---------------------------------------------------------------------------------------------------------DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
The claim listing filed July 10, 2024 is pending.
Claims 1, 12-14, 18, 19, 22, and 23 are canceled.
Claims 2-11, 15-17, 20, and 21 are pending and currently under consideration.
Claim 2 is an independent claim.
Priority
The instant application is a 371 of PCT/CN2022/102729 filed 06/30/2022 and claims foreign priority to PCTCN2021120110 filed 09/24/2021 and PCTCN2021104623 filed 07/06/2021.
Certified translated copies of PCTCN2021120110 and PCTCN2021104623 have not been filed. Therefore, it is not clear if the foreign priority documents have adequate support for the instant claims.
Claim Objections
The phrase “the amino acid sequences” should be deleted from line 3 of claims 3 and 6.
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 20 and 21 are rejected under 35 U.S.C. 101 because the claimed invention is directed to non-statutory subject matter. The claims do not fall within at least one of the four categories of patent eligible subject matter because claims 20 and 21 are directed to the “use” of the anti-CD24 antibody or antigen-binding fragment of claim 2 in the preparation of a drug for the treatment of cancer.
"Use" claims are non-statutory under 35 U.S.C. 101 because the claimed recitation of a use, without setting forth any steps involved in the process, results in an improper definition of a process, i.e., results in a claim which is not a proper process claim under 35 U.S.C. 101. See for example Ex parte Dunki , 153 USPQ 678 (Bd. App. 1967) and Clinical Products, Ltd v. Brenner, 255 F. Supp. 131, 149 USPQ 475 (D.D.C. 1966). See MPEP 2173.05(q).
Canceling claims 20 and 21 or amending claim 20 to be directed to statutory subject matter would obviate this part of the rejection.
For the purpose of applying prior art, claims 20 and 21 are being read as the anti-CD24 antibody or antigen-binding fragment of claim 2.
Claim Rejections - 35 USC § 112
Indefinite language
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 7-9, 11, 15-17, 20, and 21 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.
Claims 7 and 8 recite the VH and VL amino acid sequences of an anti-CD24 antibody. However, claims 7 and 8 are dependent on claim 5 which already recites the amino acid sequences of VH and VL of a different anti-CD24 antibody, namely an anti-CD24 antibody that has different CDRs that that of claims 7 and 8. Therefore, it is unclear if the VH and VL amino acid sequences recited in claims 7 and 8 are in addition to those already recited in claim 5 or if they are supposed to limit the VH and VL amino acid sequences of claim 5. If they are in addition to those already recited in claim 5, the claims 7 and 8 are not further limiting. If they are meant to limit the VH and VL amino acid sequences of claim 5 then they lack antecedence basis. For these reasons claims 7 and 8 are indefinite.
Amending claims 7 and 8 to be dependent on claim 6 would obviate this part of the rejection because claim 6 recites the proper CDR amino acid sequences for the VH and VL domains of claims 7 and 8.
Claims 9, 11, 15-17 are included in this part of the rejection because they depend on claim 7.
Claims 20 and 21 are directed to the “use” of the anti-CD24 antibody or antigen-binding fragment of claim 2 in the preparation of a drug for the treatment of cancer. Attempts to claim a process without setting forth any steps involved in the process generally raises an issue of indefiniteness under 35 U.S.C. 112(b). For example, a claim which read: "[a] process for using monoclonal antibodies of claim 4 to isolate and purify human fibroblast interferon" was held to be indefinite because it merely recites a use without any active, positive steps delimiting how this use is actually practiced. Ex parte Erlich, 3 USPQ2d 1011 (Bd. Pat. App. & Inter. 1986). See MPEP 2173.05(q).
This applies to the instant case where claims 20 and 21 claim “use of the anti-CD24 antibody or antigen-binding fragment” without reciting any steps involved in said use.
Canceling claims 20 and 21 or amending claim 20 to recite “A method for…” would obviate this part of the rejection.
Claim Rejections - 35 USC § 112
Written Description
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 that 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 that 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 2 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 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.
