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 .
Status of the Claims
Claims 5-7 and 14 are pending (claim set as filed on 1/4/2024). Claims 1-4 and 11-13 were withdrawn after restriction/election requirement. Applicant does not specify that claim 8 was withdrawn after restriction/election requirement. However, Group I (claims 5-7 and 14) was elected for prosecution, and therefore claim 8 is not being considered for examination. Claims 9-10 were cancelled.
Election/Restrictions
Claims 1-4 and 11-13 withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected method, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 3/6/2026.
Priority
Acknowledgment is made of applicant’s claim for foreign priority under 35 U.S.C. 119 (a)-(d). Applicant is advised of possible benefits under 35 U.S.C. 119(a)-(d) and (f), wherein an application for patent filed in the United States may be entitled to claim priority to an application filed in a foreign country. This application filed on 1/4/2024 claims benefits to parent Application No. 202111468092.2, filed on 12/3/2021.
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
However, the applicant cannot rely upon the certified copy of the foreign priority application to overcome this rejection because a translation of said application has not been made of record in accordance with 37 CFR 1.55. When an English language translation of a non-English language foreign application is required, the translation must be that of the certified copy (of the foreign application as filed) submitted together with a statement that the translation of the certified copy is accurate. See MPEP §§ 215 and 216.
To claim benefit to the earlier filing date of 12/3/2021, the applicant must provide a certified English translation of the application.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 4/9/2024 and 9/24/2024 are considered, initialed, and attached hereto. The submissions are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Claim Objections
Claim 7 is objected to because of the following informalities: the claims recites “set forth in SEQ ID NO”. It is suggested the claim is amended to “ “the nucleotide sequence of SEQ ID Nos”.
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.
Claims 5-7 and 14 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
The invention appears to employ novel biological materials, specifically a genetically engineered Escherichia coli BL21 (DE3) strain that expresses a fucosyltransferase enzyme (NCBI Accession Number RTL12957.1 or WP 120175093.1) and a bifunctional enzyme (NCBI Accession Number WP 010993080.1). Since the biological materials are essential to the claimed invention they must be obtainable by a repeatable method set forth in the specification or otherwise readily available to the public. If the biological materials are not so obtainable or available, the requirements of 35 U.S.C. § 112 may be satisfied by a deposit of the biological materials.
If the deposit is made under the Budapest Treaty, then an affidavit or declaration by Applicant, or a statement by an attorney of record over his or her signature and registration number, stating that the specific biological materials have been deposited under the Budapest Treaty and that the biological materials will be irrevocably and without restriction or condition released to the public upon the issuance of a patent, would satisfy the deposit requirement made herein. If the deposit has not been made under the Budapest Treaty, then in order to certify that the deposit meets the criteria set forth in 37 C.F.R. §§ 1.801-1.809, Applicant may provide assurance of compliance by an affidavit or declaration, or by a statement by an attorney of record over his or her signature and registration number, showing that:
(a) during the pendency of this application, access to the invention will be afforded to
the Commissioner upon request;
(b) all restrictions upon availability to the public will be irrevocably removed upon
granting of the patent;
(c) the deposit will be maintained in a public depository for a period of 30 years or 5
years after the last request or for the effective life of the patent, whichever is longer;
(d) a test of the viability of the biological material at the time of deposit will be made
(see 37 C.F.R. § 1.807); and
(e) the deposit will be replaced if it should ever become inviable.
Applicant's attention is directed to M.P.E.P. §2400 in general, and specifically to §2411.05, as well as to 37 C.F.R. § 1.809(d), wherein it is set forth that "the specification shall contain the accession number for the deposit, the date of the deposit, the name and address of the depository, and a description of the deposited material sufficient to specifically identify it and to permit examination." The specification should be amended to include this information; however, Applicant is cautioned to avoid the entry of new matter into the specification by adding any other information.
Claims 6-7 and 14 are rejected for being dependent on claim 5.
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 5-7 and 14 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.
Claim 5 recites “an enzyme corresponding to the NCBI Accession Number” which is a relative phrase that renders the claim indefinite as it is unclear how one would ascertain the degree of similarity of one enzyme to the accessioned enzyme set forth in the claim. The specification does not provide a standard for measuring the requisite degree of “corresponding to”, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention as it could be an enzyme with any percent identity match to the accessioned enzyme. Claims 6-7 and 14 are rejected for depending on claim 5.
