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 .
Claim Status
Claims 1, 4-5, 8-26, 35-51, 53, 59, 61-64, and 66-67 are cancelled. Claims 2, 3, 6-7, 27-34, 52, 54-58, 60, and 65 as filed on 29 June 2023 are pending and under examination.
Claim Rejections - 35 USC § 112
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.
Claims 2-3, 6-7, 28-32, 34, 52, 54-58, 60, and 65 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.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or it may be satisfied by the 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. “Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species. Ariad Pharmaceuticals Inc. v. Eli Lilly & Co., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010).
Scope of the Claimed Genus
The claims are broadly to an antigen-binding domain protein that specifically binds CD73 or a functionally active fragment of CD73.
Claim 2 provides only the limitation of an HCDR3 of SEQ ID NO: 1.
Claims 3, 6-7, 28-32, 34, 52, 54-58, 60, and 65 requires the HCDR3 of claim 2.
Claim 3 requires HCDR1, 2, and 3 of SEQ ID NO: 3, 2, and 1.
Claim 6 only adds the requirement of an LCDR3 of SEQ ID NO: 4 and claim 7 requires LCDR1, 2, and 3 of SEQ ID NO: 6, 5, and 4.
Claims 28, 30, and 32 requires VH and VL sequences of SEQ ID NO: 49 and 50 but these sequences comprise variable amino acids in the CDRs of these sequences.
Claim 29 requires a VH sequence with fully defined CDRs.
Claim 31 requires a VL sequence with fully defined CDRs but only limited to the HCDR3 of SEQ ID NO: 1.
Claims 34, 52, 54-58, 60, and 65 do not provide any further limitations to the CDR sequences of the antigen binding protein of the claims.
Summary of Species Disclosed in the original specification
Applicant identifies a CD73 binding protein comprising a VH of CDR1, 2, and 3 of SEQ ID NO: 3, 2, and 1, with a VL of CDR 1, 2, and 3 of SEQ ID NO: 6, 5, and 4 (Table 2 of specification and Examples 1-9).
State of the Relevant Art
CD73 is a GPI-anchored ectonucleotidase that is on the cell surface membrane and dephosphorylates adenosine monophosphate that produces adenosine. CD73 regulates extracellular adenosine concentration. CD73 is expressed at high levels in many types of tumors and is correlated with tumor progression and patient survival. There are multiple clinical studies showing CD73 is a potential biomarker for responses to chemotherapy, radiotherapy, and immune therapy and mouse models showing CD73 blockade induces an immune response against tumors and suppresses tumor growth and metastasis making CD73 as a potential target of immune checkpoint therapy (Sudo et. al. Intl J of Molecular Science. 21. 1-14. (2020)) (IDS) (Abstract and page 2 in par 2).
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. But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure of each monoclonal antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level. By the time the invention was made, it is well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33 (Of Record) (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1).
While affinity maturation techniques can result in differences in the CDRs of the antibody compared to its parental antibody (page 3 “The IgG Molecule”, second and third paragraphs), those techniques involve trial-and-error testing and the changes that maintain or improve affinity are not predictable a priori. E.g., id., (page 6 ending paragraph onto page 7). Further, the skilled artisan has long recognized that even minor changes in the amino acid sequences of the VH and VL, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al., Proc. Nat’l Acad. Sci. USA, 79:1979-83 (1982) (PTO-892). Rudikoff teaches that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function. E.g., Abstract. Similarly, Brown et al., J. Immunol., 156(9):3285-91 (1996) (PTO-892), teach that although a single amino acid change in CDR2 of heavy chain of a particular antibody was tolerated, the antibody lost binding upon introduction of two amino acid changes in the same region. Brown, p. 3290 and Tables 1 and 2. Table 1 of Brown shows that even a conservative substitution does not ensure that functionality of the antibody is retained. These older citations are supported my more recent discoveries of why these substitutions change antibody activity. Marvin et. al., Biochemistry, 42(23):7077-7083 (2003) (“Marvin” PTO-892) teaches that changes to the heavy and light chains altered binding affinity (Table 2) with changes to the CDR having large impacts but the changes with the largest impact were from residues in the CDR, but not from ones interfacing with the antigen ( Page 7081 in col 1 “Conclusions and Discussion” and Page 7082 in Figure 4).
