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 .
Election/Restrictions
Applicant’s election without traverse of the invention of Group III and the species of a peptide having an amino acid sequence of instant SEQ ID NO: 29 (SEQ ID NO: 29 = KIGRLVTRK) in the reply filed on 03/02/2026 is acknowledged.
Claims 1, 25, 31, 35, 46, 48, 55, 82, 84-85, 89, 91, 99, 111, 117, 125, 137, 139 and 140 are currently pending.
Claims 1, 25, 31, 35, 46 and 48 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected invention and species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 03/02/2026.
Claims 55, 82, 84-85, 89, 91, 99, 111, 117, 125, 137, 139 and 140 will be examined on the merits.
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 55 and 125 is 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 55
Claim 55 recites tables in the Specification in sections (i) and (j). Where possible, claims are to be complete in themselves. Incorporation by reference to a specific figure or table “is permitted only in exceptional circumstances where there is no practical way to define the invention in words and where it is more concise to incorporate by reference than duplicating a drawing or table into the claim.” See MPEP 2173.05(s).
Claim 125
Regarding claim 125, the phrase "preferably" renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Note: for the purposes of examination, claim 125 will be examined as if “preferably from a blood sample from the mammalian subject cells” did not occur.
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.
Claim 111 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a written description rejection.
Claim 111 is directed to T engineered cell receptors, antibodies and chimeric antigen receptors (CARs), each with the recited function of specifically binding a peptide of instant SEQ ID NO: 29. Please note that because TCRs and antibodies/CARs require different structural/functional analysis, they will be discussed separately, with CARs and antibodies being grouped together based on the fact that the antigen-binding scFv of a CAR is derived from an antibody.
T cell receptors
Regarding TCR structure, no TCR structure is recited in any of the instant claims subject to this rejection.
With respect to the disclosure, Table 6 (which runs from Specification, p 273-306) lists a total of 322 pairings of TCR-a CDR3s amino acid sequences each individually paired with a TCR-b CDR3 amino acid sequence, each of which from a T cell that bound a peptide of instant SEQ ID NO: 29 (Specification, p 273-306). No disclosure is made with respect to TCR-a CDR 1, TCR-a CDR 2, TCR-b CDR 1 or TCR-b CDR 2. As such, the disclosure discloses a total of 322 partial TCR structures, each capable of performing the recited function of binding instant SEQ ID NO: 29.
Jokinen (Jokinen, et al., PLoS Comput Biol 2021 17(3): e1008814) teaches on the subject of a Gaussian computational process method that predicts if TCRs recognize specified epitopes (Jokinen, Abstract). Jokinen teaches that 90-95% of TCRs are formed by a pair of alpha and beta chains (Jokinen, p 2, ¶ 2) and the that CDRs of a TCR determine whether a TCR binds an antigen or not, with CDR3 being the most variable and binding to the peptidic antigen and CDR1 and CDR2 primarily interacting with the peptide binding groove of the MHC protein (Jokinen, p 2, ¶ 3). Jokinen teaches that while it is well-known that CDR3b of a TCR is important in recognizing peptides presented to the T cell, it remains unclear which specific physiochemical or structural features of CDR3b or other parts of the TCR determine the antigen recognition specificity of the T cell (Jokinen, p 2, ¶ 4). Jokinen teaches that the work of Jokinen focuses on a method called TCRGP, which builds on non-parametric modeling using Gaussian process classification (Jokinen, p 3, ¶ 2). Jokinen teaches that in order for a GP classifier such as TCRGP to predict if TCRs recognize a certain epitope, the GP must be provided a sufficient amount of training data consisting of TCRs that are known to recognize and to not recognize a that particular epitope (Jokinen, p 3, ¶ 1-2). Jokinen teaches that once the TCRGP has been trained, it can provide predictions to new, previously unseen TCRs, with the certainty of the prediction being encoded in the predicted values: with a prediction being close to one corresponding to a TCR very likely to recognize the epitope in question and a prediction close to zero being very likely the TCR does not recognize the epitope (Jokinen, p 4, ¶2).
