DETAILED CORRESPONDENCE
Application 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. Applicant’s amendment to the claims filed on 08/21/2025 in response to the Non-Final Rejection mailed on 04/23/2025 is acknowledged. This listing of claims replaces all prior listings of claims in the application.
3. Claims 10-12 are cancelled.
4. Claims 8, 13, 16-24, 27-28 are pending.
5. Applicants’ confirmation of election without traverse of claims 8, 13, 16-19, 27 and 28 in the response filed on 08/21/2025 is acknowledged.
Claims 20-24 stand withdrawn pursuant to 37 CFR 1.142(b).
6. Applicant’s remarks filed on 08/21/2025 in response to the Non-Final Rejection mailed on 04/23/2025 have been fully considered and are deemed persuasive to overcome at least one of the rejections and/or objections as previously applied.
The text of those sections of Title 35 U.S. Code not included in the instant action can be found in the prior Office Action.
Information Disclosure Statement
7. The IDSs filed on 08/29/2025 and 09/09/2025 have been considered by the examiner and copies of the Form PTO/SB/08 are attached to the office action.
Specification
8. The objection to the disclosure for embedded hyperlink is withdrawn in view of applicants’ amendment to the specification to remove said hyperlink.
Claim Rejections - 35 USC § 112(b)
9. The rejection of claims 16-19 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, for indefiniteness is withdrawn in view of applicants’ amendment to claim 16 to recite “a fusion protein of claim 8”.
Claim Rejections - 35 USC § 112(a)
10. The written description rejection of claims 8, 10-13, 16-19, and 27-28 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, is withdrawn in view of applicants’ amendment to the claims to recite “wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300”, and in view of the cancellation of claims 10-12.
11. The scope of enablement rejection of claims 8, 10-13, 16-19, and 27-28 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, is withdrawn in view of applicants’ amendment to the claims to recite “wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300”, and in view of the cancellation of claims 10-12.
Claim Rejections - 35 USC § 103
12. The rejection of 8, 10-13, 16-19, and 27-28 under 35 U.S.C. 103 as being unpatentable over Thompson et al. (US Patent Application Publication 2016/0108096; cited on IDS filed on 05/31/2024) in view of Wilting et al. (WO 01/64853; cited on PTO-892 mailed 04/23/2025) is withdrawn in view of applicants’ amendment to the claims to recite “wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300”, and in view of the cancellation of claims 10-12.
13. Claims 8, 13, 16-19 and 27-28 are newly rejected under 35 U.S.C. 103 as being unpatentable over Thompson et al. (US Patent Application Publication 2016/0108096; cited on IDS filed on 05/31/2024) in view of Kyung et al. (KR 20110069968, 06/24/2011, examiner cited with machine translation attached). This new grounds of rejection is necessitated by applicants’ amendment to the claims to recite “wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300”.
14. As amended, claims 8, 10-12, and 27-28 are drawn to a fusion protein comprising: (A) a targeting sequence, exosporium protein, or exosporium protein fragment that targets the fusion protein to the exosporium of a recombinant Bacillus cereus family member; and (B) an enzyme, wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300.
Claim 13 is drawn to a fusion protein of claim 8, wherein the glucanase comprises an amino acid sequence having at least 95%, at least 98%, at least 99%, or 100% identity to SEQ ID NO: 300.
Claim 16 is drawn to a recombinant Bacillus cereus family member that expresses a fusion protein of claim 8.
Claims 17 and 19 are drawn to exosporium fragments derived from a recombinant Bacillus cereus family member of claim 16.
Claim 18 is drawn to a formulation comprising a recombinant Bacillus cereus family member of claim 16 or exosporium fragments derived from a recombinant Bacillus cereus family member of claim 16 and an agriculturally acceptable carrier.
15. With respect to claim 8, Thompson et al. teach fusion proteins comprising a targeting sequence, an exosporium protein, or an exosporium protein fragment that targets the fusion protein to the exosporium of a Bacillus cereus family member fused to a protein of interest such as an enzyme, wherein the peptide of interest can be an enzyme such as a cellulase and wherein the proteins can be used in a variety of process such as industrial cleaning [see Abstract; paragraphs 0003-0008; paragraphs 0806, 0847, 0874-0875; 0990]. Thompson et al. teach the fusion protein wherein the enzyme is from a Bacillus, such as Bacillus licheniformis, or Paenibacillus [see paragraphs 0641 and 0650].
With respect to claim 10, Thompson et al. teach the fusion protein wherein the enzyme is a beta-1,4-glucanase [see paragraph 0488].
