DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 8/12/2026 has been entered.
Applicant’s amendment of claim 1, 19, in the paper of 6/8/2026, is acknowledged. Applicants' arguments filed on 6/8/2026 have been fully considered and are deemed to be persuasive to overcome some of the rejections previously applied. Rejections and/or objections not reiterated from previous office actions are hereby withdrawn. Claims 1, 3, 4, 6-9, 11, 13, 14, 18, 19, 22-25 are still at issue and are present for examination.
Election/Restrictions
Applicant's election with traverse of the invention of Group 1, claims 1-9, 11, 15-21, to a DNase variant, in the paper of 1/14/2026, is acknowledged. Applicant's election with traverse of the following species:
Species Group 1: Y182H;
Species Group 2: S68;
Species Group 3: P in position 22, L in position 27, P in position 39, G in position 42, D in position 11;
Species Group 5: W57S;
in the paper of 1/14/2026, is acknowledged.
It is noted that applicants did not elect a species from Species groups 4, 6 and 7.
Claims 13, 14, 24 and 25 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species.
Claim Objections
Claims 3, 4, 6-8, 18, 19 are objected to because of the following informalities:
Claims 3, 4, 6-8, 18, 19 depend from rejected claim 1.
Appropriate correction is required.
Claim Rejections - 35 USC § 102
The rejection of claim(s) 1, 5, 9, 11, 15, 16, 17 under 35 U.S.C. 102(a)(1) as being anticipated by Beier et al. (WO 2018/011276) is withdrawn based upon applicants amendment of the claims in the paper of 6/8/2026.
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.
Claim(s) 1, 9, 11 is/are rejected under 35 U.S.C. 103 as being unpatentable over Beier et al. (WO 2018/011276) and Zhu et al. (Proceedings of the National Academy, Vol 113, No. 46, pp 12496-12951, Nov 2016).
Beier et al. (WO 2018/011276) teach Bacillus CIBI DNase variants and uses thereof. Beier et al. (WO 2018/011276) teach detergent compositions comprising DNase variants exhibiting alterations relative to the parent DNase in one or more properties including wash performance, detergent stability and/or storage stability. Beier et al. (WO 2018/011276) teach a DNase variant comprising the amino acid sequence of SEQ ID NO:1 (90.1% sequence identity to instant SEQ ID NO:1). Beier et al. (WO 2018/011276) teach the above DNase variant of SEQ ID NO:1 comprising a S82E, S82K, S82R and S82H substitutions (see page 2lines 22 thru 35 and supporting text).
Zhu et al. disclose analysis characterizing hydrophobicity of amino acid side chains in a protein environment via measuring contact angle of a water nanodroplet on planar peptide network. Zhu et al. teach that expectedly, all of the planar peptide networks with nonpolar amino acids are hydrophobic due to θ > 90°, whereas all of the planar peptide networks of the polar and charged amino acids are hydrophilic due to θ < 90°. Planar peptide networks of the charged amino acids exhibit complete-wetting behavior due to θ = 0. Zhu et al. disclose that the amino acids comprising charged side chains include histidine, lysine, glutamate, arginine and aspartate (Table 1, p 12948).
Before the effective filing date, one of ordinary skill in the art would have been motivated to make similar amino acid substitutions at position S82 of the DNase taught by Beier et al. as a means of identifying DNase variants with improved properties including wash performance, detergent stability and/or storage stability. The obvious amino acid substitutions include those amino acids with similar charged amino acid side chains as taught by Beier et al. which include histidine, lysine, glutamate and arginine (i.e. S82E, S82K, S82R and S82H). The obvious amino acids include other charged amino acids such as aspartate (i.e. S82D) as taught by Zhu et al.. The expectation of success is high based upon the high level of skill in the art of recombinant protein engineering as exemplified by the teachings of Beier et al. who teach all the methods required to make the obvious DNase variants.
Thus claim(s) 1, 9, 11 is/are rejected under 35 U.S.C. 103 as being unpatentable over Beier et al. (WO 2018/011276) and Zhu et al. (Proceedings of the National Academy, Vol 113, No. 46, pp 12496-12951, Nov 2016).
Claim(s) 1, 9, 11 is/are rejected under 35 U.S.C. 103 as being unpatentable over Oestergaard et al. (US 2019/0127664 and US 10,781,408) and Zhu et al. (Proceedings of the National Academy, Vol 113, No. 46, pp 12496-12951, Nov 2016).
Oestergaard et al. (US 2019/0127664 and US 10,781,408) teach Bacillus CIBI DNase variants and uses thereof. Oestergaard et al. (US 2019/0127664 and US 10,781,408) teach detergent compositions comprising DNase variants exhibiting alterations relative to the parent DNase in one or more properties including wash performance, detergent stability and/or storage stability. Oestergaard et al. (US 2019/0127664 and US 10,781,408) teach a DNase variant comprising the amino acid sequence of SEQ ID NO:1 (97% sequence identity to instant SEQ ID NO:1). Oestergaard et al. (US 2019/0127664 and US 10,781,408) teach the above DNase variant of SEQ ID NO:1 comprising a S82E, S82K, S82R and S82H substitutions (see claim 11 and supporting text).
