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 .
Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statement (IDS) was submitted on 6/21/2023 before the mailing of a first office action. The submissions are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Status
Claims 1-2, 7-11, 16-19, 21-24, 27, 28, and 30, filed 6/21/2023, are pending. Claims 1-2, 7-11, 16-19, 21-24, 27, 28, and 30 are under examination.
Claim Interpretation
In order to advance compact prosecution, for purposes of examination, claim 24 shall be interpreted to refer to claim 1 only.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 24 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Regarding claim 24, claim 24 refers to claims 1 to 16. Some of these claims, for example, claims 3-6, have been canceled. MPEP 608.01(n)(V) states: “If the base claim has been canceled, a claim which is directly or indirectly dependent thereon should be rejected as incomplete.” Consequently, claim 24 is rejected as incomplete.
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 17-19 and 21-24 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.
Regarding claim 17, claim 17 recites a method of treating or preventing a cancer comprising administering a compound of formula (I) or a pharmaceutically acceptable salt thereof according to claim 1.
Formula I as recited by claim 1 has several positions with wide variability: Xaa1 and Xaa4 are any hydrophobic amino acid, Xaa3 is any small side chain amino acid, and Xaa5 is any polar uncharged amino acid. The specification includes at least 30 entries for hydrophobic residues, at least 20 entries for small side chain residues, and at least 25 entries for polar uncharged residues. This yields a minimum sequence space of 30*30*25*20 = 450,000, which is still an underestimate due to the other variable positions and the claimed residue groups being somewhat larger than what was used in the calculation.
In this case, 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, 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 inventor was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. (MPEP § 2163 (II.A.3.a.ii.))
According to MPEP § 2163 (II.A.3.a.ii.), 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. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014).
As described above, claim 1 recites extremely large genus of peptides. The claimed peptides must possess the disclosed activity against cancer.
MPEP § 2163 (II.A.3.a.ii.) states that “for inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus. See, e.g., Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’”
Even when several species are disclosed, these are not necessarily representative of the entire genus. AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (“The ’128 and ’485 patents, however, only describe species of structurally similar antibodies that were derived from Joe-9. Although the number of the described species appears high quantitatively, the described species are all of the similar type and do not qualitatively represent other types of antibodies encompassed by the genus.”). Thus, when there is substantial variation within the genus, as here, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. Since each genus recited in the instant claims is large, it would be very challenging to describe sufficient species to cover the structures of the entire genus.
In the instant case, Applicant provides in silico docking data for nineteen peptides of the invention, sufficient to enable the skilled artisan to identify peptides that yield polypeptides with the recited properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336 (Fed. Cir. 2010); see also Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1876 (Fed. Cir. 2011) (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”) Absent the conserved structure provided by the provided species, the skilled artisan generally would not be able to visualize or otherwise predict, a priori, what peptide with a particular set of properties would look like structurally.
Applicant provides in silico docking data for nineteen peptides and reduces one sequence, SEQ ID NO: 1 to practice for testing. At the time the invention was made, the level of skill for preparing peptides with desired functional properties was high. However, even if a synthesis and selection procedure was, at the time In this case, 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, 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 inventor was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. (MPEP § 2163 (II.A.3.a.ii.))
Applicant reduces only SEQ ID NO: 1 to practice and presents in silico data for a total of nineteen peptides. Only two peptides disclosed used the S-S disulfide cyclization method. Only SEQ ID NO: 1 is confirmed to exhibit the required activity in a wet lab setting. Therefore, the provided examples only represent a limited structural diversity.
Since only a limited number of species of peptides are taught within the claimed genus above, the instant claim above fails the written description requirement. A representative number of species has not been taught to describe this genus. Regarding the peptides, a single point mutation can change the biophysical properties of a peptide: “In summary, we have shown that the structural changes in the fibrillar state of the Aβ42 peptide that are observed to occur upon introduction of single point mutations can be accompanied by changes in the dominance of the microscopic processes by which these aggregates are themselves formed.” (Bolognesi et al. ACS Chem Bio 9:2 (2013) page 381 col. 2 para. 3) and “In summary, while ovispirin-1 and novispirin G-10 both had solution structures that were helical and amphipathic in the presence of TFE, a relatively simple change in their primary structure (a single glycine–isoleucine exchange) had profound effects on their respective toxicities for human erythrocytes and epithelial cells.” (Sawai et al. Protein Eng. 15:3 (2002) page 232 col. 1 para. 3).
