCHPO, first entry: May 5, 2009), hereinafter referred to as ‘SCHPO.
The teachings of Xie and Touat-Todeschini as applied to claim 1 are summarized above.
With regards to claim 9, neither Xie nor Touat-Todeschini specifically teach that the protein tag comprising at least a fragment of the protein Mmi1 comprising at least the 173 C-terminal residues has an amino acid sequence comprising the amino acid sequence of SEQ ID NO: 9.
However, ‘SCHPO teaches a Mmi1 protein from Schizosaccaromyces pombe (claim 8) that comprises an amino acid sequence of SEQ ID NO: 9 of the current instant application (see sequence alignment below).
Query Match 100.0%; Score 898; Length 488;
Best Local Similarity 100.0%;
Matches 173; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 LNFSRASEHRNEKGERISMINPRVVLDENGISHRSRYFIMLCDNETAIA HAKKTSIWAVK 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 316 LNFSRASEHRNEKGERISMINPRVVLDENGISHRSRYFIMLCDNETAIA HAKKTSIWAVK 375
Qy 61 KDSSKRISDAYKKASVYFIFVAQQTYNALGYAQVVSDLNSTELPFWSDSSHAGGVRIKWI 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 376 KDSSKRISDAYKKASVYFIFVAQQTYNALGYAQVVSDLNSTELPFWSDSSHAGGVRIKWI 435
Qy 121 KTCNLFSAEISEIVSHMDHGSEARDGMEMMYDEGSRLCTLINYAIMKRIGRDR 173
|||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 436 KTCNLFSAEISEIVSHMDHGSEARDGMEMMYDEGSRLCTLINYAIMKRIGRDR 488
It would have been obvious to one of ordinary skill in the art of protein expression and purification before the effective filing date of the current instant application to use the Schizosachcaromyces pombe Mmi1 taught by ‘SCHPO as the protein tag in the method for purifying a protein of interest taught by Xie and Touat-Todeschini. One of ordinary skill in the art would be motivated to do so from the teachings of ‘SCHPO who teach an Mmi1 protein comprising the 173 C-terminal residues comprising SEQ ID NO: 9 (which has the inherent ability to bind to the UNAAAC nucleotide motif). One of ordinary skill in the art would further be motivated to use the Schizosaccharomyces pombe Mmi1 taught by ‘SCHPO as a tag fused to GST taught by Xie in order to provide an affinity tag that would bind to the affinity ligand, UNAAAC, in the protein purification method taught by Xie and Touat-Todeschini to achieve the affinity purification of the GST-Mmi1 fusion protein. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Xie, Touat-Todeschini, and ‘SCHPO who provide all the teachings, reagents, and methods needed to do so.
With regards to claim 10, neither Xie nor Touat-Todeschini specifically teach that the protein tag contains at least one domain of amino acid sequence: RXaa34EKPKXaa35RAXaa36TPPP (SEQ ID NO: 18), where Xaa34 represents a lysine or arginine residue, Xaa35 represents an alanine, proline, or threonine residue, and Xaa36 represents a serine or proline residue.
However, ‘SCHPO teaches an Mmi1 protein from Schizosaccaromyces pombe that contains an amino acid sequence of SEQ ID NO: 18 of the current instant application (see sequence alignment below).
Query Match 100.0%; Score 65; Length 480;
Best Local Similarity 78.6%;
Matches 11; Conservative 3; Mismatches 0; Indels 0; Gaps 0;
Qy 1 RXEKPKXRAXTPPP 14
|:||||:||:||||
Db 293 RKEKPKPRAPTPPP 306
In the alignment, the Schizosaccaromyces pombe Mmi1 taught by ‘SCHPO has lysine at Xaa34, proline at Xaa35 and proline at Xaa36.
It would have been one of ordinary skill in the art of protein expression and purification before the effective filing date of the current instant application to use the Schizosaccharomyces pombe Mmi1 taught by ‘SCHPO as the protein tag in the method for purifying a protein of interest taught by Xie and Touat-Todeschini. One of ordinary skill in the art would be motivated to do so from the teachings of ‘SCHPO who teaches a Mmi1 protein containing at least one domain of amino acid SEQ ID NO: 18 and has lysine at position Xaa34, proline at position Xaa35, and proline at position Xaa36) which has the inherent ability to bind to the UNAAAC nucleotide motif.
One of ordinary skill in the art would further be motivated to use the Schizosaccharomyces pombe Mmi1 taught by’ ‘SCHPO as a tag fused to GST taught by Xie in order to provide an affinity tag that would bind to the affinity ligand, UNAAAC, in the protein purification method taught by Xie and Touat-Todeschini to achieve the affinity purification of the GST-Mmi1 fusion protein. One of ordinary skill in the art would have expectations of success in doing so from the combined teachings of Xie, Touat-Todeschini, and ‘SCHPO who provide all the teachings, reagents, and methods needed to do so.
Claims 8-10 are rejected under 35 U.S.C. 103 as being unpatentable over Xie et al. (Nature Communications, Vol. 10:251; published January 16, 2019; PMID: 30651569) in view of Touat-Todeschini et al. (The EMBO Journal, Vol. 17, pg. 2627-2641; published online August 1, 2017; PMID: 28765164) as applied to claim 1 above, and further in view of UniProt Database entry (MMI1_SCHPO, first entry: May 5, 2009).
Conclusion
No claims are allowed.
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/GEORGE THEMISTOCLIS LOUNTOS/ Examiner, Art Unit 1652
/ROBERT B MONDESI/ Supervisory Patent Examiner, Art Unit 1652
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