With respect to the instant claims, a disclosure of 322 partial sequences of TCRs capable of performing the recited function of binding a peptide of SEQ ID NO: 29 is insufficient to be considered representative of the instant claimed genus, which is directed to any TCR comprising CDRs of any sequence capable of performing the recited function of specifically binding a peptide of instant SEQ ID NO: 29.
With respect to structure-function correlation, the teachings of Jokinen demonstrate that it is possible to establish an imperfect, probabilistic structure-function correlation capable of predicting whether or not a TCR will bind an epitope using computational methods such as TCRGP, such predictions are epitope-specific and require sufficient training data in the form of sequence data from TCRs known to bind and TCRs known to not bind a specific epitope to train the algorithm. For perspective, Jokinen teaches that for the CMV epitope pp65495-503 there were only 76 TCRs available for the training data, which contributed to lower prediction accuracy (Jokinen, p 5, ¶ 3), with AUROC of around 0.76 for the predictions for CDRa3 alone and AUROC of less than 0.6 for TCRb3 alone (Jokinen, Fig 2C) (note that AUROC is a measure of the performance of a model compared to the data, with an AUROC of 1 corresponding to perfect prediction and an AUROC of 0.5 corresponding to random guessing). A disclosure of 322 partial pairings of six distinct TCR CDRs is incapable of establishing reliable structure-function correlation between TCR CDR sequence and that TCR’s ability to bind a peptide having instant SEQ ID NO: 29, even using state-of-the art tools like TCRGP. Given the lack of disclosed species being sufficient to be representative of the entire claimed genus coupled with the lack of established structure-function correlation relating TCR CDR sequence(s) with the function of the resultant TCR being able to bind a peptide having instant SEQ ID NO: 29, claim 111 lacks written description and Applicant was not in possession of the invention as claimed.
Antibodies/Chimeric Antigen Receptors
Scope of the claimed antibodies and description in specification
Claim 111 is directed to all antibodies with the recited function of binding a peptide of SEQ ID NO: 26. Claim 111 does not recite any antibody structure. The instant disclosure does not provide any examples of species of antibody (or CAR) capable of performing the recited function of binding a peptide of SEQ ID NO: 26.
State of the Relevant Art
As was well-known in the antibody art, antibodies as a class share an overall structure generally comprising two heavy chain polypeptides that each comprises a heavy chain variable region (VH) and a heavy chain constant region made up of several domain (CH1, hinge, CH2, CH3, and for some antibodies, a CH4). Each of the heavy chains pairs with a light chain polypeptide that comprises a light chain variable region (VL) and a constant region. Sela-Culang (Sela-Culang, et al., Front. In Immunol. 2013; Vol. 4 Article 302) teaches on the subject of the structural basis of antibody-antigen recognition (Sela-Culang, Abstract). Sela-Culang teaches that there is a lack of intrinsic properties linking epitopic vs non-epitopic residues based on features present in said residues suggests that epitopes depend, to a great extent, on the antibody that recognizes them (Sela-Culang, p 2, ¶ 7). Sela-Culang teaches that antibodies fold in such a manner such that six hypervariable loops of the light and heavy domains of an antibody (three loops on the HC and three on the LC) are folded together and form the antigen binding site (Sela-Culang, p 3, ¶ 2). Sela-Culang teaches that the complimentary determining regions (CDRs) are amino acid sequences within this hypervariable region and that amino acids that define the CDR regions are typically defined based on numbering schemes (e.g., Kabat, Chothia, IMGT) derived from empirical studies of the boundaries between the framework and binding residues of the antibodies (Sela-Culang), p 3, ¶ 3). Sela-Culang teaches that identification of paratopes (the portion of an antibody which binds an antigen) is done through the identification of CDRs but CDRs, as identified by methods such as Kabat, Chothia and IMGT may miss ~20% of antigen binding residues (Sela-Culang, 4, ¶ 1-2). Sela-Culang teaches that each CDR has its own unique amino acid composition (i.e., different from the other CDRs) and each CDR has a unique set of contact preferences (Sela-Culang, p 5, ¶ 1).
Absent the conserved structure provided by all six CDRs of a parental antibody in the context of appropriate VH and VL framework sequences, the skilled artisan generally would not be able to visualize or otherwise predict what an antibody with a particular set of functional properties would look like structurally. As discussed above, neither an epitope nor a paratope can be calculated a priori based on properties of the component amino acids. Furthermore, each and every CDR sequence is unique and distinct and, as such, a CDR sequence cannot be predicted, either from the epitope sequence of from the CDR sequences of the antibody, if known.