Furthermore, many sequences allowed by the current scope of the claims, result in non-functional aggregates. Wang (Wang, et al. MAbs. Vol. 1. No. 3. Taylor & Francis, (2009)) discloses a variety of aggregation prone motifs that occur in commercial antibodies (Wang, page 262, Table 2). The scope of the claims currently may incorporate such motifs and result in non-functional aggregates.
Given this unpredictability of protein design, the skilled artisan would not have been in possession of the substantial repertoire of peptide species encompassed by the claimed invention; one of skill in the art would conclude that applicant was not in possession of the structural attributes of a representative number of species possessed by the members of the genus of every peptide molecule recited by claim 17. One of skill in the art would conclude that the specification fails to disclose a representative number of species to describe the claimed genus. Therefore, claim 17 is rejected.
Regarding claim 18, claim 17 is rejected as described above. Claim 18 does not change the size of the claimed genus of peptides. Consequently, the specification fails to disclose a representative number of species to describe the claimed genus and claim 18 is rejected.
Regarding claim 19, claim 18 is rejected as described above. Claim 19 does not change the size of the claimed genus of peptides. Consequently, the specification fails to disclose a representative number of species to describe the claimed genus and claim 19 is rejected.
Regarding claim 21, claim 19 is rejected as described above. Claim 21 does not change the size of the claimed genus of peptides. Consequently, the specification fails to disclose a representative number of species to describe the claimed genus and claim 21 is rejected.
Regarding claim 22, claim 22 recites a method of inhibiting urokinase plasminogen activator and/or a matrix metalloproteinase comprising contacting the urokinase plasminogen activator and/or matrix metalloprotease with a compound of formula (I) according to claim 1 or a pharmaceutically acceptable salt thereof.
Claim 22 recites a different required activity than claim 17, However, claim 22 recites a genus of peptides with the same scope as claim 17 and is therefore rejected for the same reasons as claim 17 as described above.
Regarding claim 23, claim 22 is rejected as described above. Claim 23 does not change the size of the claimed genus of peptides. Consequently, the specification fails to disclose a representative number of species to describe the claimed genus and claim 23 is rejected.
Regarding claim 24, claim 24 recites method of inhibiting tumor cell invasion in a brain tumor comprising administering to the brain tumor with a compound of formula (I) according to claim 1 or a pharmaceutically acceptable salt thereof.
Claim 24 recites a different required activity than claim 17, However, claim 24 recites a genus of peptides with the same scope as claim 17 and is therefore rejected for the same reasons as claim 17 as described above.
Claims 17-19, 21-24, 27, 28, and 30 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 SEQ ID NOs: 1-9, 12, and 23-24, and 26-30 treating, reducing, are ameliorating cancers in the form of glioblastomas and other cancers susceptible to the modulation of MMP proteins MM-2 and MM-9 and for SEQ ID NO: 1 treating, reducing, are ameliorating cancers in the form of glioblastomas and other cancers susceptible to the modulation of uPa protein, does not reasonably provide enablement for any peptide recited by Formula I to treat any possible cancer. No peptide is enabled for the prevention of any cancer. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims.
In order to determine compliance with the enablement requirement of 35 U.S.C. 112(a), the Federal Circuit developed a framework of factors in In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988), referred to as the Wands factors to assess whether any necessary experimentation required by the specification is "reasonable" or is "undue." Consistent with Amgen Inc. et al. v. Sanofi et al., 598 U.S. 594, 2023 USPQ2d 602 (2023), the Wands factors continue to provide a framework for assessing enablement in a utility application or patent, regardless of technology area. Guidelines for Assessing Enablement in Utility Applications and Patents in View of the Supreme Court Decision in Amgen Inc. et al. v. Sanofi et al., 89 FR 1563 (January 10, 2024). These factors include, but are not limited to:
The breadth of the claims;
Clam 1 recites an extremely broad range of peptides and claim 17 recites any possible cancer type.