The earlier work of Rudikoff and Brown is confirmed by Chiu et al., Antibodies, 8(55):1-80. (2019) (“Chiu” PTO-892). Chiu teaches that the complementarity-determining regions (HCDRs 1-3 and LCDRs 1-3) determine antigen binding requiring specific sequences and orientation of those sequences to properly form tertiary structures that can recognize and bind antigens (Page 4 in 1.2.2 first and last paragraphs and Figure 3). Chiu teaches that antibody modeling with known LCDRs 1-3, HCDR1 and HCDR2 could not predict HCDR3 In the decades since Rudikoff the field has increased understanding of antibody engineering. Structure-Based antibody engineering is unable to predict antibody sequences (Page 6 in 1.2.6, Pages 10-11 in Section 2 in particular second paragraph of page 11). Chiu notes the advancement in antibody engineering but notes it is still not possible to predict the point mutations that would improve affinity in both antibodies and multispecific molecules (Page 51 in lines 6-12).
In general, absent at least the conserved structure of the CDRs of the heavy chain and light chain of an antibody, the skilled artisan generally would not be able to visualize or otherwise predict an antibody with a particular set of functional properties would look like structurally.
Are the disclosed species representative of the claimed genus?
MPEP § 2163 states that a “representative number of species” means that the species which 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.
The specification discloses a single antigen binding protein that binds CD73 comprising a fully defined set of 6 CDRs with 3 in the variable light chain and 3 in the variable heavy chain.
Given the variability encompassed by the genus of antigen binding proteins the described species therefore cannot be considered representative of the genus.
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. To meet this requirement in the instant case, the specification must describe structural features that the skilled artisan as of the effective filing date would have expected to convey the claimed binding activity.
In the instant case, the specification does not describe a substantial structure that is shared by the members of the genus and that would allow others to visualize the genus. Neither is a structural core described that would be expected to correlate with the claimed function of binding. The structure of an antibody that provides function are the CDRs. By not defining the CDRs applicant has not provided a structure with a known function and the art shows that variation of the CDR sequences changes their function so the teaching of a single antibody CDRs does not provide structure/function for another set of CDRs.
Conclusion:
In 2017, the Federal Circuit emphasized that antibody claims do not merit special exemption from the law governing written description. In particular, the Federal Circuit rejected the notion that a disclosure can provide written description support for a claimed antibody simply by describing the target to which the antibody binds. Amgen Inc., v. Sanofi, LLC, 872 F.3d. 1367, 1378 (Fed. Cir. 2017) (finding that the “newly characterized antigen test” which “allow[ed] patentees to claim antibodies by describing . . . the antigen” to which they bind “flouts basic legal principles of the written description requirement.”). Accordingly, in order to provide written description for the claimed genus of antibodies, the Specification must disclose “either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Ariad, at 1350.
Because the specification does not describe either identifying characteristics of the genus or a representative number of species falling within the genus, the disclosure is not sufficient to show that applicant was in possession of the genus as broadly claimed.
Examiner notes that claims 27 and 33 are not included in this rejection because those claims are limited to fully defined
Claims 2-3, 6-7, 28-32, 34, 52, 54-58, 60, and 65 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a method of using the antigen binding protein that binds CD73 comprising a VH of CDR1, 2, and 3 of SEQ ID NO: 3, 2, and 1, with a VL of CDR 1, 2, and 3 of SEQ ID NO: 6, 5, and 4 in the treatment of a disease mediated by CD73 or detecting CD73 in a biological sample, does not reasonably provide enablement for an antigen-binding protein with only partially defined CDRs of the 6 required for antigen binding, a method of preventing a disease using an anti-CD73 antigen binding protein, a method of treatment using an antigen-binding protein with only partially defined CDRs, or the method of detecting CD73 in a biological sample using an antigen-binding protein with only partially defined CDRs. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether a disclosure meets the enablement requirement of 35 USC 112, first paragraph, have been described in In re Colianni, 195 USPQ 150 (CCPA 1977) and have been adopted by the Board of Patent Appeals and Interferences in Ex Parte Forman, 230 USPQ 546 (BPAI 1986). Among these factors are:
1. the nature of the invention,
2. the state of the prior art,
3. the predictability or lack thereof in the art,
4. the breadth of the claims,
5. the amount of direction or guidance present, and
6. the presence or absence of working examples.
The following is an analysis of these factors in relationship to this application.
Breadth of Claims
Claim 60 is to a method of treating or preventing a disease or disorder comprising the administration of an antigen binding protein that comprises an HCDR3 of SEQ ID NO: 1.
Claim 65 is to a method of detecting CD73 in a sample comprising administering the an antigen binding protein that comprises an HCDR3 of SEQ ID NO: 1.
