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 .
Claims 42-61 are pending and are under consideration.
Acknowledgment is made of applicant’s earliest effective filing date of 12/25/2020 based on PCT/CN2020/139556.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claim(s) 42-43, 45-46, 53-61 is/are rejected under 35 U.S.C. 102(a1) as being anticipated by US Patent 9079949, (Andrien et al. July 14, 2015, IDS).
Regarding Claim 42(i), Adrien et al. teach an anti-C5 isolated antibody comprising H-CDRs 1, 2, 3, comprising SEQ ID NO: 3, 4, 5, respectively. They also teach that the L-CDRs (1-3) comprise SEQ IDs 6, 7, 8. Respectively, the VH of the prior art comprises SEQ ID NO:9 and the VL comprises SEQ ID NO:2.
Adrien et al. teach [columns 19-20, see partial copy of Table 1 below] that their anti-CD5 light chain variable region comprises SEQ ID NO:8 and can have 4 histidine substitutions at positions G31, L33, V91, and T94. Similarly, their heavy chain variable region comprises SEQ ID NO:7 and can have 4 histidine substitutions at positions Y27, I34, L52, and S57.
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Below is an amino acid comparison of applicant’s VL chain (SEQ ID NO:2, Claim 43) with the VL chain of the prior art (SEQ ID NO:8). Boxed regions indicate CDRS 1, 2, and 3 respectively which are 100% identical. Thus, this also anticipates Claim 43 wherein the VL comprises SEQ ID NO:2.
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Regarding the heavy chain regions, below is an amino acid comparison of applicant’s VH chain (SEQ ID NO:9, Qy, Claim 43) with the VH chain of the prior art (SEQ ID NO:7, Db). Boxed regions indicate CDRS 1, 2, and 3 respectively. However, in this instance, we see one amino acid difference (Y27). But, the prior art clearly indicates that Y27 can be a histidine as set forth in Table I.
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Thus, claims 42(i) and 43(i) are clearly anticipated.
As to claims 45-46, Andrien et al. teach (column 9, lines 48+, column 11, line 14)) that in some embodiments, any of the antibodies or fragments described herein are humanized, fully human, deimmunized, or chimeric. In some embodiments, an antibody or fragment thereof described herein can be, e.g., a recombinant antibody, a single chain antibody, a diabody, an intrabody, an Fv fragment, an Fd fragment, an Fab fragment, an Fab′ fragment, and an F(ab′)2 fragment.
As to claims 53-54, 56-57, Andrien et al. teach (column 33, lines 4+) that the antibodies or antigen-binding fragments thereof described herein can be produced using a variety of techniques known in the art of molecular biology and protein chemistry. For example, a nucleic acid encoding one or both of the heavy and light chain polypeptides of an antibody can be inserted into an expression vector that contains transcriptional and translational regulatory sequences, which include, e.g., promoter sequences, ribosomal binding sites, transcriptional start and stop sequences, translational start and stop sequences, transcription terminator signals, polyadenylation signals, and enhancer or activator sequences. The regulatory sequences include a promoter and transcriptional start and stop sequences. In addition, the expression vector can include more than one replication system such that it can be maintained in two different organisms, for example in mammalian or insect cells for expression and in a prokaryotic host for cloning and amplification.
As to claim 58-60, Andrien et al. teach (column 10, lines 45+, column 37) that the compositions described herein can be formulated as a pharmaceutical solution, e.g., for administration to a subject for the treatment or prevention of a complement-associated disorder. The administration of the antibodies per se are designed to reduce the activity of the complement system.
As to claim 55, 61, Andrien et al. teach (column 40, lines 37+) that nucleic acids encoding a therapeutic polypeptide can be incorporated into a gene construct to be used as a part of a gene therapy protocol to deliver nucleic acids that can be used to express and produce agents within cells. Expression constructs of such components may be administered in any therapeutically effective carrier, e.g. any formulation or composition capable of effectively delivering the component gene to cells in vivo. Approaches include insertion of the subject gene in viral vectors including recombinant retroviruses, adenovirus, adeno-associated virus, lentivirus, and herpes simplex virus-1 (HSV-1), or recombinant bacterial or eukaryotic plasmids.