With respect to claim 16, Thompson et al. teach a recombinant Bacillus cereus family member that expresses the fusion protein [see Abstract; paragraphs 0003-0008].
With respect to claim 17, Thompson et al. teach exosporium fragments derived from a recombinant Bacillus cereus family member [see Abstract; paragraphs 0003-0008].
With respect to claims 18 and 19, Thompson et al. teach a formulation comprising a recombinant Bacillus cereus family member or exosporium fragments derived from a recombinant Bacillus cereus family member and an agriculturally acceptable carrier [see Abstract; paragraphs 0003-0008, 0028; 0621].
With respect to claims 27 and 28, Thompson et al. teach fusion proteins comprising a targeting sequence, an exosporium protein, or an exosporium protein fragment that targets the fusion protein to the exosporium of a Bacillus cereus family member fused to a protein of interest such as an enzyme, wherein the peptide of interest can be an enzyme is a endoglucanase, wherein the enzyme is a beta-1,4-glucanase and wherein the proteins can be used in a variety of process such as industrial cleaning [see Abstract; paragraphs 0003-0008; 0488; paragraphs 0847, 0874-0875; 0990].
However, Thompson et al. does not teach the fusion protein of claim 8, wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300; the fusion protein of claim 13, wherein the glucanase comprises an amino acid sequence having at at least 95%, at least 98%, at least 99%, or 100% identity to SEQ ID NO: 300; the fusion protein of claim 27, wherein the fusion protein comprises a signal peptide comprising SEQ ID NO: 340 at its amino terminus; or the fusion protein comprises a signal peptide comprising SEQ ID NO: 339 at its amino terminus; and the fusion protein of claim 28, wherein the enzyme further comprises a signal peptide.
Kyung et al. teach cold-active cellulases from Bacillus that exhibit activity at low temperatures comprising an amino acid sequence that is 100% identical to SEQ ID NO: 300 and a signal peptide that is 100% identical to SEQ ID NO: 340 that is useful in the food, paper, and fermentation industries [see Abstract; p. 4 of translation and alignment attached as APPENDIX A].
Before the effective filing date of the claimed invention, it would have been obvious for one of ordinary skill in the art to combine the teachings of Thompson et al. and Kyung et al. to fuse the cellulase of Kyung et al. to the exosporium proteins of Thompson et al. because Thompson et al. teach fusion proteins comprising cellulases for industrial cleaning compositions. Kyung et al. teach cold-active cellulases from Bacillus that exhibit activity at low temperatures comprising an amino acid sequence that is 100% identical to SEQ ID NO: 300 and a signal peptide that is 100% identical to SEQ ID NO: 340 that is useful in the food, paper, and fermentation industries. One of ordinary skill in the art would have had a reasonable expectation of success, a reasonable level of predictability and would have been motivated to combine the teachings of Thompson et al. and Kyung et al. because Kyung et al. acknowledges these cellulases are useful in the food, paper, and fermentation industries where low temperatures are necessary. Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
Response to Remarks Regarding Prior Art Rejections
16. Applicants’ remarks filed on 08/21/2025 have been fully considered by the examiner and are rendered moot in view of the new rejection set forth above, which is necessitated by applicants’ amendment.
Regarding applicants’ remarks on p. 14 that the claimed fusion proteins yield unexpected results to stimulate plant growth, this argument is found to be not persuasive because MPEP 2145.II states “[m]ere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention. In re Wiseman, 596 F.2d 1019, 201 USPQ 658 (CCPA 1979) (Claims were directed to grooved carbon disc brakes wherein the grooves were provided to vent steam or vapor during a braking action. A prior art reference taught noncarbon disc brakes which were grooved for the purpose of cooling the faces of the braking members and eliminating dust. The court held the prior art references when combined would overcome the problems of dust and overheating solved by the prior art and would inherently overcome the steam or vapor cause of the problem relied upon for patentability by applicants. Granting a patent on the discovery of an unknown but inherent function (here venting steam or vapor) "would remove from the public that which is in the public domain by virtue of its inclusion in, or obviousness from, the prior art." 596 F.2d at 1022, 201 USPQ at 661.); In re Baxter Travenol Labs., 952 F.2d 388, 21 USPQ2d 1281 (Fed. Cir. 1991) (Appellant argued that the presence of DEHP as the plasticizer in a blood collection bag unexpectedly suppressed hemolysis and therefore rebutted any prima facie showing of obviousness. However, the closest prior art utilizing a DEHP plasticized blood collection bag inherently achieved same result, although this fact was unknown in the prior art.).”