Claim 6 recites “the genetically engineered bacterium is an engineered E. coli or yeast”. The language renders the claim indefinite as it is unclear whether the yeast is supposed to be considered a genetically engineered bacterium.
Claims 6 and 7 recite the word “preferably” which renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Claims 6 and 14 recite the term “DE3” in parentheses. It is unclear if D3 is a synonym for strain E.coli BL21. The use of parentheses does not further limit the claims and can introduce semantic ambiguity into the meaning of the claims. Further clarification is requested.
Claim 7 recites the word “more preferably” which renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Claim 7 recites the phrase "such as" which renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d). This renders the gene encoding 3-galactosidase, the genes encoding L-fucose isomerase and/or L-fuculokinase, and the gene encoding UDP-glucose lipid carrier transferase as indefinite by the use of this term.
Claim Rejections - 35 USC § 102/103
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 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)(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.
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 5-7 and 14 are rejected under 35 U.S.C. 102(a)(2) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Parschat (European Patent Application No.EP3425052A1 – date of patent 1/9/2019).
Parschat’s general disclosure relates to fucosyl transferases and fucosylated oligosaccharides (see abstract).
Regarding claim 5, Parschat teaches a genetically engineered bacteria (see [0076-0077]) that expresses a fucosyltransferase (see 0079]), wherein the fucosyltransferase has α-1,2-fucosyltransferase activity (see [00147]). Parschat teaches the fucosyltransferase transfers a fucosyl group of a donor to an oligosaccharide receptor (see 0031]). Parschat also teaches the genetically engineered bacteria expresses a bifunctional enzyme with L-fucokinase and L-fucose-1-phosphate-guanyltransferase activity (see [0083]).
Parschat does not specify that the fucosyltransferase corresponds to NCBI Accession No. RTL12957.1 or WP_120175093.1, or that the bifunctional enzyme corresponds to NCBI Accession No. WP_010993080.1. However, it teaches a fucosyltransferase and a bifunctional enzyme that appear to have the same functions of transferring a fucosyl group from a donor to an oligosaccharide receptor (see 0031]) and of having L-fucokinase and L-fucose-1-phosphate-guanyltransferase activity (see [0083]), respectively. Therefore, Parschat either teaches the same or an obvious variant unless indicated otherwise.
Alternatively, it would be obvious to one of ordinary skill in the arts before the effective filing date to substitute the fucosyltransferase enzyme corresponding to NCBI Accession No. RTL12957.1 or WP_120175093.1 for the fucosyltransferase enzyme as taught in Parschat. One would be motivated to do so because Parschat teaches the fucosyltransferase in the genetically engineered bacteria has the same function of transferring a fucosyl group from a donor to an oligosaccharide receptor (see Parschat [0031]) as the claimed fucosyltransferase (see specification pg. 5, ¶ 2). So it would be prima facie obvious to do a simple substitution of one fucosyltransferase for another and one would have had a reasonable expectation of success in doing so.
Also it would be obvious to one of ordinary skill in the arts before the effective filing date to substitute the bifunctional enzyme corresponding to NCBI Accession No. WP_010993080.1 for the bifunctional enzyme as taught in Parschat. One would be motivated to do so as Parschat teaches the bifunctional enzyme in the genetically engineered bacteria has the same function of having L-fucokinase and L-fucose-1-phosphate-guanyltransferase activity (see Parschat [0083]) as the claimed bifunctional enzyme (see specification pg. 5, ¶ 6). So it would be prima facie obvious to do a simple substitution of one bifunctional enzyme for another and one would have had a reasonable expectation of success in doing so.
Regarding claim 6, Parschat teaches the oligosaccharide receptor is lactose (see [0092]), the fucosylated oligosaccharide is 2’-fucosyllactose (see [0130]), the donor is guanosine-diphosphate L-fucose (see [0031]), and the engineered bacteria is E.coli BL21 (DE3) strain (see [0147]).
