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 .
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1-19 (claim set filed 01/25/2023) in the reply filed on 10/22/2025 is acknowledged.
Priority
The instant application filed on 01/25/2023 is a 371 of PCT/IB2021/056629 filed on 07/22/2021, which claims priority to U.S. Provisional Application Number 63/056,949 filed on 07/27/2020. U.S. PRO 63/056,949 finds support for the instantly claimed invention; therefore, the effective filing date of the instant application is 07/27/2020.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 01/19/2024 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Drawing Objections
The drawings are objected to because higher quality figures are required for figures 1 and 2. Additionally, the Examiner cannot differentiation between the different black and white dots in figures 1 and 2; therefore, a better method for differentiating between these dots, such as colors or shapes, is required. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Claim Rejections - 35 USC § 112(b), Indefiniteness
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.
Claims 1-19 are rejected under 35 U.S.C. 112(b) 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.
Claim 1 recites the abbreviation “RSV”; however, abbreviations must be spelled out upon first use.
Claim 17 recites the limitation "the load challenge". There is insufficient antecedent basis for this limitation in the claim. No load challenge was previously recited.
Claims 18 recites the abbreviation “cHA”; however, abbreviations must be spelled out upon first use.
Claim 19 recites the abbreviation “HIC”’ however, abbreviations must be spelled out upon first use.
Claims 2-16 are included in this rejection for depending on rejected independent claim 1 and failing to rectify the noted deficiency.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1, 3, and 19 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Roder (Purification of respiratory syncytial virus F and G proteins; 2000 – cited in the IDS filed on 01/19/2024).
Roder’s general disclosure relates to a three-step purification protocol for RSV glycoproteins F and G (see, e.g., Roder, abstract). Moreover, Roder discloses “RSV-infected HEp-2 cells were lysed by a Triton X-100 containing buffer. The viral proteins were captured by QAE-Sephadex A-50 material in a batch procedure. A first elution with 100 mM NaCl led to a crude F protein fraction, and a second elution with 300 mM NaCl led to a crude G protein fraction. The F protein was further purified on a Lentil-lectin Sepharose 4B column and finally polished using a Resource Isopropyl column. Lentil-lectin Sepharose 4B was also used to purify the G protein from the crude fraction, but polishing of the G protein was carried out on a Resource Q column. Homogenous RSV-F and RSV-G proteins were obtained by this protein purification protocol” (see, e.g., Roder, abstract). Additionally, Roder discloses additional purification methods, such as HIC chromatography, which can be employed following purification of the RSV F and G proteins by anion exchange chromatography (see, e.g., Roder, section 2.6.3, pg. 100).
Regarding claim 1 pertaining to purifying an RSV protein, Roder teaches “The clarified lysate was added to 10 ml QAE-Sephadex A-50 equilibrated with 25 mM MES-NaOH pH 5.7, 0.1% v/v Triton X-100, 10 mM NaCl (MT-10) buffer. The proteins were allowed to bind to the material for 30 min, followed by washing five times with MT-10 buffer using the same volume as the batch volume. The RSV fusion protein was then eluted by increasing the NaCl concentration to 100 mM. Five fractions of 10 ml each were collected. Finally, the RSV attachment protein was eluted by increasing the NaCl concentration to 300 mM and again five fractions each of 10 ml were collected” (see, e.g., Roder, Section 2.6.1, pg. 99).
Regarding claim 3 pertaining to the pH of the lower wash solution, Roder teaches an MT-10 wash solution that has a pH of 5.7 (see, e.g., Roder, Section 2.6.1, pg. 99).
Regarding claim 19 pertaining to HIC chromatography, Roder teaches HIC chromatography for purification of RSV proteins (see, e.g., Roder, Section 2.6.3, pg. 100).
Claim Rejections - 35 USC § 103, Obviousness
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 2 is rejected under 35 U.S.C. 103 as being unpatentable over Roder as applied to claims 1, 3, and 19 above, and further in view of Yu (AU 2014/100888; Date of Publication: September 11, 2014 – cited in the IDS filed on 01/19/2024; herein referred to as “Yu 2014”).
The teachings of Roder as it pertains to purification of an RSV protein are discussed above.
However, Roder does not teach: wherein the pH of the load solution is between 7.0 and 8.5 (claim 2).