Guidance/Working Examples
Applicant identifies a CD73 binding protein comprising a VH of CDR1, 2, and 3 of SEQ ID NO: 3, 2, and 1, with a VL of CDR 1, 2, and 3 of SEQ ID NO: 6, 5, and 4 (Table 2 of specification and Examples 1-9).
Applicant identifies that the CD73 binding protein binds CD73 and has anti-tumor activity (Examples 11-12).
State of the Art/Predictability
Regarding antigen binding activity:
CD73 is a GPI-anchored ectonucleotidase that is on the cell surface membrane and dephosphorylates adenosine monophosphate that produces adenosine. CD73 regulates extracellular adenosine concentration. CD73 is expressed at high levels in many types of tumors and is correlated with tumor progression and patient survival. There are multiple clinical studies showing CD73 is a potential biomarker for responses to chemotherapy, radiotherapy, and immune therapy and mouse models showing CD73 blockade induces an immune response against tumors and suppresses tumor growth and metastasis making CD73 as a potential target of immune checkpoint therapy (Sudo et. al. Intl J of Molecular Science. 21. 1-14. (2020)) (IDS) (Abstract and page 2 in par 2).
Sudo further teaches the use of antibodies that binds CD73 in detecting CD73 using FACS and imaging (pages 2-6 in Results 2.1-2.4).
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. But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure of each monoclonal antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level. By the time the invention was made, it is well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33 (Of Record) (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1).
While affinity maturation techniques can result in differences in the CDRs of the antibody compared to its parental antibody (page 3 “The IgG Molecule”, second and third paragraphs), those techniques involve trial-and-error testing and the changes that maintain or improve affinity are not predictable a priori. E.g., id., (page 6 ending paragraph onto page 7). Further, the skilled artisan has long recognized that even minor changes in the amino acid sequences of the VH and VL, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al., Proc. Nat’l Acad. Sci. USA, 79:1979-83 (1982) (PTO-892). Rudikoff teaches that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function. E.g., Abstract. Similarly, Brown et al., J. Immunol., 156(9):3285-91 (1996) (PTO-892), teach that although a single amino acid change in CDR2 of heavy chain of a particular antibody was tolerated, the antibody lost binding upon introduction of two amino acid changes in the same region. Brown, p. 3290 and Tables 1 and 2. Table 1 of Brown shows that even a conservative substitution does not ensure that functionality of the antibody is retained. These older citations are supported my more recent discoveries of why these substitutions change antibody activity. Marvin et. al., Biochemistry, 42(23):7077-7083 (2003) (“Marvin” PTO-892) teaches that changes to the heavy and light chains altered binding affinity (Table 2) with changes to the CDR having large impacts but the changes with the largest impact were from residues in the CDR, but not from ones interfacing with the antigen ( Page 7081 in col 1 “Conclusions and Discussion” and Page 7082 in Figure 4).
The earlier work of Rudikoff and Brown is confirmed by Chiu et al., Antibodies, 8(55):1-80. (2019) (“Chiu” PTO-892). Chiu teaches that the complementarity-determining regions (HCDRs 1-3 and LCDRs 1-3) determine antigen binding requiring specific sequences and orientation of those sequences to properly form tertiary structures that can recognize and bind antigens (Page 4 in 1.2.2 first and last paragraphs and Figure 3). Chiu teaches that antibody modeling with known LCDRs 1-3, HCDR1 and HCDR2 could not predict HCDR3 In the decades since Rudikoff the field has increased understanding of antibody engineering. Structure-Based antibody engineering is unable to predict antibody sequences (Page 6 in 1.2.6, Pages 10-11 in Section 2 in particular second paragraph of page 11). Chiu notes the advancement in antibody engineering but notes it is still not possible to predict the point mutations that would improve affinity in both antibodies and multispecific molecules (Page 51 in lines 6-12).
In general, absent at least the conserved structure of the CDRs of the heavy chain and light chain of an antibody, the skilled artisan generally would not be able to visualize or otherwise predict an antibody with a particular set of functional properties would look like structurally.