Regarding claim 7, Parschat teaches the nucleotide sequence of fucosyltransferase is set forth in SEQ ID NOs: 2 (see pg. 94, claim 4) and 5 (see pg. 94, claim 4). Parschat teaches that the nucleotide sequence of the bifunctional enzyme is set forth in SEQ ID NO: 10 (see [0159]). As the applicant does not define the meaning of the term “set forth” in the specification of the instant application, it can be reasonably interpreted that since the enzymes were found to align to some degree with the enzyme sequences taught in Parschat, that they were set forth in SEQ ID NOs: 2, 5, and 10. Parschat teaches the precursor to the donor is L-fucose and the donor is guanosine diphospho-fucose (see [0083]). Parschat also teaches the following genes were knocked out: lacZ (see [0091]), wacJ (see [0086]), FucI and FucK (see [0087]).
Regarding claim 14, Parschat teaches the engineered bacteria is E.coli BL21 (DE3) strain (see [0147]). Parschat also teaches the following genes were knocked out: lacZ (see [0091]), wacJ (see [0086]), FucI and FucK (see [0087]).
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 5-7 and 14 are rejected under 35 U.S.C. 103 as being unpatentable over Chin (Chin et al., “Enhanced production of 2’-fucosyllactose in engineered Escherichia coli BL21star(DE3) by modulation of lactose metabolism and fucosyltransferase”, 2015 Jun 26, Journal of Biotechnology, 210, pgs. 107-110), in view of Parschat (Pre-Grant Publication No. EP3425052A1 – date of patent 1/9/2019).
Chin’s general disclosure relates to the expression of fucosyltransferase in a genetically engineered bacterium (see abstract).
Regarding claim 5, Chin teaches a genetically engineered bacterium expressing fucosyltransferase wherein the fucosyltransferase has α-1,2-fucosyltransferase activity (see Chin abstract). Chin teaches the fucosyltransferase catalyzes the transfer of a fucosyl group of L-fucose from a guanosine diphospho-fucose (abbreviated to GDP-L-fucose) donor to a lactose oligosaccharide receptor (see Chin pg. 107, ¶ 3). GDP-L-fucose is reasonably interpreted to be a nucleotide-activated donor as GDP-L-fucose is embodied as a donor in the specification of the instant application (see specification pg. 2, ¶ 6).
However, Chin does not teach the bacterium expresses a bifunctional enzyme with L-fucokinase and fucose-1-phosphate guanyltransferase activities.
Parschat’s general disclosure relates to fucosyl transferases and fucosylated oligosaccharides (see abstract).
Regarding claim 5, Parschat teaches the genetically engineered bacteria expresses a bifunctional enzyme with L-fucokinase and L-fucose-1-phosphate-guanyltransferase activity (see [0083]).
It would be obvious to one of ordinary skill in the art before the effective filing date to add the bifunctional enzyme as taught in Parschat to the engineered bacterium as taught in Chin. Motivation to do so would be because Parschat teaches the bifunctional enzyme converts the L-fucose precursor to the GDP-L-fucose donor in the process of producing fucosylated oligosaccharides (see Parschat [0083]). This addition would be an advantage in Chin which discloses a need for the overexpression of GDP-L-fucose and the bifunctional enzyme in Parschat would provide an increase in available GDP-L-fucose from overexpression of the bifunctional enzyme (see Parschat [0083]).
Parschat does not specify that the fucosyltransferase enzyme corresponds to NCBI Accession No. RTL12957.1 or WP_120175093.1, or that the bifunctional enzyme corresponds to NCBI Accession No. WP_010993080.1.
However, it would be obvious to one of ordinary skill in the arts before the effective filing date to substitute the fucosyltransferase enzyme corresponding to NCBI Accession No. RTL12957.1 or WP_120175093.1 for the fucosyltransferase enzyme as taught in Parschat. One would be motivated to do so because Parschat teaches the fucosyltransferase in the genetically engineered bacteria has the same function of transferring a fucosyl group from a donor to an oligosaccharide receptor (see Parschat [0031]) as the claimed fucosyltransferase (see specification pg. 5, ¶ 2). So it would be prima facie obvious to do a simple substitution of one fucosyltransferase for another and one would have had a reasonable expectation of success in doing so.