The claims are drawn to an anti-CD24 antibody or antigen-binding fragment thereof, comprising a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the heavy chain complementary determining regions HCDR1, HCDR2, and HCDR3, and the light chain variable region comprises the light chain complementary determining regions LCDR1, LCDR2, and LCDR3, wherein:
(a) HCDR1 of the heavy chain variable region is selected from any amino acid sequence of SEQ ID NOs: 2, 17, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 2, 17, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 2, 17;
(b) HCDR2 of the heavy chain variable region is selected from any amino acid sequence of SEQ ID NOs: 3, 18, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 3, 18, or an amino acid sequence having one or more conserved amino acid mutations comparison to any amino acid sequence of SEQ ID NOs: 3, 18;
(c) HCDR3 of the heavy chain variable region is selected from any amino acid sequence of SEQ ID NOs: 4, 19, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 4, 19, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 4, 19;
(d) LCDR1 of the light chain variable region is selected from any amino acid sequence of SEQ ID NOs: 6, 21, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 6, 21, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 6, 21;
(e) LCDR2 of the light chain variable region is selected from any amino acid sequence of SEQ ID NOs: 7, 22, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 7, 22, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 7, 22; and/or
(f) LCDR3 of the light chain variable region is selected from any amino acid sequence of SEQ ID NOs: 8, 23, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 8, 23, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 8, 23.
The Applicant disclosed the generation of anti-CD24 antibodies by the immunization of balb/c mice with human CD24-his and VLP-huCD24 as immunogens (e.g. see [0072]). Immune serum were diluted proportionally and the breast cancer MDA-MB-231 cells overexpressing CD24 (huCD24-MDA-MB-23] were detected by ELISA for serum potency assay. When the potency result meets the requirement and anti-human CD24 antibody was detected at a dilution of
>
1:10K, rat spleen and lymph nodes could be harvested (e.g. see [0072]). The harvested lymph nodes were the fused with myeloma cells SP2/0 (ATCC) (B lymphocytes) (e.g. see [0073] and [0074]). The fusion cell lines with OD450>1.0 in the fusion supernatant result were selected as candidate positive cell lines for initial screening (e.g. see [0075]). These cells were analyzed by flow cytometry and the cells producing antibodies that bound specifically to huCD24-MDA-MB-231 cells were screened by FACS method (e.g. see [0076]). The hybridoma cells were monoclonalized and ELISA was used for detection (e.g. see [0077]). The monoclones with OD450>1.0 were selected as the definitive candidate cell lines for passage, and clones without monoclonal antibodies were selected with OD450>1.0 for the next subcloning (e.g. see [0077]). The final positive clones were confirmed by evaluating the binding activity of the candidate antibodies to tumor cells MCF7 (ATCC), SKOV3 (ATCC), HT55 (ATCC), and huCD24-MDA-MB-231 using the FACS method (e.g. see [0079]).
The Applicant discloses the murine anti-CD24 antibody ms-01 with good binding activity to tumor cells MCF7 and SKOV3 was obtained by hybridoma screening, and Fab fragment of the murine anti-CD24 antibody ms-02 was obtained by mouse immune library screening (e.g. see [0096]). The amino acid sequences of murine anti-CD24 antibody ms-01 and ms-02 were finally obtained by sequencing ms-01 and ms-02, respectively:
(1) The amino acid sequences of ms-01 (and CH-01) are as follows: The amino acid sequence of the heavy chain variable region of ms-01 is SEQ ID NO: 1 which comprises the amino acid sequences of HCDR1, HCDR2 and HCDR3 as SEQ ID NO: 2, SEQ ID NO: 3 and SEQ ID NO: 4, respectively; the amino acid sequence of the light chain variable region of ms-01 is SEQ ID NO: 5 which comprises the amino acid sequences of LCDR1, LCDR2 and LCDR3 as SEQ ID NO: 6, SEQ ID NO: 7 and SEQ ID NO: 8, respectively; and
(2) The amino acid sequences of ms-02 (and CH-02) are as follows: The amino acid sequence of the heavy chain variable region of ms-02 is SEQ ID NO: 16 which comprises the amino acid sequences of HCDR1, HCDR2 and HCDR3 as SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 19, respectively; The amino acid sequence of the light chain variable region of ms-02 is SEQ ID NO: 20 comprising the amino acid sequences of LCDR1, LCDR2 and LCDR3 as SEQ ID NO: 21, SEQ ID NO: 22 and SEQ ID NO: 23, respectively (e.g. see [0096] – [0121]).