Claim Rejections - 35 USC § 103
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 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claim 48 is/are rejected under 35 U.S.C. 103 as being obvious over US Patent 9079949, (Andrien et al. July 14, 2015, IDS) as applied to Claim(s) 42-43, 45-46, 53-61 above, in further view of Silva et al. (J.Biol.Chem., 290 (9), 2015).
Claim 48 is drawn to two specific Fc regions comprising amino acid residues 99-327 of SEQ ID Nos: 26 or 27. SEQ ID NO:26 and 27 comprise the hinge region, the CH2 domain and the Ch3 domain of a human IgG4 antibody. Collectively, these components form the Fc (fragment crystallizable) region and include known mutations.
While Adrien does not specifically teach the claimed IgG4 sequences, they do teach that that the anti-C5 human antibody can comprise the constant regions 2 and 3 of human IgG4 (See Figure 30). Adrien et al. teach (column 8, lines 5+, column 25, lines 11+) that in some embodiments, any of the antibodies or fragment thereof comprise a variant human Fc constant region (e.g., a variant human IgG Fc constant region) that binds to human neonatal Fc receptor (FcRn) with greater affinity than that of the native human Fc constant region from which the variant human Fc constant region was derived. Substitutions that enhance the binding affinity of an antibody Fc constant region for FcRn are known in the art and include, e.g., (1) the M252Y/S254T/T256E triple substitution described by Dall'Acqua et al. (2006) J Biol Chem 281: 23514-23524; (2) the M428L or T250Q/M428L substitutions described in Hinton et al. (2004) J Biol Chem 279:6213-6216 and Hinton et al. (2006) J Immunol 176:346-356; and (3) the N434A or T307/E380A/N434A substitutions described in Petkova et al. (2006) Int Immunol 18(12):1759-69.
Claim 48 is drawn to two specific Fc regions comprising amino acid residues 99-327 of SEQ ID Nos: 26 or 27. SEQ ID NO:26 and 27 are well known in the art as comprising the standard Fc region of IgG4 with known improved mutations. For example, amino acids 99-327 of SEQ ID NO:26 and SEQ ID NO:27 comprise the S228P mutation. Silva et al. (J.Biol.Chem., 290 (9), 2015) demonstrated that the core-hinge stabilized serine 228 to proline (S228P) mutation prevents in vivo and in vitro IgG4 Fab-arm exchange. SEQ ID NO:27 includes the M428L and N434A mutations which are both taught by Adrien et al. A sequence homology comparison of amino acids 99-327 of SEQ ID NO:26 (Qy) and 27(Db) is shown below:
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One of ordinary skill in the art at the time of filing would consider it prima facie obvious for Adrien et al. to incorporate the IgG4 Fc regions as specifically claimed because both sequences were known as standard IgG4 Fc regions with known mutations that improve therapeutic efficacy. Specifically, both sequences incorporate the S228P mutation (at the 11th position in the sequence comparison above) which prevents Fab-arm exchange creating a more stable IgG4 molecule. Further, Adrien et al. specifically references the other two boxed substitutions that enhance the binding affinity of an antibody Fc constant region for FcRn. Thus, all the claimed elements were known in the prior art and one skill in the art would/could have combined the elements as claimed by known methods with no change in their respective functions, and the combination would yield nothing more than predictable results to one of ordinary skill in the art.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 49-51 is/are further rejected under 35 U.S.C. 103 as being obvious over US Patent 9079949, (Andrien et al. July 14, 2015, IDS) as applied to claim 42 above in the 102(a)(1) rejection, in view of Song et al. (US20220204602, April 24, 2019, IDS)
The applied reference has common applicants/inventors with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(2).
This rejection under 35 U.S.C. 103 might be overcome by: (1) a showing under 37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in accordance with 35 U.S.C.102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public disclosure under 35 U.S.C. 102(b)(2)(B); or (3) a statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing date of the claimed invention, the subject matter disclosed and the claimed invention were either owned by the same person or subject to an obligation of assignment to the same person or subject to a joint research agreement. See generally MPEP § 717.02.