Double Patenting
17. The nonstatutory double patenting rejection of claims 8, 10-13, 16-19, 27-28 over claims 1-27, 52-57, 70-78, 86-117, and 138-148 of U.S. Patent No. 9,845,342 in view of Wilting et al. (WO 01/64853; cited on PTO-892 mailed 04/23/2025) is withdrawn in view of applicants’ amendment to the claims to recite “wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300” and to cancel claims 10-12.
18. The nonstatutory double patenting rejection of claims 8, 10-13, 16-19, and 27-28 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-14, 18-19, and 32-34 U.S. Patent No. 10,836,800 in view of (WO 01/64853; cited on PTO-892 mailed 04/23/2025) is withdrawn in view of applicants’ amendment to the claims to recite “wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300” and to cancel claims 10-12.
19. Claims 8, 13, 16-19, and 27-28 are newly rejected on the grounds of nonstatutory double patenting as being unpatentable over claims 1-27, 52-57, 70-78, 86-117, and 138-148 of U.S. Patent No. 9,845,342 in view of Kyung et al. (KR 20110069968, 06/24/2011, examiner cited with machine translation attached). This new grounds of rejection is necessitated by applicants’ amendment to the claims to recite “wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300”.
Claims 1-27, 52-57, 70-78, 86-117, and 138-148 recite a recombinant Bacillus cereus family member that expresses a fusion protein comprising: at least one protein or peptide of interest; a targeting sequence, exosporium protein, or exosporium protein fragment that targets the fusion protein to the exosporium of the recombinant Bacillus cereus family member; and an amino acid linker between the targeting sequence, the exosporium protein, or the exosporium protein fragment and the protein or peptide of interest, wherein the linker comprises a polyalanine linker, or polyglycine linker, or a linker comprising a mixture of both alanine and glycine resides; and wherein the recombinant Bacillus cereus family member comprises a mutation that results in Bacillus cereus family member spores having an exosporium that is easier to remove from the spore as compared to the spore of a wile-type spore.
However, the claims of the ‘342 patent do not recite the fusion protein of claim 8, wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300; the fusion protein of claim 13, wherein the glucanase comprises an amino acid sequence having at at least 95%, at least 98%, at least 99%, or 100% identity to SEQ ID NO: 300; the fusion protein of claim 27, wherein the fusion protein comprises a signal peptide comprising SEQ ID NO: 340 at its amino terminus; or the fusion protein comprises a signal peptide comprising SEQ ID NO: 339 at its amino terminus; and the fusion protein of claim 28, wherein the enzyme further comprises a signal peptide.
Kyung et al. teach cold-active cellulases from Bacillus that exhibit activity at low temperatures comprising an amino acid sequence that is 100% identical to SEQ ID NO: 300 and a signal peptide that is 100% identical to SEQ ID NO: 340 that is useful in the food, paper, and fermentation industries [see Abstract; p. 4 of translation and alignment attached as APPENDIX A].
Before the effective filing date of the claimed invention, it would have been obvious for one of ordinary skill in the art to combine the recitations of the ‘342 patent and Kyung et al. to fuse the cellulase of Kyung et al. to the exosporium proteins of the ‘342 patent because the ‘342 patent recite fusion proteins for industrial cleaning compositions. Kyung et al. teach cold-active cellulases from Bacillus that exhibit activity at low temperatures comprising an amino acid sequence that is 100% identical to SEQ ID NO: 300 and a signal peptide that is 100% identical to SEQ ID NO: 340 that is useful in the food, paper, and fermentation industries. One of ordinary skill in the art would have had a reasonable expectation of success, a reasonable level of predictability and would have been motivated to combine the recitations of the ‘342 patent and Kyung et al. because Kyung et al. acknowledges these cellulases are useful in the food, paper, and fermentation industries where low temperatures are necessary. Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
20. Claims 8, 13, 16-19, and 27-28 are newly rejected on the grounds of nonstatutory double patenting as being unpatentable over claims claims 1-14, 18-19, and 32-34 U.S. Patent No. 10,836,800 in view of Kyung et al. (KR 20110069968, 06/24/2011, examiner cited with machine translation attached). This new grounds of rejection is necessitated by applicants’ amendment to the claims to recite “wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300”.
