DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. Claims 1-15 are pending and currently under consideration.
The independent claim 1 is drawn to a compound comprising
a biopolymer scaffold that is an anti-CD163 antibody,
at least a first peptide n-mer of P9-S-P) (n-1), and
a second peptide n-mer of P(-S-P)(n-1),
wherein P is a peptide with a sequence length of 2-13 amino acids, S is a non-peptide spacer, and n is an integer of at least 1.
3. 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.
4. Claims 1-15 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 1-15 are indefinite in the recitation of wherein each of the peptide n-mers is bound to the biopolymer scaffold, “preferably” via a linker each (in claim 1, line 15), wherein the compound is non-immunogenic in a mammal, preferably in a human, non-human, non-human primate, sheep, pig, dog, or rodent (in claim 6), and for use in prevention or treatment of adverse reaction based on anti-drug antibodies ….. “preferably” wherein the drug is a peptide…. (in claim 12) because the metes and bounds of the phrases are ambiguous. It is not clear if a linker is encompassed linking the biopolymer scaffold to the first and the second peptides in independent claim 15. In claim 12, it is not clear if the adverse reaction s is based on what kind of drug for the anti-drug antibodies that induced adverse reactions.
Further, claim 12 is indefinite in the recitation of “in particular” in line 4 and “especially” in line 8 of the claim and “optionally” in line 1 in page 6 because it is not clear whether the narrow range, e.g. anti-AAV antibodies, after the “in particular” and enzymes etc. after the work “specially” are limitation.
Dependent claim 14 recites “such as” in line 3 and “optionally” in line 4. The phrase "such as" or “optionally” renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
For the purpose of examination and application of prior art, the limitations after the word “preferably” are not considered as limiting the scope of the claims.
5. 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.
6. Claims 1-15 are 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.
The claims are drawn to a compound comprising a biopolymer scaffold and at least a first peptide n-mer of the general formular P(-S-P)(n-1) and a second peptide n-mer of the general formular P(-S-P)(n-1)-, wherein the n is at least 1, wherein p is a peptide with a sequence length of at least 2-13 amino acids, wherein each of the peptide n-mers is bound to the biopolymer scaffold, and wherein the biopolymer is an anti-CD163 antibody. Dependent claims, e.g. claim 6 further recite that the compound is non-immunogenic. Dependent claims 9-12 further recite the function of the compound for use in therapy including prevention or treatment of an autoimmune disease or being at risk of developing the autoimmune disease. Dependent claims 13 and 15 are drawn to a method of sequestering one or more antibodies presented in an individual by administering the compound or a method of inhibiting an immune response to a treatment with an active agent in an individual by administering the compound.
The specification discloses that there are known anti-CD163 antibodies in the art (e.g. see page 15 of the specification as-filed). The specification further discloses that the anti-CD163 can be humanized, human, non-human primate, sheep, pig, dog or rodent antibody (e.g. see page 16 of the specification as-filed). Regarding the peptides that are conjugated to the anti-CD163 antibody, the specification discloses that the peptides can be one type of epitopic peptide or mixture of upto 8 different epitopic peptide (e.g. see page 20 of the specification as-filed), and preferably, the peptides are antigens identified to be involved in autoimmune diseases (e.g. see page 22 of the specification as-filed).
The specification further discloses anti-mouse-CD163 mAb E10B10 is rapidly cleared in vivo from the mouse blood making this antibody suitable as selective antibody depletion compounds (SADCs) (e.g. see Example 11 in page 119 of the specification as-filed). The specification further discloses epitope mapping of the anti-human CD163 mAB (Mac2-158) and identified highly suitable epitopes of anti-human CD163 antibodies at the SRCR domain 1 of human CD163 as well as human homologues of mouse CD163 (e.g. see Example 13).
There is insufficient written description in the specification as-filed of a compound comprising a biopolymer scaffold that is an anti-CD163 antibody and first and the second peptide with a sequence length of 2-13 amino acids as recited in the instant claims.
The claims recite a genus of a compound comprising an anti-CD163 antibody and at least a first peptide n-mer and a second peptide n-mer as part of the invention without providing a physical structure or testable functional activity for the the antibody and the peptide n-mers .
