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 .
Detailed Action
The Amendments and Remarks filed 5/7/26 in response to the Office Action of 1/7/26 are acknowledged and have been entered.
Claims 1, 14-21, 23, 24, 27, 29, 32-39, 48, and 63 are pending.
Claims 1 and 63 have been amended by Applicant.
Claims 1, 14-21, 23, 24, 27, 29, 32-39, 48, and 63 are currently under examination.
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
The following Office Action contains NEW GROUNDS of rejections Necessitated by Amendments.
Objections Withdrawn
The objections to the claims are withdrawn.
Rejections Withdrawn
The rejection under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, is withdrawn.
Rejections Maintained
Claim Rejections - 35 USC § 102
Claim(s) 1, 14, 15, 19, 21, 23, 27, and 32-37 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Benson et al (WO 2017/025889 A1; 2/16/17; 7/20/22 IDS).
Benson et al teaches SEQ ID NO:29 (recombinant human DEC-205 protein containing monomeric human IgG Fc), which is a protein comprising a human DEC-205 extracellular domain fused to a monomeric human IgG1 Fc fragment (page 32 and Example 4 on page 43, in particular). SEQ ID NO:29 is a 435 amino sequence comprising a 182 amino acid portion 100% identical to 183 amino acids instant SEQ ID NO:1 that is linked by about 23 amino acids to a 210 amino acid portion C-terminal to the 182 amino acid portion wherein the C-terminal 210 amino acid portion is 88.3% identical to the FcgRIIb sequence of instant SEQ ID NO:5. Benson et al teaches oligonucleotides as ligands of the DEC-205 extracellular domain (lines 22-23 on page 14, in particular). Benson et al does not explicitly describe the oligonucleotides as “mitochondrial DNA” or “genomic DNA”. However, as evidenced by the instant specification, the DEC-205 extracellular domain portion of SEQ ID NO:29 of Benson et al comprising a 182 amino acid sequence that is 100% identical to 182 of the 183 amino acids instant SEQ ID NO:1 would bind mitochondrial and/or genomic DNA because the instant specification discloses DEC-205 fragments 99% identical to instant SEQ ID NO:1 bind mitochondrial and/or genomic DNA (see [0076] and [0091], in particular). Further, as evidenced by instant Figure 10, DEC-205 extracellular domain of the construct of Benson et al comprises Ricin B-type domain, fibronectin type II domain, and multiple C-type lectin domains. The DEC-205 extracellular domain portion of SEQ ID NO:29 comprises a polypeptide having 182 consecutive amino acids of instant SEQ ID NO:4. As recited by instant claim 32, every protein (including DEC-205 extracellular domain of the construct of Benson et al) comprises a broadly-recited “fragment of TLR9 with one or more amino acid deletions, additions or substitutions.” Benson et al further teaches the recombinant human DEC-205 protein containing monomeric human IgG Fc was generated by expressing a polynucleotide vector encoding the recombinant human DEC-205 protein containing monomeric human IgG Fc in HEK host cells (Example 4 on page 43, in particular). Benson et al further teaches use of an ELISA to measure binding of anti-DEC-205 proteins to recombinant human DEC-205 protein containing monomeric human IgG Fc (“DEC-205-Fc”). Benson et al teaches targeting ligands, such as antibodies, for DEC-205 provide therapeutic benefit by delivering protein antigens to DEC-205 expressing cells (lines 16-20 on page 2 and page 5, in particular). Benson et al further teaches using a Biacore® system to determine binding of an antibody (lines 19-23 on page 12, in particular). In particular regards to instant claim 23, SEQ ID NO:29 of Benson et al comprises a sequence identical to a broadly-recited Fc “fragment” of a mouse IgG1 receptor gamma (FcgRIIb) Fc domain (a full mouse IgG1 receptor gamma (FcgRIIb) Fc domain is set-forth by instant SEQ ID NO:6).
Response to Arguments
In the Reply of 5/7/26, Applicant argues it is believed this rejection is overcome by inserting subject matter of claims that have not been rejected into rejected claims.
The amendments to the claims and the arguments found in the Reply of 5/7/26 have been carefully considered, but are not deemed persuasive. In regards to the indication it is believed this rejection is overcome by inserting subject matter of claims that have not been rejected into rejected claims, the rejection is maintained for reasons of record. Only claim 1 of the rejected claims was amended with newly added text. The newly added text recites a fragment of DEC205 comprises a polypeptide with a sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3 an da polypeptide that is at least 90% identical to a sequence comprising SEQ ID NO:4. However, claim 1 is not drawn to a fragment of DEC205 and claim 1 lacks antecedent basis for “the fragment of DEC205”. Therefore, the “wherein” claim of claim 1 does not further limit the claims.