The nature of the invention;
The invention is a series of peptides which modulate MMP proteins and uPa proteins, and thereby treat cancers susceptible to modulation of these proteins, such as glioblastomas.
The state of the prior art;
Roomi et al. (Roomi, M. W., et al. Oncology reports 21.5: 1323-1333. (2009)) discusses the roles of MMP-2 and MM-9 in cancers: “MMP-2 and MMP-9 secretion is elevated in several types of human cancers and their elevated expression has been associated with poor prognosis. (Roomi, et al., page 1323, Abstract.)
Hadler-Olsen et al. (Hadler-Olsen, et al. Tumor Biology 34.4: 2041-2051 (2013)) further discusses the role of MMPs in cancer: “ This is a family of proteolytic enzymes that are involved in many phases of cancer progression, including angiogenesis, invasiveness, and metastasis. It has therefore been expected that MMPs could serve as both diagnostic and prognostic markers in cancer patients, but despite a huge number of studies, it has been difficult to establish MMPs as cancer biomarkers.” (Hadler-Olsen et al., page 2041, Abstract).
Hadler-Olsen also describes this area of research as very unpredictable: “Many MMP members have overlapping substrate specificity, illustrating a high degree of redundancy among them. This makes it difficult to predict the actual function of a specific MMP in cancer.” (Hadler-Olsen et al., page 2042, col. 1, para. 4). However, Hadler-Olsen also discloses that MMPs are implicated in breast, colorectal, prostate, and lung cancer. (Hadler-Olsen et al., page 2045-2046).
Scherer (Scherer et al. Cancer and Metastasis Reviews 27.4: 679-690 (2008)) provides a summary of the complex role of MMP in cancers: “MMP expression is generally present in higher amounts in and around malignant cancers compared to normal, benign, or premalignant tissues. For example, in melanomas the expression of MMP9 is associated with the conversion from radial growth phase to vertical growth phase and subsequent metastasis [7]. MMP2 is highly expressed in breast cancers, but the ratio of activated to total MMP2 levels increases as the disease progresses to metastasis, increasing with tumor grade [8, 9]. MMPs are often associated with the removal of the ECM barrier to allow cancer cells to invade and metastasize.” (Scherer, page 680, col. 2, para. 2).
The level of one of ordinary skill;
A person of ordinary skill in the art typically would possess at least a Master’s level education and frequently a Ph.D.
The level of predictability in the art;
Protein-protein interactions are very unpredictable in general. A single point mutation can change the biophysical properties of a peptide: “In summary, we have shown that the structural changes in the fibrillar state of the Aβ42 peptide that are observed to occur upon introduction of single point mutations can be accompanied by changes in the dominance of the microscopic processes by which these aggregates are themselves formed.” (Bolognesi et al. ACS Chem Bio 9:2 (2013) page 381 col. 2 para. 3) and “In summary, while ovispirin-1 and novispirin G-10 both had solution structures that were helical and amphipathic in the presence of TFE, a relatively simple change in their primary structure (a single glycine–isoleucine exchange) had profound effects on their respective toxicities for human erythrocytes and epithelial cells.” (Sawai et al. Protein Eng. 15:3 (2002) page 232 col. 1 para. 3).
Furthermore, many sequences allowed by the current scope of the claims, result in non-functional aggregates. Wang (Wang, et al. MAbs. Vol. 1. No. 3. Taylor & Francis, (2009)) discloses a variety of aggregation prone motifs that occur in commercial antibodies (Wang, page 262, Table 2). The scope of the claims currently may incorporate such motifs and result in non-functional aggregates.
(F) The amount of direction provided by the inventor and the existence of working examples and the quantity of experimentation needed to make or use the invention based on the content of the disclosure.
Regarding claim 17, claim 17 recites a method of treating or preventing a cancer comprising administering a compound of formula (I) or a pharmaceutically acceptable salt thereof according to claim 1.
As discussed above, Formula I encompasses a huge range of peptides for which only nineteen peptides are docked against an MMP target. Of note, SEQ ID NOs: 14 and 25 do not appear to be predicted to bind correctly.