The genus of the anti-CD163 antibody and first and second n-mers are therefore extremely large. Applicant has disclosed some anti-CD163 antibodies and n-mers. Thus Applicant has disclosed only a limited species. The species of anti-CD163 antibodies do not appear to share any common structure essential to the function of CD163 binding and for use in therapy including prevention or treatment of an autoimmune disease or being at risk of developing the autoimmune disease or transplant rejection or for use in prevention or treatment of adverse reactions based on anti-drug antibodies or anti-gen delivery vector antibodies.
The claimed anti-CD163 antibodies and the n-mers lack a common structure essential for their function and the claims do not require any particular structure basis or testable functions be shared by the instant antibody and n-mers.
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 antibody 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 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.
Artisans are well aware that knowledge of a given antigen (for instance human CD40) 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). Similarly, Lloyd et al. (Protein Engineering Design & Selection 2009, 22;3:159-168) teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding, as their sequencing studies revealed that out of 841 unselected and 5,044 selected antibodies, all but one of the 49 functional VH gene segments was observed (see entire document). Goel et al. (The Journal of Immunology, 2004, 173:7358-7367) disclose the synthesis of three mAbs that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (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 antibodies that gives rise to the function of antigen binding. Further, given data such as that of Edwards et al. indicating the diversity of sequence bound 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 that bind the given antigen. Indeed, Kanyavuz et al. (Nature Review Immunology, 2019, 19: 355-368) teach that “Theoretically, under physiological conditions, the human immune system can generate BCRs with 1026 distinct sequences, an astronomical number that is far greater than the calculated number of all B cell clones that can be generated during the lifespan of a healthy human (estimated to be 4 × 1014).
As has already been pointed out none of the instant claims recite any structure for the administered compound that provides for the functions for use in therapy, in prevention or treatment, in e.g. autoimmune disease or at risk of developing the autoimmune disease.
All present utilize only functional language to describe the product which is necessarily administered in the instant claims 13 and 15.
The specification discloses epitope mapping of SRCR domain 1 of human CD163 for the two anti-CD163 antibodies mAB Mac2-158 and mAb E10B10 (e.g. see pages 121-123 of the specification as-filed).
Such disclosure does not serve to provide a written description of the genus of anti-CD163 antibody as it does not identify any specific structural feature or combination of features which give rise to the function of CD163 binding and thus could be used, for example, for therapy or the methods in instant 13 and 15.
Further, there does not appear to be any reasonable shared structure present in the genus of recited first n-mers and the second n-mers which give rise to their functional activity.
It is noted that the specification does disclose working examples which utilized two anti-CD163 antibodies mAB Mac2-158 and mAb E10B10. However, the two anti-CD163 antibodies species are not reasonably representative of the species of all possible anti-CD163 antibodies because of the structural diversity found in antibodies that bind the same antigen as discussed by for example Edwards et al., Llyod et al., and Goel et al. discussed above. Further, as has been discussed above, identifying an antibody simply on the basis of what it binds rather than by identifying the sequence/structure of the antibody in question is generally insufficient to provide sufficient written description of the antibody in question.
Therefore, in view of the breadth of the claims and the generic nature of the instant specification, artisans would reasonably conclude that applicant was not in possession of the full breadth of the anti-CD163 antibody and the first and second n-mers at the time the instant application was filed. Logically, if applicant was not in possession of the compound which is being administered, applicant also was not in possession of methods of administering such compound at the time the instant application was filed.
7. Claims 1-15 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
Factors to be considered in determining whether undue experimentation is required to practice the claimed invention are summarized In re Wands (858 F2d 731, 737, 8 USPQ2d 1400, 1404 (Fed.Cir.1988)). The factors most relevant to this rejection are the scope of the claim, the amount of direction or guidance provided, the lack of sufficient working examples, the unpredictability in the art and the amount of experimentation required to enable one of the skilled in the art to practice the claimed invention.