In addition to the importance of the CDR regions, Sela-Culang also teaches that framework residues are also play an important role in antigen binding (Sela-Culang, P 7, ¶ 3). These framework residues can be divided into two types. The first are framework residues that actually contact the antigen and therefore are part of the binding site (Sela-Culang, p 7 ¶ 4). The second type of framework residues that affect antigen binding are framework residues that do not directly contact the antigen but affect binding indirectly (Sela-Culang, p 7, ¶ 5). Some of the framework residues are in close proximity to the CDR regions, providing structural support that allows the CDRs to adopt the right conformation to form the antigen binding site (Sela-Culang, p 7, ¶ 5). The other type of framework residues that indirectly affect antigen binding are further from the CDR regions and affect the relative orientation of the VH and VL regions, and thus the orientation of the CDRs relative to each other (Sela-Culang, p 7, ¶ 6). Sela-Culang also teaches that the effect of framework residues on antigen binding is impossible to predict a priori. For example, Sela-Culang teaches that positions in FR-3 of the heavy chain affects the orientation of CDRH1 relative to CDRH2, however this is not always the case, as it has been shown that mutating a Lys in this region for either a Val, Ala or Arg resulted in affinity differences but no structural changes (Sela-Culang, p 7, ¶ 5).
Are the disclosed species representative of the claimed genus?
MPEP § 2163 states that a “representative number of species” means that the species that are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
As stated above, the instant disclosure does not disclose any examples of antibodies or CARs capable of performing the required function of binding a peptide of SEQ ID NO: 26 and a disclosure of no antibodies is not representative of all antibodies capable of performing the recited function.
Identifying characteristics and structure/function correlation
In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied by disclosure of relevant, identifying characteristics; i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus.
As noted above, the art generally accepted that the combination of the CDRs within the VH and VL pair of an antibody was the minimum structure essential for binding specificity, an antibody is often defined in terms of the epitope that it binds and there is currently no way of predicting the CDR sequence required to bind an antigen. There is nothing in the instant Specification that would supplant these notions and, as such, the is no structure/function correlation that would allow a skilled artisan to envision which, if any, CDR combinations encompassed by the instant claims would form a functional antibody with the required function of binding a peptide of SEQ ID NO: 26
Because the species disclosed are insufficient to be considered representative of any the genus of all antibodies with the recited function of binding a peptide of SEQ ID NO: 26 coupled with the lack of established structure/function correlation, claim 111 lacks written description and Applicant was not in possession of the invention as claimed.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 55, 82, 84-85, 99, 111 and 137 are rejected under 35 U.S.C. 101 because the claimed invention is directed to naturally occurring peptidic cancer antigens derived from alternative splicing, nucleic acids encoding such antigens and host cells without significantly more.
Claim 55 recites peptides satisfying at least one of (a)-(j), all of which are naturally occurring cancer antigens derived from alternative splicing (AS). Claim 82 is directed to nucleic acids encoding such peptides, which are also naturally occurring. Claim 84 is directed to host cells comprising such nucleic acids and these cells are also naturally occurring. Claim 85 is directed to host cells that are dendritic cells comprising the peptides of claim 55 and cells, which are also naturally occurring. Claim 99 is directed to compositions comprising DCs and the peptide of claim 55, which is also naturally occurring. Claim 111 is directed to a composition comprising a TCR that recognizes the peptide of claim 55, which is also a naturally occurring phenomenon because the peptides of claim 55 are naturally occurring and, as such, natural TCRs recognizing these peptides are also naturally occurring because they form when T cells are activated by naturally present peptides of claim 55 in vivo leading to naturally occurring TCRs. Claim 137 is directed to compositions comprising peptide-specific T cells, which are also naturally occurring phenomenon based on the fact these T cell comprise the naturally occurring TCRs of instant claim 111.
None of these judicial exceptions are integrated into a practical application because the claims are all composition claims and, as such, do not recite any applications for the claimed compositions. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the claims are just directed to the peptides, nucleic acids, TCRs and cells only, without any modifications.