Regarding Prevention of Disease or Disorder Activity:
The nature of the invention is such that the composition of the instant claims must have a therapeutic benefit and be able to prevent a disease (i.e. PCOS, endometriosis, premature menopause, and cancers) from forming in a patient, much like a vaccine. The art teaches that a vaccine must be prophylactic (Stedman's Medical dictionary, 2012, page 11760, in col 1 bullets 9-10)(PTO-892). The specification does not provide any teachings of the prophylaxis of PCOS, endometriosis, premature menopause, and cancers, how to determine the individuals who will develop one or more of the conditions of the claims, nor how to effectively prevent said particular diseases before occurrence. Thus, one of skill in the art would not be able to use the composition of the invention as a preventing vaccine without undertaking to determine how to select for individuals who will develop the diseases before the said disease occurs in the individual. An effective therapeutic protocol for the treatment or prevention of the formation of any disease is subject to a number of factors, which enter the picture beyond simply the administration of the antibody claimed.
Predicting whether an individual is at risk for developing a disease is a very unpredictable art. Several factors play a role including, genetic makeup, environmental factors, age, diet, etc. Therefore, given the unpredictability of prevention and the unpredictability and the broad scope of the claims, undue experimentation would be required to use the claimed antibody as a method for preventing any disease, or prevention of even the cancers applicant has shown as a method of treating.
Regarding Treatment of Disease or Disorder Activity:
The skilled artisan recognized that it was unpredictable in the absence of in vivo experiments that each of the recited agents would be active in vivo or effective in vivo to treat cancer. The skilled artisan recognized that a combined approach of cell culture and mouse models of human cancer was most likely to predict the efficacy of new anti cancer agents. (HogenEsch et al. J. Controlled Release 2012; 164:183-186) (PTO-892). HogenEsch notes that, “it is highly unlikely that the complexity of tumors and their interactions with the host can be completely recapitulated in cell culture.” (page 2 “Tissue Culture”). HogenEsch concludes on page 6 that, while in vitro studies have a role in cancer research, they "cannot mimic the complexity of the reciprocal interactions between the growing tumor and the co-evolving microenvironment." Later reviews continue to note that the complexity of the tumor microenvironment is a primary reason that in vitro studies are not predictive of in vivo success. (Tang et al. Cancer Letters 2016; 370:85-90) (PTO-892)
Conclusion
Applicant does not provide one of skill in the art with a way to make and use the many antibodies in the methods of the claims. One of skill in the art would be left with undue experimentation to determine how to prevent any disease or disorder with a CD37 binding protein. The specification and the art do not provide one with a method of using any antibody, even the one disclosed by the applicant, in a method of preventing diseases or disorders.
The method of either detecting CD73 or treating a disease or disorder mediated by CD73 comprising administering an antigen binding protein that binds CD73 would require an antigen binding protein with fully defined CDRs of the VH and VL domains.
Applicant does not provide one of skill in the art with a way to use all of the antigen binding proteins that are encompassed within the claims. The specification provides one with the way to use only the antibody disclosed that comprises a VH of CDR1, 2, and 3 of SEQ ID NO: 3, 2, and 1, with a VL of CDR 1, 2, and 3 of SEQ ID NO: 6, 5, and 4 (Table 2 of specification and Examples 1-9).
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, 3, 6-7, 27-34, 52, 54-58, 60, and 65 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-14 of copending Application No. 18872227 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
The reference application recites an antigen binding protein that binds CD73 and comprises a HCDR3 of SEQ ID NO: 27 which matches instant SEQ ID NO: 1 (claims 1-2). The HCDR 1, 2, and 3 of instant SEQ ID NO: 3, 2, and 1 are within SEQ ID NO: 41 of the reference application thus reciting instant claims 2-3.
The VH of the claims of instant SEQ ID NO: 30 matches SEQ ID NO: 41 of the reference application and the VL of instant SEQ ID NO: 31 matches SEQ ID NO: 42 of the reference application reciting the antibody of instant claims 2-3, 6-7, 27-33, and 52.
Regarding claim 34, the reference application recites the heavy constant region comprises one derived from human heavy chain constant region (claim 33) and a constant region derived from an Igκ region (claim 48).
Regarding claims 54-55 and 57, the reference application recites a cell comprising a vector comprising a nucleic acid encoding the antibody of the claims (claims 102-104).
Regarding claim 56, the reference application recites the antibody linked to a further binding domain (claims 11, 14, 24, 27, 41, 44, and 54-56).
Regarding claim 58, the reference application recites a pharmaceutical composition comprising the antibody (claim 105).
Regarding claim 60, the reference application recites a method of detecting CD73 using the antigen binding protein of the instant claims (claim 112).
Regarding claim 65, the reference application recites preventing or treating a disease or disorder by administering the antigen binding protein of the claims (claim 107).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claims allowable.
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/F.E./Examiner, Art Unit 1643
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643