Yu 2014’s general disclosure relates to protein purification techniques that can be used as virus clearance techniques, wherein these techniques can clear proteins of viruses in a highly efficient manner without compromising protein yield (see, e.g., Yu 2014, abstract). Moreover, Yu 2014 discloses “purifying RSV F from a composition comprising RSV F and impurities, comprising the steps of: (a) performing anion exchange chromatography and ultrafiltration, in either order, on the composition to give a first purified composition containing RSV F; and (b) performing a virus clearance step on the first purified composition” (see, e.g., Yu, pg. 2, lines 13-16). Moreover, Yu 2014 teaches that decreasing the pH of the eluate to a pH of 3.0-4.5 can be used to inactivate any virus particles in the eluate to give a composition comprising RSV F (see, e.g., Yu 2014, pg. 2, lines 19-21). Additionally, Yu 2014 discloses that “high pH binding conditions used in anion exchange chromatography can avoid precipitation of particular proteins, e.g. RSV F, at the low pH conditions then used in cation exchange chromatography.” (see, e.g., Yu 2014, pg. 8, lines 3-24).
Regarding claim 2 pertaining to the pH of the load solution, Yu 2014 teaches that the anion exchange chromatography may be performed at a pH between 6.0 and 10.0, and that the pH is usually higher than the pI of the protein of interest (see, e.g., Yu 2014, “Anion exchange chromatography”, pg. 7, lines 19-22). Therefore, one of ordinary skill in the art, based on the pI of the RSV protein, would use a load solution that is basic, wherein the pH is between 6.0 and 10.0.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to purify an RSV protein using anion exchange chromatography methods, as taught by Roder, wherein the pH of the load solution is between 7.0 and 8.5, as taught by Yu 2014. One would have been motivated to do so because Yu 2014 teaches “Anion exchange chromatography may be performed before cation exchange chromatography (described above). Performing these steps in this order provides the advantage that the high pH binding conditions used in anion exchange chromatography can avoid precipitation of particular proteins, e.g. RSV F, at the low pH conditions then used in cation exchange chromatography. This is due to the fact that many host cell proteins have a pI at lower pH range. When pH is close to the pI of the protein, each protein molecule has a low charge or no charge. Therefore protein molecules within a composition do not repel each other, and instead attract each other due to hydrophobic interaction to form complex or aggregation, which may then cause precipitation. The high pH binding conditions used in anion exchange chromatography prevent such precipitation from occurring. Precipitation occurs by complex interactions between host cell proteins and RSVF at lower pH. Therefore, once host cell proteins have been removed using anion exchange chromatography, the composition can be moved to a lower pH without risk of precipitation” (see, e.g., Yu 2014, pg. 8, lines 3-24). Moreover, Roder teaches anion exchange chromatography methods for purifying RSV proteins; however, Roder teaches a load solution at an acidic pH of 5.7 (see, e.g., Roder, section 2.6.1, pg. 99). Therefore, based on the teaching of Roder and Yu 2014, it would have been obvious to purify an RSV protein using anion exchange chromatography, wherein the load solution is at a basic pH. One would have expected success because Roder and Yu 2014 both teach purification of RSV proteins using anion exchange chromatography.
Regarding claim 2’s pH limitations, those working in the biological and/or pharmaceutical arts would understand that the adjustments of particular conventional working conditions (e.g., pH of a solution or buffer) is deemed a matter of judicious selection and routine optimization, which is within the purview of the skilled artisan. For example, the disclosure of Yu 2014 teaches, as it pertains to anion exchange chromatography, “When pH is close to the pI of the protein, each protein molecule has a low charge or no charge. Therefore protein molecules within a composition do not repel each other, and instead attract each other due to hydrophobic interaction to form complex or aggregation, which may then cause precipitation. The high pH binding conditions used in anion exchange chromatography prevent such precipitation from occurring. Precipitation occurs by complex interactions between host cell proteins and RSVF at lower pH” (see, e.g., Yu 2014, pg. 8, lines 3-24). Moreover, Roder teaches anion exchange chromatography methods for purifying RSV proteins; however, Roder teaches a load solution at an acidic pH of 5.7 (see, e.g., Roder, section 2.6.1, pg. 99). Therefore one of ordinary skill in the art would readily understand that manipulating the pH of the buffer would influence the formation of complex or aggregates when purifying proteins. This is motivation for someone of ordinary skill in the art to practice or test the parameter widely in order to find those that are functional or optimal which then would be inclusive or cover the steps as instantly claimed. Absent any teaching of criticality by the Applicant concerning the pH, it would be prima facie obvious that one of ordinary skill in the art would recognize these limitations are result effective variables which can be met as a matter of routine optimization
Claims 4-13, and 17-18 are rejected under 35 U.S.C. 103 as being unpatentable over Roder as applied to claims 1, 3, and 19 above, and further in view of Yu (WO 2015/038888 –cited in the IDS filed on 01/19/2024; herein referred to as “Yu 2015”).