The Applicant also discloses that the ms-01 and ms-02 antibodies were humanized to generate 37 different antibodies hu-01-L1H1, hu-01-L2H1, hu-01-L3H1, hu-01-L1H2, hu-01, L2H2, hu-01-L3H2, hu-01-L1H3, hu-01-L2H3, hu-01-L3H3, hu-01-L1H4, hu-01-L2H4, hu-01-L3H4, hu-02-L1H1, hu-02-L2H1, hu-02-L3H1, hu-02-L1H2, hu-02-L2H2, hu-02-L3H2, hu-02-L1H3, hu-02-L2H3, hu-02-L3H3, hu-02-L3H3, hu-02-L1H4, hu-02-L2H4, hu-02-L3H4, hu-02-L1H5, hu-02-L2H5, hu-02-L3H5, hu-02-L1H6, hu-02-L2H6, hu-02-L3H6, hu-02-L1H7, hu-02-L2H7, hu-02-L3H7, hu-02-L1H8, hu-02-L2H8, and hu-02-L3H8 (e.g. see [00126] – [00138]).
It is noted that hu-01-L1H1 (comprising SEQ ID NOs: 9 and 13), hu-01-L2H1 (comprising SEQ ID NOs: 9 and 14), and hu-01-L3H1 (comprising SEQ ID NOs: 9 and 15) did not exhibit CD24 binding (e.g. see table 5 on page 31) and hu-02-L1H2 (comprising SEQ ID NOs: 25 and 32), hu-02-L1H4 (comprising SEQ ID NOs: 27 and 32), hu-02-L1H5 (comprising SEQ ID NOs: 28 and 32), hu-02-L1H6 (comprising SEQ ID NOs: 29 and 32), and hu-02-L1H8 (comprising SEQ ID NOs: 31 and 32) were not tested for CD24 binding.
When given the broadest reasonable interpretation in light of specification, the anti-CD24 antibody or antigen-binding fragment thereof of the instant invention is defined broadly to be any agent that binds to CD24 and comprises:
an HCDR1 of any amino acid sequence of SEQ ID NOs: 2, 17, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 2, 17, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 2, 17;
an HCDR2 of any amino acid sequence of SEQ ID NOs: 3, 18, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 3, 18, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 3, 18;
an HCDR3 of any amino acid sequence of SEQ ID NOs: 4, 19, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 4, 19, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 4, 19;
an LCDR1 of any amino acid sequence of SEQ ID NOs: 6, 21, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 6, 21, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 6, 21;
an LCDR2 of any amino acid sequence of SEQ ID NOs: 7, 22, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 7, 22, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 7, 22; and/or
an LCDR3 of any amino acid sequence of SEQ ID NOs: 8, 23, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 8, 23, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 8, 23.
It is noted that claim 2 does not recite sufficient structure for the genus of anti-CD24 antibodies or antigen-binding fragments thereof because the anti-CD24 antibodies or antigen-binding fragments may comprise less than 6 CDRs with have variable amino acid sequences and/or may comprise any combination of CDRs.
It is further noted that the remaining claims do recite sufficient structure for the genus of anti-CD24 antibodies or antigen-binding fragments thereof, however claims 5 and 8 recite antibodies which have do not show CD24 binding.
The guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, § 1 "Written Description" Requirement make clear that if a claimed genus does not show actual reduction to practice for a representative number of species, then the Requirement may be alternatively met by reduction to drawings, or 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 genus (Federal Register, Vol. 66, No. 4, pages 1099-1111, January 5, 2001, see especially page 1106 column 3). In The Regents of the University of California v. Eli Lilly (43 USPQ2d 1398-1412) 19 F. 3d 1559, the court held that disclosure of a single member of a genus (rat insulin) did not provide adequate written support for the claimed genus (all mammalian insulins). In this same case, the court also noted:
“A definition by function, as we have previously indicated, does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. See Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen). It is only a definition of a useful result rather than a definition of what achieves that result. Many such genes may achieve that result. The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does “little more than outlin[e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate.”). Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.”
Artisans are well aware that knowledge of a given antigen (for instance CD24) provides no information concerning the sequence/structure of antibodies that bind the given antigen. For example, Edwards et al. (J. Mol. Biol., 2003, 334:103-118) teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well, see entire document).