Also, it would be obvious to one of ordinary skill in the arts before the effective filing date to substitute the bifunctional enzyme corresponding to NCBI Accession No. WP_010993080.1 for the bifunctional enzyme as taught in Parschat. One would be motivated to do so as Parschat teaches the bifunctional enzyme in the genetically engineered bacteria has the same function of having L-fucokinase and L-fucose-1-phosphate-guanyltransferase activity (see Parschat [0083]) as the claimed bifunctional enzyme (see specification pg. 5, ¶ 6). So it would be prima facie obvious to do a simple substitution of one bifunctional enzyme for another and one would have had a reasonable expectation of success in doing so.
Regarding claim 6, Chin teaches the oligosaccharide receptor is lactose (see pg. 107, ¶ 3), the fucosylated oligosaccharide is 2’fucosyllactose (see abstract), the donor is GDP-L-fucose (see pg. 107, ¶ 3), and the genetically engineered bacterium is E. coli BL21 (DE3) strain (see abstract).
Regarding claim 7, Chin teaches in the genetically engineered bacterium the oligosaccharide receptor is lactose (see pg. 107, ¶ 3) and the whole endogenous lactose operon, which includes a lacZ gene, is knocked out by deletion (see abstract). Chin also teaches that the donor is GDP-L-fucose (see pg. 107, ¶ 3) and the precursor is L-fucose (see pg. 107, ¶ 3).
Regarding claim 14, Chin the genetically engineered bacterium is E. coli BL21 (DE3) (see abstract). Chin also teaches that the whole endogenous lactose operon, which includes a lacZ gene, is knocked out by deletion (see abstract).
Chin does not teach that the nucleotide sequence of fucosyltransferase is set forth in SEQ ID NOs: 2 and 5, that the nucleotide sequence of the bifunctional enzyme is set forth in SEQ ID NO: 10, or that the genes wacJ, FucI, and FucK were knocked out.
Regarding claim 7, Parschat teaches the nucleotide sequence of fucosyltransferase is set forth in SEQ ID NOs: 2 (see pg. 94, claim 4) and 5 (see pg. 94, claim 4). Parschat teaches that the nucleotide sequence of the bifunctional enzyme is set forth in SEQ ID NO: 10 (see [0159]). As the applicant does not define the meaning of the term “set forth” in the specification of the instant application, it can be reasonably interpreted that since the enzymes were found to align to some degree with the enzyme sequences taught in Parschat such as 26.2%, 16.3%, and 99.8%, that they were set forth in SEQ ID NOs: 2, 5, and 10 respectively.
It would be obvious to one of ordinary skill in the arts before the effective filing date to substitute the fucosyltransferase enzyme set forth in SEQ ID NOs: 2 and 5 for the fucosyltransferase enzyme as taught in Parschat. One would be motivated to do so because Parschat teaches the fucosyltransferase in the genetically engineered bacteria has the same function of transferring a fucosyl group from a donor to an oligosaccharide receptor (see Parschat [0031]) as the claimed fucosyltransferase (see specification pg. 5, ¶ 2). So it would be prima facie obvious to do a simple substitution of one fucosyltransferase for another and one would have had a reasonable expectation of success in doing so.
It would also be obvious to one of ordinary skill in the arts before the effective filing date to substitute the bifunctional enzyme set forth in SEQ ID NO: 10 for the bifunctional enzyme as taught in Parschat. One would be motivated to do so as Parschat teaches the bifunctional enzyme in the genetically engineered bacteria has the same function of having L-fucokinase and L-fucose-1-phosphate-guanyltransferase activity (see Parschat [0083]) as the claimed bifunctional enzyme (see specification pg. 5, ¶ 6). So it would be prima facie obvious to do a simple substitution of one bifunctional enzyme for another and one would have had a reasonable expectation of success in doing so.
Regarding claim 7, Parschat teaches the following genes were knocked out: wacJ (see [0086]), FucI and FucK (see [0087]).