Regardless, there is no limit to the scope of peptides claimed by formula (I) in claim 17 and this would certainly require undue experimentation to test each of these peptides in a clinical setting, particularly when only data for one such peptide is provided by the specification.
Furthermore, the scope of the claimed cancers would also require undue experimentation. The specification focuses on glioblastomas and the prior art gives indications that a fairly wide range of cancer would be enabled due to implication of MMPs in cancer provided by Hadler-Olsen and Scherer above. However, as Scherer points out, MMP is not associated with benign cancers/tumors generally speaking:
“MMP expression is generally present in higher amounts in and around malignant cancers compared to normal, benign, or premalignant tissues. For example, in melanomas the expression of MMP9 is associated with the conversion from radial growth phase to vertical growth phase and subsequent metastasis [7]. MMP2 is highly expressed in breast cancers, but the ratio of activated to total MMP2 levels increases as the disease progresses to metastasis, increasing with tumor grade [8, 9]. MMPs are often associated with the removal of the ECM barrier to allow cancer cells to invade and metastasize.” (Scherer, page 680, col. 2, para. 2).
Finally, the phrase “preventing a cancer” is not supported by the specification. The data provided only shows the ability to treat, reduce, or ameliorate relevant cancer targets. No data is provided for actual prevention in a population that does not yet have a relevant cancer target.
The scope of these three elements create a situation wherein it would require undue experimentation to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with claim 17. Consequently, claim 17 is rejected.
Regarding claim 18, claim 17 is rejected as described above. Claim 18 does not resolve the peptide scope or “preventing a cancer” scope issues. Further reciting the case wherein the cancer is a central nervous system cancer does not rule out cancers for which MMP treatment is likely not efficacious, such as benign cancers. Consequently, claim 18 is rejected.
Regarding claim 19, claim 18 is rejected as described above. Claim 19 does not resolve the peptide scope or “preventing a cancer” scope issues. Further reciting the case wherein the cancer is a brain cancer, a glioblastoma, or a medulloblastoma does not completely rule out cancers for which MMP treatment is likely not efficacious, such as benign cancers. Consequently, claim 19 is rejected.
Regarding claim 21, claim 19 is rejected as described above. Claim 21 does not resolve the peptide scope or “preventing a cancer” scope issues. Further reciting the case wherein the cancer is a glioblastoma multiforme, however, does resolve the scope of cancer target issue. Claim 21 is rejected because of remaining scope of enablement issues.
Regarding claim 22, claim 22 recites a method of inhibiting urokinase plasminogen activator and/or a matrix metalloproteinase comprising contacting the urokinase plasminogen activator and/or matrix metalloprotease with a compound of formula (I) according to claim 1 or a pharmaceutically acceptable salt thereof.
SEQ ID NOs: 1-9, 12, and 23-24, and 26-30 are enabled for MMP-2 and MM-9 binding, but only SEQ ID NO: 1 is shown to bind to urokinase plasminogen activator. It would require undue experimentation for a person of ordinary skill in the art to determine the efficacy of all peptides recited by formula (I) for inhibiting all possible MMPs as well as uPa. Consequently, claim 22 is rejected.
Regarding claim 23, claim 22 is rejected as described above. Claim 23 recites the case wherein the MMP is MM-2 or MM-9, which partially resolves the enablement issue claim 22. However, it would require undue experimentation for a person of ordinary skill in the art to determine the efficacy of all peptides recited by formula (I) for inhibiting MMN-2 and MM-9 as well as uPa. Consequently, claim 23 is rejected.
Regarding claim 24, claim 24 recites a method of inhibiting tumor cell invasion in a brain tumor comprising administering to the brain tumor with a compound of formula (I) according to any one of claims 1 to 16 or a pharmaceutically acceptable salt thereof.
This inhibition is tied to the peptide of formula (I) interacting with MM-2 or MM-9 as described in the specification. Therefore, the analysis is similar to claim 22: SEQ ID NOs: 1-9, 12, and 23-24, and 26-30 are enabled for MMP-2 and MM-9 binding, but only SEQ ID NO: 1 is shown to bind to urokinase plasminogen activator. It would require undue experimentation for a person of ordinary skill in the art to determine the efficacy of all peptides recited by formula (I) for inhibiting all possible MMPs as well as uPa and thereby inhibiting tumor cell invasion in a brain tumor. Consequently, claim 24 is rejected.