As such, it does not seem possible to predict the sequence/structure of an antibody that binds a given antigen, as there does not appear to be any common or core structure present within all antigen binding molecules that gives rise to the function of antigen binding. Further, given data, such as that of Edwards et al., indicating the diversity of sequences in a population of antibodies that bind to a given antigen, no number of species appears to reasonably representative of the breadth of the genus of antibodies or antigen binding molecules that bind the given antigen.
It should be pointed out that it is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antigen binding molecule to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin (Janeway Jr et al., Immunology, 3rd Edition, 1997 Garland Publishing Inc., pages 3:1-3:11.see entire selection).
Thus, based upon the prior art, skilled artisans would reasonably understand that it is the structure of the CDRs within an antibody which gives rise to the functional property of antigen binding, the epitope to that which said CDRs bind is an inherent property which appears to necessarily be present due to conservation of critical structural elements, namely the CDR sequences themselves.
This applies to the instant invention which is drawn to a genus of anti-CD24 antibodies or antigen-binding fragments thereof that may comprise less than 6 CDRs with have variable amino acid sequences and/or may comprise any combination of CDRs.
As noted above, the Applicant has disclosed two anti-CD24 antibodies, ms-01 and ms-02, which comprise a complete set of 6 CDRs with defined amino acid sequences (e.g. see [0096] – [0121]). Such a disclosure does not serve to provide sufficient written description of the claimed to a genus of anti-CD24 antibodies or antigen-binding fragments thereof that may comprise less than 6 CDRs with have variable amino acid sequences and/or may comprise any combination of CDRs. The disclosure does not identify sufficient structural features or combination of features which give rise to the function of binding to CD24. Additionally, there does not appear to be any reasonable shared structure present in the genus of antibodies or antigen binding fragments thereof which gives rise to their functional activity. Ultimately, identifying an antibody or antigen binding fragment thereof on the basis binding to CD24 rather than by identifying the sequence/structure, namely a complete set of six CDRs, of the antibody or antigen binding fragment thereof in question is generally insufficient to provide written description.
This reasoning further applies to limitations in claim 2 which recite that the CDRs may comprise “a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: X, Y, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: X, Y.” These limitations do not satisfy the written description requirement because the claim language allows for up to 20%, 15%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, and 1% variability in the amino acid sequence structure of the CDRs which would be expected to impact the functional binding activity of the antibodies and antigen binding fragments thereof based on the state of the prior art. Claim 2 encompasses a subgenus of antibody and antigen binding fragment structures which are functionally defined by their ability to bind to CD24 without reciting a corresponding structure expected to correlate with this ability as supported by Applicant’s disclosure.
Therefore, in view of the breadth of the claims and the limited disclosure, artisans would reasonably conclude that applicant was not in possession of the full breadth of antibodies or antigen binding fragments thereof that bind CD24 as encompassed by the claims at the time the instant application was filed.
Amending:
claim 2 to limit the anti-CD24 antibody or antigen binding fragment thereof to that which comprises (with no variability or mutations):
the amino acid sequences of HCDR1, HCDR2 and HCDR3 as SEQ ID NO: 2, SEQ ID NO: 3 and SEQ ID NO: 4, respectively, and the amino acid sequences of LCDR1, LCDR2 and LCDR3 as SEQ ID NO: 6, SEQ ID NO: 7 and SEQ ID NO: 8, respectively; or
the amino acid sequences of HCDR1, HCDR2 and HCDR3 as SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 19, respectively, the amino acid sequences of LCDR1, LCDR2 and LCDR3 as SEQ ID NO: 21, SEQ ID NO: 22 and SEQ ID NO: 23, respectively;
claim 5 to delete antibodies 1-3; and
claim 8 to delete antibodies 4, 10, 13, 16, and 22
would obviate this part of the rejection.
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.
Claims 2, 20, and 21 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Arber et al. 2020 (WO2020261280).