The scope of the claims is drawn to a compound comprising a biopolymer scaffold and at least a first peptide n-mer of the general formular P(-S-P)(n-1) and a second peptide n-mer of the general formular P(-S-P)(n-1)-, wherein the n is at least 1, wherein p is a peptide with a sequence length of at least 2-13 amino acids, wherein each of the peptide n-mers is bound to the biopolymer scaffold, and wherein the biopolymer is an anti-CD163 antibody. Dependent claims, e.g. claim 6 further recite that the compound is non-immunogenic. Dependent claims 9-12 further recite the function of the compound for use in therapy including prevention or treatment of an autoimmune disease or being at risk of developing the autoimmune disease. Dependent claims 13 and 15 are drawn to a method of sequestering one or more antibodies presented in an individual by administering the compound or a method of inhibiting an immune response to a treatment with an active agent in an individual by administering the compound.
The specification discloses that there are known anti-CD163 antibodies in the art (e.g. see page 15 of the specification as-filed). The specification further discloses that the anti-CD163 can be humanized, human, non-human primate, sheep, pig, dog or rodent antibody (e.g. see page 16 of the specification as-filed). Regarding the peptides that are conjugated to the anti-CD163 antibody, the specification discloses that the peptides can be one type of epitopic peptide or mixture of upto 8 different epitopic peptide (e.g. see page 20 of the specification as-filed), and preferably, the peptides are antigens identified to be involved in autoimmune diseases (e.g. see page 22 of the specification as-filed).
The specification further discloses anti-mouse-CD163 mAb E10B10 is rapidly cleared in vivo from the mouse blood making this antibody suitable as selective antibody depletion compounds (SADCs) (e.g. see Example 11 in page 119 of the specification as-filed).
The specification further discloses epitope mapping of the anti-human CD163 mAB (Mac2-158) and identified highly suitable epitopes of anti-human CD163 antibodies at the SRCR domain 1 of human CD163 as well as human homologues of mouse CD163 (e.g. see Example 13).
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 and use the invention commensurate in scope with these claims.
The claimed compound comprising a biopolymer scaffold that is an anti-CD163 antibody and a first peptide n-mer and a second peptide n-mer each with a sequence length of 2-13 amino acids. The compound encompasses any anti-CD163 antibodies and any peptide that is 2013 amino acids. However, the claims do not recite sufficient structural elements for the compound. The specification does not provide sufficient guidance and direction to enable any anti-CD163 antibodies and peptides with 2-13 amino acids which might be used for therapy or in a method of sequestering one or more antibodies present in an individual or method of inhibiting an immune reaction to a treatment with an active agent.
Instant claims 10, 11, and 12 also recite that the pharmaceutical composition for use in prevention of an autoimmune disease or treatment of an autoimmune disease in an individual being at risk of developing the autoimmune disease, for use in prevention of transplant rejection or eligible for transplant, or for use in prevention or treatment of adverse reactions based on anti-drug antibodies or antigen-gene delivery vector antibodies. Instant claims 13 and 15 also encompass method of sequestering one or more antibodies by administering the pharmaceutical compositions or method of inhibiting an immune reaction to a treatment with an active agent in an individual by administering the compound.
Pharmaceutical therapies in the absence of in vivo clinical data are unpredictable for the following reasons: (1) the protein may be inactivated before producing an effect, i.e. such as proteolytic degradation, immunological inactivation or due to an inherently short half-life of the protein; (2) the protein may not reach the target area because, i.e. the protein may not be able to cross the mucosa or the blood-brain barrier; (3) other functional properties, known or unknown, may make the protein unsuitable for in vivo therapeutic use.
Further, the burden of enabling the prevention of a diseases such as autoimmune disease would be greater than that of enabling a treatment due to the need to screen those humans susceptible to such diseases and the difficulty of proof that the administration of the drug was the agent that acted to prevent the condition. In addition, the specification does not provide guidance as to how one skilled in the art would go about screening those patients susceptible to autoimmune disease or being at risk of developing the autoimmune disease. Nor is guidance provided as to a specific protocol to be utilized in order to prove the efficacy of the presently claimed pharmaceutical composition in preventing these diseases.