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.
Claim(s) 55, 82, 84 and 89 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Bancel (Bancel, et al., WO 2013/151672 A2; Published 10/10/2013; Priority to 4/2/2012 via US 61/618,862).
Bancel teaches on the subject of compositions and methods related to oncology related polynucleotides and transcripts (Bancel, Abstract).
Regarding the amino acid sequence limitation of claim 55, Bancel teaches SEQ ID NO: 7655 of Bancel, which is derived from (PLA2G6) (Bancel, p 280, 2nd row from top), which comprises 100% of instant SEQ ID NO: 29 (See DAV for pairwise comparison):
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Regarding claim 82, teaches methods of treating a disease, disorder and/or condition in a subject in need thereof by increasing the level of an oncology-related polypeptide of interest comprising administering to said subject an isolated polynucleotide encoding said oncology-related polypeptide. (Bancel, ¶ 0007-00010). Regarding claims 84 and 89, Bancel teaches the introduction of polynucleotides comprising the nucleic acids of Bancel to host cells (Bancel, ¶ 000774).
Claim Rejections - 35 USC § 103
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.
Claim(s) 55, 82, 84, 89 and 117 is/are rejected under 35 U.S.C. 103 as being unpatentable over Bancel (Bancel, et al., WO 2013/151672 A2; Published 10/10/2013; Priority to 4/2/2012 via US 61/618,862) as applied to claims 55, 82, 84 and 89 above and in further consideration of the Bancel reference.
The teachings of Bancel are discussed above. Additionally, Bancel teaches a method of treating a disease comprising administering to a subject the polynucleotide of Bancel (Bancel, claim 1), wherein the disease is brain cancer (Bancel, claim 4).
Bancel does not teach a method of treating brain cancer comprising the administration of a polypeptide having SEQ ID NO: 7655 of Bancel.
It would be prima facie obvious to one of ordinary skill in the art to administer a polypeptide having SEQ ID NO: 7655 of the Bancel reference. One of ordinary skill in the art would be motivated to do this in order to better fight brain cancer. One of ordinary skill in the art would have a reasonable expectation of success administering the polypeptide having SEQ ID NO: 7655 of Bancel in a method of treating brain cancer because Bancel teaches a method of treating brain cancer comprising administering a polynucleotide encoding a polypeptide having SEQ ID NO: 7655 of Bancel and one of skill in the art would reasonably deduce that administering the peptide itself would have a similar effect because the polynucleotide of Bancel is eventually translated into the polypeptide having SEQ ID NO: 7655 of Bancel.
Claim(s) 55, 82, 84-85, 89, 91, 99, 117 and 139 is/are rejected under 35 U.S.C. 103 as being unpatentable over Bancel (Bancel, et al., WO 2013/151672 A2; Published 10/10/2013; Priority to 4/2/2012 via US 61/618,862) as applied to claims 55, 82, 84, 89 and 117 above and in further view of Kim (Kim, et al., Neurosurgery Clin. N. Am. 2010 21(1):139).
The teachings of Bancel are discussed above.
Bancel does not teach a method of treating brain cancer comprising administering to a patient in need of treatment a formulation comprising dendritic cells that have contacted a peptide comprising instant SEQ ID NO: 29.
Kim teaches on the subject of dendritic cell vaccines for brain cancers (Kim, Abstract). Kim teaches that dendritic cell vaccines are DCs loaded with antigens such as antigens found in glioma that are administered to patients in order to induce an antigen-specific T cell mediated anti-tumor response (Kim, p 2¶ 2). Kim teaches that DCs localize to lymph organs rich in naïve T cells and mobilized many different arms of the immune system, including CD8+ cytotoxic T cells (CTLs), CD4+ helper T cells, natural killer (NK) cells, and NK-like T cells, all of which play an essential role in anti-tumor responses (Kim, p 2, ¶ 3). Kim teaches that DC vaccines are prepared by activating DCs via a wide range of antigen sources including synthetic peptides, acid-eluted tumor peptides, tumor lysate, DC-tumor fusion cells and antigen-containing vectors (e.g., cDNA/RNA carrying viruses) (same as “contacting” the DCs with the antigen in vitro) and then administering the “loaded” DCs to a patient (Kim, p 3, ¶ 2). Kim also teaches that, at the time of publication, numerous study groups had reached the clinical stage of development for DC vaccines for brain cancers (Kim, p 3, ¶ 5 – p 7, ¶ 1).