Regarding claim 27, claim 27 recites a compound of formula (I) according to claim 1 or a pharmaceutically acceptable salt thereof for use in treating cancer. This claim has a scope identical to claim 17 with regards to claimed activity of any possible cancer and permutations of Formula (I). Consequently, claim 27 is rejected.
Regarding claim 28, claim 27 is rejected as described above. Claim 28 further recites the case wherein the cancer is a central nervous system cancer. This claim reduces the scope of the claimed cancer, but still includes cancers unlikely to respond to MM-2 or MM-9. Also, the compound scope is unaltered. Consequently, claim 28 is rejected.
Regarding claim 30, claim 30 recites a compound of formula (I) according to claim 1 or a pharmaceutically acceptable salt thereof for use in inhibiting tumor cell invasion in a brain tumor. Because the claimed activity precludes tumors unlikely to respond to MM-2 or MM-9, the activity scope is enabled for the sequences discussed above, but not any possible compound of Formula (I). Consequently, claim 30 is rejected.
Closest Prior Art
Claim 1 recites the following formula:
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45
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Greyscale
Fraga et al. WO2012041261, published 4/5/2012 discloses the SEQ ID NO: 7: LPCALNDGGLCK. SEQ ID NO: 7 reads on claim 1 to the following extent:
Xaa1 is a hydrophobic residue, such as Leu in SEQ ID NO: 7.
Pro
Xaa2 is selected from SSA, Asp, Glu, and Cys; in SEQ ID NO: 7, it is Cys.
Xaa3 has a small side chain, such as Ala in SEQ ID NO: 7.
Xaa4 is a hydrophobic residue, such as Leu in SEQ ID NO: 7.
Xaa5 is a polar uncharged amino acid, such as Asn in SEQ ID NO: 7.
Xaa6 is a negatively charged amino acid, such as Asp in SEQ ID NO: 7.
Xaa7 has a small side chain, such as Gly in SEQ ID NO: 7.
Xaa8 has a small side chain, such as Gly in SEQ ID NO: 7.
Xaa9 is selected from SSA, Asp, Glu, and Cys; in SEQ ID NO: 7, it is Cys.
Xaa10 is a positively charged amino acid, such as Lys in SEQ ID NO: 7.
However, SEQ ID NO: 7 has an extra leucine which does not fit the formula. Furthermore, there is no teaching, suggestion or motivation in the prior art to insert a leucine at that position to arrive at Formula (I). Consequently, claims 1-2, 7-11, 16-19, 21-24, 27, 28, and 30 are free from the prior art.
Allowable Subject Matter
Claims 1-2, 7-11, and 16 are allowable over the prior art. As discussed above, Fraga et al. is the closest available prior art and these claims are novel and nonobvious with respect to the sequence disclosed by Fraga. The linker structure SSA was not found in a prior art search, nor any teaching suggestion or motivation to use SSA in the sequences disclosed by this Application.
Duplicate Claim Warning
Applicant is advised that should claim 1 be found ultimately allowable, claim 27, 28, and 30 will be objected to under 37 CFR 1.75 as being a substantial duplicate thereof. In claims 27, 28, and 30 the stated intended use does not result in additional structural limitations.
When two claims in an application are duplicates or else are so close in content that they both cover the same thing, despite a slight difference in wording, it is proper after allowing one claim to object to the other as being a substantial duplicate of the allowed claim. See MPEP § 608.01(m).
Conclusion
Claims 1-2, 7-11, and 16 are allowable.
Claims 17-19, 21-24, 27, 28, and 30 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to David Paul Bowles whose telephone number is (571)272-0919. The examiner can normally be reached Monday-Friday 8:30-5:00.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Lianko Garyu can be reached on (571) 270-7367. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/DAVID PAUL BOWLES/ Examiner, Art Unit 1654
/LIANKO G GARYU/ Supervisory Patent Examiner, Art Unit 1654