Adrien et al. teach as set forth above.
Adrien et al. do not teach a fusion protein comprising anti-human C5 antibody fused to a factor H polypeptide or fragment thereof (Claim 49). And, wherein the factor H polypeptide or fragment therof comprises short consensus repeat domains 1-4 of Factor H (Claim 50). And, wherein the idolaed anti-human C5 antibody is an anti-human C5 full-length antibody, and wherein the factor H polypeptide or fragment thereof is fused to the C-terminus of at least one of the heavy chains of the anti-human C5 full-length antibody (Claim 51).
Song et al. teach [0005] that blocking C5 activation should prevent C5a and the membrane attack complex (MAC) and be of therapeutic value. A humanized mouse anti-human C5 mAb, eculizumab has been used to treat two complement-mediated diseases paroxysmal nocturnal hemoglobinuria 2 (PNH) and atypical hemolytic uremic syndrome (aHUS). However, not all PNH patients are responsive to eculizumab treatments and one of the reasons for non-responsiveness is genetic polymorphism of human C5 with loss of epitope binding to eculizumab. Additionally, due to high plasma concentration of C5 and targeted-mediated rapid removal of antibody, eculizumab has to be administered to patients at high doses and frequency. Thus, more effective and more convenient anti-complement drugs are needed, both in the treatment of PNH and aHUS, and in other complement-mediated diseases. Song et al. teach one solution to this problem was to fuse Factor H to anti-C5 antibody. Song et al. teach [0484] that the anti-C5 mAb-FH fusion protein was much more potent than their corresponding parent mAb and benchmark regular anti-C5 mAbs (Eculizumab and Ravulizumab) in inhibiting rabbit RBC and PNH RBC lysis. Further, the anti-C5 mAb-fusion protein, but not the corresponding parent anti-mAb or benchmark anti-C5 mAbs (Eculizumab and Ravulizumab), was further shown to inhibit C3 opsonization of rabbit and PNH RBCS. Regarding the structure of the antibody-fusion product Song et al. teach [0011] that fragments of Factor H may be incorporated into the fused product such as the short consensus repeat (SCR) domains 1-5 of the FH protein. Further, Song et al. teach [0371, 0258] that the anti-C5 antibody can be an anti-human C5 full-length antibody and that the fusion protein comprises a fusion protein partner (e.g., FH or a functional fragment thereof) fused to C-terminal of a VH sequence of the antibody.
One of ordinary skill in the art at the time of filing would consider it prima facie obvious for the inventors of Adrien et al. (having read the specification of Song et al.) to also make anti-C5 antibody protein fusions that incorporated Factor H polypeptides or fragments thereof because both references discuss improving anti-C5 antibodies to treat complement-associated diseases or disorders. One would have been motivated to make the fusion because Song et al. specifically teaches that not all nocturnal hemoglobinuria 2 (PNH) patients are responsive to eculizumab treatments and that one of the reasons for this non-responsiveness is genetic polymorphism of human C5 with loss of epitope binding to eculizumab. Thus, given the success of Song’s fusion protein, one of ordinary skill would have been motivated to combine the teachings to arrive at the claimed invention so that there would be an even greater therapeutic effect. This is somewhat analogous to the decision in In re Kerkhoven: "It is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the same purpose, in order to form a third composition to be used for the very same purpose.... [T]he idea of combining them flows logically from their having been individually taught in the prior art." In re Kerkhoven, 626 F.2d 846, 850, 205 USPQ 1069, 1072 (CCPA 1980).
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 59 and 61 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 treating paroxysmal nocturnal hemoglobinuria (PNH), atypical hemolytic uremic syndrome (aHUS), myasthenia gravis, or neuromyelitis optica, does not reasonably provide enablement for treating any and all complement-associated diseases or conditions. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to practice the invention commensurate in scope with these claims.