Claims 1-14, 18-19, and 32-34 recite a recombinant Bacillus cereus family member that expresses a fusion protein comprising: at least one protein or peptide of interest; a targeting sequence, exosporium protein, or exosporium protein fragment that targets the fusion protein to the exosporium of the recombinant Bacillus cereus family member; and an amino acid linker between the targeting sequence, the exosporium protein, or the exosporium protein fragment and the protein or peptide of interest, wherein the linker comprises a polyalanine linker, or polyglycine linker, or a linker comprising a mixture of both alanine and glycine resides; and wherein the recombinant Bacillus cereus family member comprises a mutation that results in Bacillus cereus family member spores having an exosporium that is easier to remove from the spore as compared to the spore of a wile-type spore.
However, the claims of the ‘800 patent do not recite the fusion protein of claim 8, wherein the enzyme comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 300; the fusion protein of claim 13, wherein the glucanase comprises an amino acid sequence having at at least 95%, at least 98%, at least 99%, or 100% identity to SEQ ID NO: 300; the fusion protein of claim 27, wherein the fusion protein comprises a signal peptide comprising SEQ ID NO: 340 at its amino terminus; or the fusion protein comprises a signal peptide comprising SEQ ID NO: 339 at its amino terminus; and the fusion protein of claim 28, wherein the enzyme further comprises a signal peptide.
Kyung et al. teach cold-active cellulases from Bacillus that exhibit activity at low temperatures comprising an amino acid sequence that is 100% identical to SEQ ID NO: 300 and a signal peptide that is 100% identical to SEQ ID NO: 340 that is useful in the food, paper, and fermentation industries [see Abstract; p. 4 of translation and alignment attached as APPENDIX A].
Before the effective filing date of the claimed invention, it would have been obvious for one of ordinary skill in the art to combine the recitations of the patent and Kyung et al. to fuse the cellulase of Kyung et al. to the exosporium proteins of the ‘800 patent because the ‘800 patent recite fusion proteins for industrial cleaning compositions. Kyung et al. teach cold-active cellulases from Bacillus that exhibit activity at low temperatures comprising an amino acid sequence that is 100% identical to SEQ ID NO: 300 and a signal peptide that is 100% identical to SEQ ID NO: 340 that is useful in the food, paper, and fermentation industries. One of ordinary skill in the art would have had a reasonable expectation of success, a reasonable level of predictability and would have been motivated to combine the recitations of the ‘800 patent and Kyung et al. because Kyung et al. acknowledges these cellulases are useful in the food, paper, and fermentation industries where low temperatures are necessary. Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
Conclusion
17. Status of the claims:
Claims 8, 13, 16-24, 27-28 are pending.
Claims 20-24 stand withdrawn pursuant to 37 CFR 1.142(b).
Claims 8, 13, 16-19, and 27-28 are rejected.
No claims are in condition for an allowance.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to PAUL J HOLLAND whose telephone number is (571)270-3537. The examiner can normally be reached Monday to Friday from 8AM to 5PM.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath Rao can be reached at 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/PAUL J HOLLAND/Primary Examiner, Art Unit 1656
APPENDIX A
Kyung et al. with SEQ ID NO: 300
Query Match 100.0%; Score 1287; Length 232;
Best Local Similarity 100.0%;
Matches 232; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 ASSSNPSDKLYFKNKKYYIFNNVWGADQVSGWWQTIYHNSDSDMGWVWNWPSNTSTVKAY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 ASSSNPSDKLYFKNKKYYIFNNVWGADQVSGWWQTIYHNSDSDMGWVWNWPSNTSTVKAY 60
Qy 61 PSIVSGWHWTEGYTAGSGFPTRLSDQKNINTKVSYSISANGTYNAAYDIWLHNTNKASWD 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 PSIVSGWHWTEGYTAGSGFPTRLSDQKNINTKVSYSISANGTYNAAYDIWLHNTNKASWD 120
Qy 121 SAPTDEIMIWLNNTNAGPAGSYVETVSIGGHSWKVYKGYIDAGGGKGWNVFSFIRTANTQ 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SAPTDEIMIWLNNTNAGPAGSYVETVSIGGHSWKVYKGYIDAGGGKGWNVFSFIRTANTQ 180
Qy 181 SANLNIRDFTNYLADSKQWLSKTKYVSSVEFGTEVFGGTGQINISNWDVTVR 232
||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 SANLNIRDFTNYLADSKQWLSKTKYVSSVEFGTEVFGGTGQINISNWDVTVR 232
Kyung et al. with SEQ ID NO: 340
Query Match 100.0%; Score 148; Length 261;
Best Local Similarity 100.0%;
Matches 29; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MKNNHLLKSILLWGAVCIIVLAGPLSAFA 29
|||||||||||||||||||||||||||||
Db 1 MKNNHLLKSILLWGAVCIIVLAGPLSAFA 29