Independent claim 2 is drawn to an anti-CD24 antibody or antigen-binding fragment thereof comprising:
an HCDR1 of any amino acid sequence of SEQ ID NOs: 2, 17, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 2, 17, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 2, 17;
an HCDR2 of any amino acid sequence of SEQ ID NOs: 3, 18, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 3, 18, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 3, 18;
an HCDR3 of any amino acid sequence of SEQ ID NOs: 4, 19, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 4, 19, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 4, 19;
an LCDR1 of any amino acid sequence of SEQ ID NOs: 6, 21, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 6, 21, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 6, 21;
an LCDR2 of any amino acid sequence of SEQ ID NOs: 7, 22, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 7, 22, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 7, 22; and/or
an LCDR3 of any amino acid sequence of SEQ ID NOs: 8, 23, or a sequence having at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more identity to any amino acid sequence of SEQ ID NOs: 8, 23, or an amino acid sequence having one or more conserved amino acid mutations in comparison to any amino acid sequence of SEQ ID NOs: 8, 23.
It is noted that when given the broadest reasonable interpretation and the recitation of the CDRs having “any amino acid sequence of SEQ ID NOs: X, Y,” the anti-CD24 antibodies of the instant invention encompass those anti-CD24 antibodies that comprise only two consecutive amino acids with “at least 80%...or more identity” or “one or more conserved amino acid mutations” of the recited SEQ ID NOs. It is further noted that in view of the recitation of the phrase “and/or” in line 35, claim 2 encompasses anti-CD24 antibodies that comprise only one of the six recited CDRs.
For the purpose of applying prior art, dependent claims 20 and 21 are being read as the anti-CD24 antibody or antigen-binding fragment of claim 2. See rejection under 35 USC § 101 above.
Arber et al. teach an anti-CD24 antibody comprising an LCDR1 that comprises an amino acid sequence that least two consecutive amino acid sequences of instant SEQ ID NO: 6 (e.g. see Figure 17). See sequence alignment below.
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Alignment of Arber et al.’s SEQ ID NO: 1 and instant SEQ ID NO: 6:
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 2, 6-9, 11, 15-17, 20, and 21 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 23 of U.S. Application No. 19/104,761 (the ‘761 Application).
Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims and the claims in the ‘761 Application are drawn to the same or nearly the same anti-CD24 antibody or antigen binding fragment thereof having the same or nearly the same structure.
Dependent claim 23 of the ‘761 Application is drawn to a bispecific antibody but is otherwise identical to instant claim 2. Therefore, claim 23 of the ‘761 Application recites a “species” of the generic invention of instant claim 2.
It is noted that the anti-CD24 antibody of the ‘761 Application comprises instant SEQ ID NOs: 17-19 and 21-23. See sequence alignments below.
Therefore, claim 23 of the ‘761 Application anticipates the instant invention.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
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Alignment of the ‘761 Application’s SEQ ID NO: 9 and fused instant SEQ ID NOs: 17-19:
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Alignment of the ‘761 Application’s SEQ ID NO: 13 and fused instant SEQ ID NOs: 21-23:
Claims 2-11, 15-17, 20, and 21 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 20, 21, and 24-29 of U.S. Application No. 18/713,398 (the ‘398 Application).
Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims and the claims in the ‘398 Application are drawn to the same or nearly the same anti-CD24 antibody or antigen binding fragment thereof having the same or nearly the same structure.
Dependent claim 20 of the ‘398 Application is drawn to a bispecific antibody but is otherwise identical to instant claim 2. Therefore, claim 20 of the ‘398 Application recites a “species” of the generic invention of instant claim 2.
It is noted that the anti-CD24 antibody of the ‘398 Application comprises instant SEQ ID NOs: 2-4 and 6-8 or 17-19 and 21-23. See sequence alignments below.
Therefore, claims 20, 21, 24-29 of the ‘398 Application anticipate the instant invention.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
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Alignment of the ‘398 Application’s SEQ ID NO: 1 and fused instant SEQ ID NOs: 2-4:
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Alignment of the ‘398 Application’s SEQ ID NO: 5 and fused instant SEQ ID NOs: 6-8:
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Alignment of the ‘398 Application’s SEQ ID NO: 9 and fused instant SEQ ID NOs: 17-19:
Alignment of the ‘398 Application’s SEQ ID NO: 13 and fused instant SEQ ID NOs: 21-23:
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Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Grace H. Lunde whose telephone number is (703)756-1851. The examiner can normally be reached Monday - Thursday 6:00 a.m. - 3:00 p.m. (EST).
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Misook Yu can be reached on (571) 272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/GRACE H LUNDE/Examiner, Art Unit 1641
/MISOOK YU/Supervisory Patent Examiner, Art Unit 1641
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