The teachings of Roder as it pertains to purification of an RSV protein are discussed above.
However, Roder does not teach: wherein the lower pH wash solution comprises acetate (claim 4); or wherein the concentration of acetate in the lower pH wash solution is between 56 and 84 mM (claim 5); or wherein prior to eluting the RSV protein, the anion exchange chromatography medium is washed with at least a first higher pH wash solution at a pH between 7.0 and 8.0 (claim 6); or wherein the first higher pH wash solution comprises Tris at a concentration between 18 and 22 mM (claim 7); or wherein the first higher pH was solution comprises NaCl at a concentration between 45 and 55 mM (claim 8); or wherein the wash step using the first higher pH wash solution is performed prior to the wash step using said lower pH wash solution (claim 9); or wherein prior to elution of the RSV protein, the anion exchange chromatography medium is further washed with at least a second higher pH wash solution at a pH between 7.0 and 8.0 (claim 10); or wherein said second higher pH wash solution comprises Tris at a concentration between 45 and 55 mM (claim 11); or wherein said second higher pH wash solution comprises NaCl at a concentration between 18 and 22 mM (claim 12); or wherein the wash step using said second higher pH wash solution is performed after the wash step using said lower pH wash solution (claim 13); or wherein the load challenge is between 7.5 and 15.0 mg per ml of the anion exchange chromatography medium (claim 17); or wherein the purification further comprises a cHA chromatography step (claim 18).
Yu 2015’s general disclosure relates to “the development of improved processes for the purification of recombinant polypeptides produced in Chinese hamster ovary (CHO) cells that provide purified product with substantially reduced levels of hamster PLBL2. Recombinant polypeptides purified according to the methods of the invention, including therapeutic antibodies such as an anti-IL13 antibody, may have reduced immunogenicity when administered to human subjects.” (see, e.g., Yu 2015, [0021]). Moreover, Yu 2015 discloses anion exchange chromatography methods for purifying anti-IL13 antibodies from CHO cells (see, e.g., Yu 2015, [0009], [00245]).
Regarding claims 4-5 pertaining to the lower pH wash solution comprising acetate, Yu 2015 teaches “In certain embodiments, the HIC step comprises an equilibration buffer and a wash buffer, wherein each of the equilibration buffer and the wash buffer comprise 50 mM sodium acetate pH 5.0” (see, e.g., Yu 2015, [0023]). The 50 mM acetate concentration is approaching the claimed acetate concentration (see, e.g., MPEP 2144.05(I)).
Regarding claim 6 pertaining to a first higher pH wash solution, Yu 2015 teaches an intermediate wash buffer that is used prior to elution of the bound protein, wherein “the pH of the intermediate wash buffer is typically from about 4 to about 8, or from about 4.5 to about 5.5, or about 5.0. In one embodiment, the pH is 7.00 + 0.10” (see, e.g., Yu 2015, [00145]).
Regarding claims 7-8 and 11-12 pertaining to the Tris and NaCl concentrations in the first and second higher pH wash solutions, Yu 2015 teaches that after loading the protein, the column was washed with a buffer containing 25 mM sodium chloride and 25 mM Tris (see, e.g., Yu 2015, [00274]-[00275]) (see, e.g., MPEP 2144.05(I)).
Regarding claim 9 pertaining to the order of the wash steps, Yu 2015 teaches that the chromatography column is first washed and equilibrated with a buffer that has a pH of 7.7 (see, e.g., Yu 2015, [00139]), followed by an intermediary wash step that has a pH from about 4 to about 8 (see, e.g., Yu 2015, [00145]), followed by washing and eluting the protein in a buffer with a pH from about 2 to about 5 (see, e.g., Yu 2015, [00146]).