The focus of the enablement inquiry is whether everything within the scope of the claim(s) is/are enabled, at the time of filing, without requiring undue experimentation to make or use the invention. The factors to be considered in determining whether a disclosure would require undue experimentation include: (A) The breadth of the claims; (B) The nature of the invention; (C) The state of the prior art; (D) The level of one of ordinary skill; (E) The level of predictability in the art; (F) The amount of direction provided by the inventor; (G) The existence of working examples; and (H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure. In re Wands, 8 USPQ2d, 1400 (CAFC 1988) and MPEP 2164.01.
The breadth of the claims: With respect to claim breadth, the standard under 35 U.S.C. §112(a) or 35 U.S.C. §112, first paragraph, entails the determination of what the claims recite and what the claims mean as a whole. The claims are broadly drawn to treating an individual having a complement-associated disease or condition comprising administering pharmaceutical compositions comprising the isolated anti-human C5 antibodies of Claim 42.
The specification teaches [0035] that such complement diseases or conditions may comprise macular degeneration (MD), age-related macular degeneration (AMD), ischemia reperfusion injury, arthritis, rheumatoid arthritis, lupus, ulcerative colitis, stroke, post-surgery systemic inflammatory syndrome, asthma, allergic asthma, chronic obstructive pulmonary disease (COPD), paroxysmal nocturnal hemoglobinuria (PNH) syndrome, myasthenia gravis, neuromyelitis optica, (NMO), multiple sclerosis, delayed graft function, antibody-mediated rejection, atypical hemolytic uremic syndrome (aHUS), central retinal vein occlusion (CRVO), central retinal artery occlusion (CRAO), epidermolysis bullosa, sepsis, organ transplantation, inflammation (including, but not limited to, inflammation associated with cardiopulmonary bypass surgery and kidney dialysis), C3 glomerulopathy, membranous nephropathy, IgA nephropathy, glomerulonephritis (including, but not limited to, anti-neutrophil cytoplasmic antibody (ANCA)-mediated glomerulonephritis, lupus nephritis, and combinations thereof), ANCA-mediated vasculitis, Shiga toxin induced HUS, and antiphospholipid antibody-induced pregnancy loss, or any combinations thereof.
The state of the prior art and the level of predictability in the art: Hillman et al. (N Engl J Med 2006;355:1233-43) teach that the complement inhibitor Eculizumab (anti-C5) is an effective therapy for paroxysmal nocturnal hemoglobinuria (PNH). Wong et al. (Translational Research, Vol 165, Issue 2, February 2015) teach (introduction) that Eculizumab remains the first and only inhibitor of the complement system used in clinical practice. Specifically, it targets the terminal complement pathway and leaves the proximal complement pathways intact. It was approved by the United States Food and Drug Administration and the European Medicines Agency in 2007 for the treatment of paroxysmal nocturnal hemoglobinuria (PNH) and in 2011 for the treatment of atypical hemolytic uremic syndrome (aHUS). Similarly, Dhillon (Drugs (2018) 78:367–376) discusses the use of eculizumab in a review of generalized myasthenia gravis. Specifically, Dhillon teaches (page 368, 2nd column) that Eculizumab is a recombinant humanized monoclonal IgG2/4K antibody that binds to human C5 complement protein and inhibits the activation of terminal complement and that it is the first targeted complement inhibitor approved worldwide for the treatment of complement-mediated diseases, including paroxysmal nocturnal haemoglobinuria (PNH) and atypical haemolytic uremic syndrome (aHUS). Recently, eculizumab was also approved for the treatment of adults with anti-AChR antibody-positive gMG in the USA, anti-AChR antibody-positive refractory gMG in the EU or patients with anti-AChR antibody-positive gMG whose symptoms are difficult to control with high-dose IVIg therapy or PLEX in Japan.