It would be obvious to one of ordinary skill in the art before the effective filing date to add the knockout of the FucI, FucK, and wacJ genes as taught in Parschat to the lacZ gene knockout in the genetically engineered bacterium as taught in Chin. One would be motivated to do so because Parschat teaches that knocking out these three genes increases the yield of the synthesized 2’-fucosyllactose by increasing the amount of available GDP-L-fucose donor and L-fucose precursor molecules (see Parschat [0086-0087]). This addition would be advantageous to the disclosure of Chin which teaches that the deletion of the lacZ gene was not enough to improve yield of 2’-fucosyllactose (see Chin pg. 110, ¶ 5), and therefore it would be within the skill of the ordinary artisan to add the knockout of additional genes meant to increase 2’-fucosyllactose accumulation to improve upon Chin’s method.
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 5-7 and 14 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 5 of copending Application No. 18/576,585 in view of Parschat - reference cited from above and reprised herein.
This is a provisional nonstatutory double patenting rejection. Although the claims at issue are
not identical, they are not patentably distinct from each other because:
Instant claims are directed towards:
Genetically engineered bacterium wherein the strain is E. coli BL21 (DE3) (claims 5-7 and 14)
The bacterium expresses fucosyltransferase which has α-1,2-fucosyltransferase activity (claim 5 and 7)
Wherein the genes lacZ, wacJ, FucI, and FucK are knocked out (claims 7 and 14)
Co-pending Application No. 18/576,585 claims are directed towards:
Genetically engineered bacterium wherein the strain is E. coli BL21 (DE3) (claims 1 and 5)
The bacterium expresses fucosyltransferase which has FucT (α-1,2-fucosyltransferase) activity (claim 1)
Wherein the genes lacZ, wacJ, FucI, and FucK are knocked out (claim 1)
Although the preambles are different, both sets of claims are directed to a genetically engineered bacterium that expresses fucosyltransferase and wherein the genes lacZ, wacJ, FucI, and FucK are knocked out. Copending Application No. 18/576,585 does not recite:
The bacterium expresses the bifunctional enzyme
The fucosyltransferase corresponds to NCBI Accession No. RTL12957.1 or WP_120175093.1
The bifunctional enzyme corresponds to NCBI Accession No. WP_010993080.1
Parschat teaches a bifunctional enzyme (see [0083]).
It would be obvious to one of ordinary skill in the arts before the effective filing date to add the expression of the bifunctional enzyme to the genetically engineered bacteria. One would be motivated to do so because Parschat teaches the bifunctional enzyme converts the L-fucose precursor to the GDP-L-fucose donor in the process of producing fucosylated oligosaccharides (see Parschat [0083]). This addition would be beneficial in ‘585 which discloses a method to produce 2’-fucosyllatose by adding L-fucose precursor to the fermentation medium (see ‘585 [0021]), and where the addition of a bifunctional enzyme could facilitate the process.
Parschat does not specify that the fucosyltransferase enzyme corresponds to NCBI Accession No. RTL12957.1 or WP_120175093.1, or that the bifunctional enzyme corresponds to NCBI Accession No. WP_010993080.1.
However, it would be obvious to one of ordinary skill in the arts before the effective filing date to substitute the fucosyltransferase enzyme corresponding to NCBI Accession No. RTL12957.1 or WP_120175093.1 for the fucosyltransferase enzyme as taught in Parschat. One would be motivated to do so because Parschat teaches the fucosyltransferase in the genetically engineered bacteria has the same function of transferring a fucosyl group from a donor to an oligosaccharide receptor (see Parschat [0031]) as the claimed fucosyltransferase (see specification pg. 5, ¶ 2). So it would be prima facie obvious to do a simple substitution of one fucosyltransferase for another and one would have had a reasonable expectation of success in doing so.
Also it would be obvious to one of ordinary skill in the arts before the effective filing date to substitute the bifunctional enzyme corresponding to NCBI Accession No. WP_010993080.1 for the bifunctional enzyme as taught in Parschat. One would be motivated to do so as Parschat teaches the bifunctional enzyme in the genetically engineered bacteria has the same function of having L-fucokinase and L-fucose-1-phosphate-guanyltransferase activity (see Parschat [0083]) as the claimed bifunctional enzyme (see specification pg. 5, ¶ 6). So it would be prima facie obvious to do a simple substitution of one bifunctional enzyme for another and one would have had a reasonable expectation of success in doing so.
Conclusion
No claims are allowed.
Correspondence Information
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/E.R.W./ Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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