It would be prima facie obvious to one of ordinary skill in the art to start with the oncology-related polypeptide of Bancel (which comprises all of instant SEQ ID NO: 29) and the anti-tumor DC vaccines of Kim, prepare a DC vaccine by contacting the DCs of Kim with the oncology-related polypeptide of Bancel and administer the resultant DC vaccine to a patient as part of a method of treating brain cancer. One of ordinary skill in the art would be motivated to do this in order to better treat brain cancer. One of ordinary skill in the art would have a reasonable expectation of success preparing a DC vaccine by contacting the DCs of Kim with the oncology-related polypeptide of Bancel and administer the resultant DC vaccine to a patient as part of a method of treating brain cancer because: 1) Bancel teaches the use of the oncology-related polypeptide of Bancel as an antigen in methods of treating brain cancer, 2) Kim teaches that DC vaccines comprising DCs that have been contacted with tumor-derived peptidic antigens in vitro have been widely used at the clinical stage as a method of treating various brain cancers and 3) one of ordinary skill in the art would reasonably deduce that contacting DCs with the oncology-related peptide of Bancel would produce a DC vaccine that recognizes the oncology-related peptide of Bancel because Kim teaches “pulsing” DCs with a wide range of tumor antigens.
Claim(s) 55, 82, 84, 89, 117, 125, 137 and 140 is/are rejected under 35 U.S.C. 103 as being unpatentable over Bancel (Bancel, et al., WO 2013/151672 A2; Published 10/10/2013; Priority to 4/2/2012 via US 61/618,862) as applied to claims 55, 82, 84, 89 and 117 above and in further view of Kwon (Kwon, et al., US 2018/0216066 A1; Published 8/2/2018).
The teachings of Bancel are discussed above.
Bancel does not teach a method of treating brain cancer in a subject, said method comprising administering peptide-specific T cells that have been activated by contacting a starting population of T cells with the oncology-related polypeptide of Bancel ex vivo.
Kwon teaches a method of isolating and proliferating autologous, antigen-specific CD8+ T cells (Kwon, Abstract). Kwon teaches a method of isolating autologous cancer antigen-specific CD8+ T cells comprising culturing PMBCs (which comprise nave T cells) in cell culture in the presence of peptide antigens (same as “contacting” the T cells with the peptide antigens) (Kwon, claim 1). Kwon also reaches methods of treating cancer, said methods comprising administering the autologous, antigen-specific T cells of Kwon (Kwon, claim 27), wherein said cancer is a solid tumor (Kwon, claim 27) that is brain cancer (Kwon, claim 29).
It would be prima facie obvious to one of ordinary skill in the art to start with the oncology-related polypeptide of Bancel, apply the T cell-producing method of Kwon to produce a population of T cells specific for the oncology-related polypeptide of Bancel and administer the resultant T cell population to a subject as part of a method of treating brain cancer. One of ordinary skill in the art would be motivated to do this in order to better treat brain cancer. One of ordinary skill in the art would have a reasonable expectation of success starting with the oncology-related polypeptide of Bancel, applying the T cell-producing method of Kwon to produce a population of T cells specific for the oncology-related polypeptide of Bancel and administering the resultant T cell population to a subject as part of a method of treating brain cancer because: 1) Bancel teaches the use of the oncology-related polypeptide of Bancel as an antigen in methods of treating brain cancer and 2) Kwon teaches that the method of Kwon is be used to produce T cell populations that are capable of being used in methods of treating brain cancer, wherein said methods comprise administering the activated, antigen-specific T cells produced by the method of Kwon.
Conclusion
Claims 55, 82, 84-85, 89, 91, 99, 111, 117, 125, 137, 139 and 140 are rejected.
No claims are allowed
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Sydney Van Druff whose telephone number is (571)272-2085. The examiner can normally be reached 10 am - 6 pm.
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/SYDNEY VAN DRUFF/Examiner, Art Unit 1643
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643
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