While the above indicates some predictability of treating a few species of diseases associated with complement-associated disorders, the state of the art does not extrapolate to any and all such diseases. For example, it would not be predictable that the claimed antibodies of Claim 42 would successfully treat Shiga toxin E. coli related hemolytic uremic syndrome (STEC-HUS). As evidenced by Buelli et al. (Microorganisms, 2019 Jan 10;7(1)), a large body of evidence collected over the last three decades shows that complement activation contributes to the pathophysiology of STEC-HUS. Moreover, the FDA approval labeling and prescribing usage for Eculizumab (FDA, revised: 04/2025) specifically teaches that Eculizumab is not indicated for the treatment of patients with Shiga toxin E. coli related hemolytic uremic syndrome (STEC-HUS). See also Garnier et al., J Am Soc Nephrol. 2023 Jun 12;34(9):1561–1573; In pediatric patients with STEC-HUS, eculizumab treatment does not appear to be associated with improved renal outcome during acute phase of the disease.
Further, the instant specification does not provide any in vitro or in vivo data demonstrating the efficacy of treating a specific complement-related disease or condition. This lack of experimental guidance in view of the complexities of antibody-based therapy would not permit one of skill in the art to reasonably predict or conclude that the claimed method would treat any and all complement-related diseases or conditions.
The quantity of experimentation needed to make or use the invention based on the content of the disclosure: The standard of an enabling disclosure is not the ability to make and test if the invention works but one of the ability to make and use with a reasonable expectation of success. A patent is granted for a completed invention, not the general suggestion of an idea (MPEP 2164.03 and Chiron Corp. v. Genentech Inc., 363 F.3d 1247, 1254, 70 USPQ2d 1321, 1325-26 (Fed. Cir. 2004)). The instant specification is not enabling for the invention as broadly claimed because one cannot follow the guidance presented therein, or within the art at the time of filing, and perform the method claimed without first making a substantial inventive contribution. See also OSI Pharm., LLC v. Apotex Inc., 939 F.3d 1375, 1385, 2019 USPQ2d 379681 (Fed. Cir. 2019) ("These references provide no more than hope—and hope that a potentially promising drug will treat a particular cancer is not enough to create a reasonable expectation of success in a highly unpredictable art such as this. Indeed, given a 99.5% failure rate and no efficacy data or any other reliable indicator of success, the only reasonable expectation at the time of the invention was failure, not success.").
Thus, while being enabling for treating some complement-associated disorders like paroxysmal nocturnal hemoglobinuria (PNH), atypical hemolytic uremic syndrome (aHUS), myasthenia gravis, or neuromyelitis optica, there is no evidence to suggest that the antibodies of Claim 42 could predictably treat all diseases or conditions associated with the complement pathway.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 47 and 52 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 47 (and 52) is drawn anti-C5 antibodies comprising the VL chain of either SEQ ID NO:23 or 18. However, these sequences do not further limit the subject matter of ultimate claim 42 as they do not appear to comprise the claimed CDRs of Claim 42. For example, Claim 42(viii) has an L-CDR 3 of SEQ ID NO:17 which is QNVLNTPLH. However, the VL chain of SEQ ID NO:18 in Claim 47 does not appear to have the same L-CDR3 (QNVLNTPLT) as there is a histidine/threonine difference. Thus, the scope of claim 47 or 52 does not clearly limit Claim 42. Applicant may wish to scrutinize the other sequences in Claim 47/52 for failing to further limit Claim 42 as SEQ ID NO:23 also appears to have the same issue.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Allowable Subject Matter
Claim 44 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims. US Patent 9079949, (Andrien et al. July 14, 2015, IDS) does not teach the Q38R mutation. Further, even though SEQ ID NO:2 with the Q38R mutation is known as the light chain variable region of the anti-C5 antibody known as pexelizumab, there is nothing to suggest that Andrien et al. would have incorporated this structure into their anti-C5 antibody structures because pexelizumab is no longer under active clinical development as primary endpoints were not met in several clinical trials.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to GARY B NICKOL, Ph.D. whose telephone number is (571)272-0835. The examiner can normally be reached M-F 9AM-5:30PM.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Julie Wu can be reached at 571-272-5205. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/GARY B NICKOL/Primary Examiner, Art Unit 1643