Claim Rejections - 35 USC § 103
Claim(s) 1, 14, 15, 19, 21, 23, 25, 27, and 32-39 remain rejected under 35 U.S.C. 103 as being unpatentable over Benson et al (WO 2017/025889 A1; 2/16/17; 7/20/22 IDS) as applied to claims 1, 14, 15, 19, 21, 23, 27, and 32-37 above, and further in view of Lindskog et al (Biopharmaceutical Processing, 2018, 111-130).
Teachings of Benson et al are discussed above.
Benson et al does not specifically teach expressing a recited protein in in CHO or BHK host cells, as opposed to HEK host cells. However, these deficiencies are made up in the teachings of Lindskog et al.
Lindskog et al teaches HEK, BHK, and CHO as three types of host cells used to make recombinant proteins (Table 6.1, in particular).
One of ordinary skill in the art would have been motivated, with a reasonable expectation of success, to perform a combined method of generating the recombinant human DEC-205 protein containing monomeric human IgG Fc by of Benson et al by expressing a polynucleotide vector encoding the recombinant human DEC-205 protein containing monomeric human IgG Fc in CHO or BHK host cells, as opposed to HEK host cells of Benson et al, because Lindskog et al teaches HEK, BHK, and CHO as three types of host cells used to make recombinant proteins. This is an example of a simple substitution of one known element for another to obtain predictable results. See MPEP 2143. Therefore, the invention as a whole would have been prima facie obvious to one of ordinary skill in the art, absent unexpected results.
Response to Arguments
In the Reply of 5/7/26, Applicant repeats arguments addressed above.
Claim Rejections - 35 USC § 103
Claim(s) 1, 14, 15, 19, 21, 23, 25, 27, 32-37, and 48 is/are rejected under 35 U.S.C. 103 as being unpatentable over Benson et al (WO 2017/025889 A1; 2/16/17; 7/20/22 IDS) as applied to claims 1, 14, 15, 19, 21, 23, 25, 27, and 32-37 above, and further in view of Urh et al (Methods in Enzymology, 2009, 463: 417-438).
Teachings of Benson et al are discussed above.
Benson et al does not specifically teach a device comprising an inlet, an outlet, a chamber comprising a solid substrate, wherein a protein containing monomeric human IgG Fc by of Benson et al is immobilized on the solid substrate. However, these deficiencies are made up in the teachings of Urh et al.
Urh et al an affinity chromatography device to identify reagents that bind a given protein within a chamber/column comprising a solid substrate that permits flow (which one of skill in the art would recognize is through an inlet and outlet), wherein the given protein is immobilized on the solid substrate and binds to reagents that bind to the given protein (see “ligand attachment” and “purification method” sections at pages 430-435, in particular).
One of ordinary skill in the art would have been motivated, with a reasonable expectation of success, to perform a combined method comprising using an affinity chromatography device of Urh et al wherein the DEC-205 protein containing monomeric human IgG Fc by of Benson et al is immobilized on a solid support and binds to targeting ligands suspected of binding to DEC-205 because Benson et al teaches targeting ligands, such as antibodies, for DEC-205 provide therapeutic benefit by delivering protein antigens to DEC-205 expressing cells, and the affinity chromatography device of Urh et al is capable of identifying targeting ligands of a given protein (such as DEC-205). Further, targeting ligands bound to DEC-205 protein containing monomeric human IgG Fc by of Benson et al are “therapeutic agents” due to their ability to deliver protein antigens to DEC-205 expressing cells. Therefore, the invention as a whole would have been prima facie obvious to one of ordinary skill in the art, absent unexpected results.
Response to Arguments
In the Reply of 5/7/26, Applicant repeats arguments addressed above.
New Rejections Necessitated by Amendments
Claim Rejections - 35 USC § 112
Claims 1, 14-21, 23, 24, 27, 29, 32-39, 48, and 63 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 1 recites “…wherein the fragment of DEC205 comprises….” There is insufficient antecedent basis for “the fragment of DEC205” in the claims.
Conclusion
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.
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/SEAN E AEDER/Primary Examiner, Art Unit 1642
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