Regarding claims 10-13 pertaining to a second higher pH wash solution, Yu 2015 teaches an intermediate wash buffer that is used prior to elution of the bound protein, wherein “the pH of the intermediate wash buffer is typically from about 4 to about 8, or from about 4.5 to about 5.5, or about 5.0. In one embodiment, the pH is 7.00 + 0.10” (see, e.g., Yu 2015, [00145]). The Examiner has interpreted the second higher pH wash solution to merely be repetition of the first higher pH wash solution, except that the NaCl and Tris concentrations have been manipulated and optimized. The simple repetition of a known step to achieve an art recognized outcome is “merely the logical result of common sense application to the maxim ‘try, try again’” (see, e.g., Perfect Web Technologies, Inc v. InfoUSA, Inc. 587 F.3d 1324 (Fed Cir. Dec. 2, 2009)). In the instant case, the ordinary artisan would understand that repeating the washing steps, while manipulating and optimizing the NaCl and Tris concentrations, would result in elution of different impurities from the anion exchange chromatography column.
Regarding claim 14-16 pertaining to elution of the protein having a pH between 7 and 8, Yu 2015 teaches elution of a protein from an anion-exchange chromatography column with 85 mM sodium chloride, 50 mM Tris at a pH of 8.0 (see, e.g., Yu 2015, [00275]) (see, e.g., MPEP 2144.05(I)).
Regarding claim 17 pertaining to the load challenge, Yu 2015 teaches diluting the protein pool to 1.7 mg/mL and loading it onto the chromatography resin (see, e.g., Yu 2015, [00256]) (see, e.g., MPEP 2144.05(I)).
Regarding claim 18 pertaining to the cHA chromatography step, Yu 2015 teaches “he eluted protein preparation may be subjected to additional purification steps either prior to, or after, the Protein A chromatography step”, which can include hydroxyapatite chromatography (cHA) (see, e.g., Yu 2015, [00147], [00259).
It would have been first obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to purify an RSV protein using anion exchange chromatography methods, as taught by Roder, wherein the lower pH wash buffer contains acetate, as taught by Yu 2015. One would have been motivated to do so because Yu 2015 teaches that the equilibration buffer and wash buffer contains acetate in order to maintain an acidic pH (see, e.g., Yu 2015, [00106], [00146], [00154]). Moreover, Roder teaches purification of RSV proteins using anion exchange chromatography, wherein the equilibration and wash buffers are at an acidic pH of 5.7 (see, e.g., Roder, Section 2.6.1, pg. 99). Therefore, based on the teachings of Roder and Yu 2015, it would have been obvious to perform anion exchange chromatography to purify a protein, wherein the wash buffer(s) contain acetate in order to maintain an acidic pH.
It would have been secondly obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to purify an RSV protein using anion exchange chromatography methods, as taught by Roder, wherein Yu 2015 teaches performing a first and second higher pH washing steps. One would have been motivated to do so because Yu 2015 teaches that these intermediary washing steps, wherein the pH of the buffer(s) are manipulated, “is used to elute one or more impurities from the ion exchange resin, prior to eluting the polypeptide molecule of interest. The conductivity and/or pH of the intermediate buffer is/are such that one or more impurity is eluted from the ion exchange resin, but not significant amounts of the polypeptide of interest” (see, e.g., Yu 2015, [00109]). Moreover, Roder teaches the clarified lysate was added to 10 ml QAE-Sephadex A-50 equilibrated with 25 mM MES-NaOH pH 5.7, 0.1% v/v Triton X-100, 10 mM NaCl (MT-10) buffer. The proteins were allowed to bind to the material for 30 min, followed by washing five times with MT-10 buffer using the same volume as the batch volume. The RSV fusion protein was then eluted by increasing the NaCl concentration to 100 mM. Finally, the RSV attachment protein was eluted by increasing the NaCl concentration to 300 mM and again five fractions each of 10 ml were collected” (see, e.g., Roder, Section 2.6.1, pg. 99). Therefore, Roder teaches manipulation of the NaCl concentrations in order to influence elution of different bound proteins on the anion exchange chromatography column(s). Therefore, based on the teachings of Roder and Yu 2015, it would have been obvious to perform different washing steps, wherein the concentration of NaCl and/or Tris, as well as the pH of the buffer(s), are manipulated in order to elute any impurities from the columns before elution of the protein of interest.