The instant specification discloses working examples of SADCs with haptoglobin biopolymer scaffold that binds CD163 (but not anti-CD163 antibody) (e.g. see Examples 1-3 and 5-8 in the specification as-filed). Example 4 proposed the use of anti-CD163 antibody and peptide screened but does not show any examples of anti-CD163 antibody and any particular first and second n-mers. Example 10 appears to also propose anti-CD163 antibodies Mac-158 or Mac2-48 as biopolymer scaffold and specific peptides sequences LQQQNT or TTTGQNNNS, both peptides are identified as AAC-8-neutralizing antibodies that hamper gen therapy and proposed that administering the biopolymer scaffold to an individual who will undergo gene therapy with AAAC-8 as vector can increase efficiency of the gene therapy. Examples 11-13 discloses epitopes for the antibodies Mac-158 or Mac2-48. There is no in vivo data showing that anti-CD163 biopolymer scaffold comprising n-mers.
The instant specification relies upon screening for n-mers as well as screening for anti-CD163 antibodies. The specification appears to discloses two anti-CD163 antibodies and some specific n-mers. The in vivo animal models do not use the anti-CD163 antibodies but rather use haptoglobin biopolymer scaffold. The claims are not limited to the a single class of compounds but rather encompasses a broad range of distinct compounds that defined as the antigen CD163 or any or all n-mers with 2-13 amino acids for use in therapy, in preventing and treating an autoimmune disease, transplant rejection or adverse reactions based on anti-drug antibodies or anti-gene delivery vector or to be administered to sequester one or more antibodies/inhibit an immune reaction.
The scope of the claims encompasses a genus of anti-CD163 antibodies and peptides defined only by the number of amino acids (2-13 amino acid residues). There is insufficient objective evidence that two specific anti-CD163 antibodies, the anti-mouse-CD163 mAb E10B10 and the anti-human CD163 mAB (Mac2-158) as disclosed in the specification as-filed can be extrapolated to enable the genus of anti-CD163 antibody.
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 antibody 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 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.
Artisans are well aware that knowledge of a given antigen (for instance human CD40) 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). Similarly, Lloyd et al. (Protein Engineering Design & Selection 2009, 22;3:159-168) teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding, as their sequencing studies revealed that out of 841 unselected and 5,044 selected antibodies, all but one of the 49 functional VH gene segments was observed (see entire document). Goel et al. (The Journal of Immunology, 2004, 173:7358-7367) disclose the synthesis of three mAbs that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (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 antibodies that gives rise to the function of antigen binding. Further, given data such as that of Edwards et al. indicating the diversity of sequence bound 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 that bind the given antigen. Indeed, Kanyavuz et al. (Nature Review Immunology, 2019, 19: 355-368) teach that “Theoretically, under physiological conditions, the human immune system can generate BCRs with 1026 distinct sequences, an astronomical number that is far greater than the calculated number of all B cell clones that can be generated during the lifespan of a healthy human (estimated to be 4 × 1014).
The scope of the required enablement varies inversely with the degree of predictability involved and in cases involving unpredictable factors such as physiological activity more may be required. See MPEP 2164.03 and 2164.02.
Given the relatively incomplete understanding in the biotechnological field involved and the lack of a reasonable correlation between the narrow disclosure in the specification and broad scope of protection sought in the claims; the lack of enablement is deemed appropriate. See MPEP 2164.08.
In view of the lack of predictability of the art to which the invention pertains, the claimed compound comprising an anti-CD163 antibody as a biopolymer scaffold and first and second n-mers with a sequence length of 2-13 amino acids for preventing or treating disease such as autoimmune disease, organ transplant, and method of sequestering one or more antibodies by administering the compound, and method of inhibiting an immune reaction to a treatment with an active agent by administering the compound would be unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue.
8. 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.
9. Claims 1-15 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of copending USSN 18/246,117 (‘117 application).
Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the claims in the ‘117 application are drawn to the same compound comprising a biopolymer scaffold that is an anti-CD163 antibody (see claim 7 of the ‘117 application) and a method of sequestering one or more antibodies in an individual by administering the compound. Therefore, the claims in the ‘117 application would anticipate the instant invention.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
10. No claim is allowed.
11. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHUN DAHLE whose telephone number is (571)272-8142. The examiner can normally be reached Mon-Fri 6:30am-4:00pm.
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/CHUN W DAHLE/Primary Examiner, Art Unit 1641