Zhu et al. disclose analysis characterizing hydrophobicity of amino acid side chains in a protein environment via measuring contact angle of a water nanodroplet on planar peptide network. Zhu et al. teach that expectedly, all of the planar peptide networks with nonpolar amino acids are hydrophobic due to θ > 90°, whereas all of the planar peptide networks of the polar and charged amino acids are hydrophilic due to θ < 90°. Planar peptide networks of the charged amino acids exhibit complete-wetting behavior due to θ = 0. Zhu et al. disclose that the amino acids comprising charged side chains include histidine, lysine, glutamate, arginine and aspartate (Table 1, p 12948).
Before the effective filing date, one of ordinary skill in the art would have been motivated to make similar amino acid substitutions at position S82 of the DNase taught by Oestergaard et al. (SEQ ID NO:28) as a means of identifying DNase variants with improved properties including wash performance, detergent stability and/or storage stability. The obvious amino acid substitutions include those amino acids with similar charged amino acid side chains as taught by Oestergaard et al. which include histidine, lysine, glutamate and arginine (i.e. S82E, S82K, S82R and S82H). The obvious amino acids include other charged amino acids such as aspartate (i.e. S82D) as taught by Zhu et al.. The expectation of success is high based upon the high level of skill in the art of recombinant protein engineering as exemplified by the teachings of Oestergaard et al. who teach all the methods required to make the obvious DNase variants.
Thus claim(s) 1, 9, 11 is/are rejected under 35 U.S.C. 103 as being unpatentable over Oestergaard et al. (US 2019/0127664 and US 10,781,408) and Zhu et al. (Proceedings of the National Academy, Vol 113, No. 46, pp 12496-12951, Nov 2016).
Claim(s) 22 and 23 is/are rejected under 35 U.S.C. 103 as being unpatentable over Oestergaard et al. (US 2019/0127664 and US 10,781,408) and Zhu et al. (Proceedings of the National Academy, Vol 113, No. 46, pp 12496-12951, Nov 2016).
Oestergaard et al. teach Bacillus cibi DNase variants and uses thereof. Oestergaard et al. teach detergent compositions comprising DNase variants exhibiting alterations relative to the parent DNase in one or more properties including wash performance, detergent stability and/or storage stability. Oestergaard et al. teach a DNase variant comprising the amino acid sequence of SEQ ID NO:28 (97% sequence identity to instant SEQ ID NO:1). Oestergaard et al. teach the above DNase variant of SEQ ID NO:28 comprising a S68H substitution (see page claim 11 and supporting text).
Zhu et al. disclose analysis characterizing hydrophobicity of amino acid side chains in a protein environment via measuring contact angle of a water nanodroplet on planar peptide network. Zhu et al. teach that expectedly, all of the planar peptide networks with nonpolar amino acids are hydrophobic due to θ > 90°, whereas all of the planar peptide networks of the polar and charged amino acids are hydrophilic due to θ < 90°. Planar peptide networks of the charged amino acids exhibit complete-wetting behavior due to θ = 0. Zhu et al. disclose that the amino acids comprising charged side chains include histidine, lysine, glutamate, arginine and aspartate (Table 1, p 12948).
Before the effective filing date, one of ordinary skill in the art would have been motivated to make similar amino acid substitutions at position S68 of the DNase taught by Oestergaard et al. (SEQ ID NO:28) as a means of identifying DNase variants with improved properties including wash performance, detergent stability and/or storage stability. The obvious amino acid substitutions include those amino acids with similar charged amino acid side chains as taught by Oestergaard et al. which include histidine (i.e. S68H). The obvious amino acids include other charged amino acids such as lysine (i.e. S68K) as taught by Zhu et al.. It would have been further to include the obvious DNAse variant comprising a S68K substitution in a detergent composition comprising additional detergent adjunct ingredients such as taught by Oestergaard et al.. The expectation of success is high based upon the high level of skill in the art of recombinant protein engineering as exemplified by the teachings of Oestergaard et al. who teach all the methods required to make the obvious DNase variants.
Thus claim(s) 22 and 23 is/are rejected under 35 U.S.C. 103 as being unpatentable over Beier et al. (WO 2018/011276) and Zhu et al. (Proceedings of the National Academy, Vol 113, No. 46, pp 12496-12951, Nov 2016).
Remarks
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to RICHARD G HUTSON whose telephone number is (571)272-0930. The examiner can normally be reached 6-3 EST Mon-Fri.
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, Robert Mondesi can be reached at (408) 918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
rgh
8/27/2026
/RICHARD G HUTSON/Primary Examiner, Art Unit 1652
Prosecution Insights