It would have been thirdly obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to purify an RSV protein using anion exchange chromatography methods, as taught by Roder, wherein Yu 2015 teaches subsequently performing cHA chromatography of the eluted protein after anion exchange chromatography. One would have been motivated to do so because Yu 2015 teaches that hydroxyapatite chromatography (i.e., cHA chromatography) can be performed on the eluted protein for additional purification (see, e.g., Yu 2015, [00147], [00259). Moreover, Yu 2015 teaches that additional purification steps can be used in order to formulate the recovered protein in a pharmaceutically acceptable carrier for diagnostic or therapeutic uses (see, e.g., Yu 2015, [00148]). Moreover, Roder teaches additional purification methods following anion exchange chromatography, such as hydrophobic interaction chromatography (see, e.g., Roder, section 2.6.3, pg. 100). Therefore, based on the teachings of Roder and Yu 2015, it would have been obvious to one of ordinary skill in the art to perform additional purification steps following anion exchange chromatography in order to ensure the protein of interest obtained is indeed purified. One would have expected success because Roder and Yu 2015 both teach purification of proteins using anion exchange chromatography.
Regarding claims 6, 10, and 14’s pH limitations, those working in the biological and/or pharmaceutical arts would understand that the adjustments of particular conventional working conditions (e.g., pH of a solution or buffer) is deemed a matter of judicious selection and routine optimization, which is within the purview of the skilled artisan. For example, the disclosure of Yu 2015 teaches that these intermediary washing steps, wherein the pH of the buffer(s) are manipulated, “is used to elute one or more impurities from the ion exchange resin, prior to eluting the polypeptide molecule of interest. The conductivity and/or pH of the intermediate buffer is/are such that one or more impurity is eluted from the ion exchange resin, but not significant amounts of the polypeptide of interest” (see, e.g., Yu 2015, [00109]). Moreover, Roder teaches anion exchange chromatography methods for purifying RSV proteins; however, Roder teaches a load solution at an acidic pH of 5.7 (see, e.g., Roder, section 2.6.1, pg. 99). Therefore one of ordinary skill in the art would readily understand that manipulating the pH of the buffer would influence the formation of complex or aggregates when purifying proteins. This is motivation for someone of ordinary skill in the art to practice or test the parameter widely in order to find those that are functional or optimal which then would be inclusive or cover the steps as instantly claimed. Absent any teaching of criticality by the Applicant concerning the pH, it would be prima facie obvious that one of ordinary skill in the art would recognize these limitations are result effective variables which can be met as a matter of routine optimization.
Regarding claims 5, 7-8, 11-12, and 15-17’s concentration limitations, those working in the biological and/or pharmaceutical arts would understand that the adjustments of particular conventional working conditions (e.g., concentration of NaCl or Tris within a buffer, and load challenge of a protein) is deemed a matter of judicious selection and routine optimization, which is within the purview of the skilled artisan. For example, Yu 2015 teaches that after loading the protein, the column was washed with a buffer containing 25 mM sodium chloride and 25 mM Tris (see, e.g., Yu 2015, [00274]-[00275]) (see, e.g., MPEP 2144.05(I)). Additionally, Yu 2015 teaches elution of a protein from an anion-exchange chromatography column with 85 mM sodium chloride, 50 mM Tris at a pH of 8.0 (see, e.g., Yu 2015, [00275]) (see, e.g., MPEP 2144.05(I)). Moreover, Roder teaches that RSV F proteins elute at a lower NaCl concentration, compared to RSV G proteins (see, e.g., Roder, abstract). Therefore, one of ordinary skill in the art would reasonably understand that manipulating the amount of NaCl and Tris within the buffer effects the washing and elution of the protein of interest during anion exchange chromatography. This is motivation for someone of ordinary skill in the art to practice or test the parameter widely to find those that are function or optimal which then would be inclusive or cover the steps as instantly claimed. Absent any teaching of criticality by the Applicant concerning the concentration, it would be prima facie obvious that one of ordinary skill in the art would recognize these limitations are result effective variables which can be met as a matter of routine optimization.
Conclusion
Claims 1-19 are rejected.
No claims are allowed.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE IANNUZO whose telephone number is (703)756-5559. The examiner can normally be reached Mon - Fri: 8:30-6:00 EST.
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/NATALIE IANNUZO/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653