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 invention Group I, claims 68-84, and Applicant’s election with traverse of the product species ‘medical material’, in the reply filed on 10/01/2025 is acknowledged. Claims 85-91 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions, there being no allowable generic or linking claim.
In Applicant’s reply, Applicant states that “the method of the present invention generates soluble collagen, which imparts equivalent properties to all species: textile, food product, cosmetic product, and medical material.”, that “]t]his constitutes a common technical feature”, and that “the species can be analyzed together without imposing an extra burden on the Examiner in view of the common technical feature” (remarks, page 7).
The Examiner responds that, as discussed in the previous Office action, the
claims in the instant Application are directed to more than one species of the generic
invention. These species are deemed to lack unity of invention because they are not so
linked as to form a single general inventive concept under PCT Rule 13.1. Regarding the instant product species textile, food product, cosmetic product, or medical material, the product species are different products with different structures and properties, and therefore are affected differently by the incorporation of a collagen composition.
In conclusion, Applicant’s arguments are not persuasive. The requirement
is still deemed proper and is therefore made FINAL.
Claim Status
The amendment of 10/01/2025 has been entered. Claims 68-91 are pending (claim set as filed on 10/01/2025). Claims 85-91 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election of invention Group I was made without traverse in the reply filed on 10/01/2025.
Claims 68-84 are currently under examination and were examined on their merits.
Priority
This application filed on 02/14/2023 claims priority to PCT application no. PCT/IL2021/051026, filed on 08/22/2021, and claims priority to provisional application no. PRO 63/122,957, filed on 12/09/2020, and to provisional application no. PRO 63/069,049, filed on 08/23/2020.
Information Disclosure Statement
The Information Disclosure Statements (IDS) filed on 10/11/2024 and 05/15/2023 have been received and considered.
Drawings
The drawings are objected to because Fig. 7B misses the legend for the circle symbol. 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.
Specification
The disclosure is objected to because of the following informalities:
The term “cooper” recited on page 10, lines 3, 6, and 7, on page 26, lines 29 and 31, and on page 27, line 1, should read “copper”.
Appropriate correction is required.
Claim Objections
Claim 80 is objected to because of the following informalities:
“a cooper-free medium” (claim 80, line 4) should read “a copper-free medium”.
Appropriate correction is required.
Claim Rejections - 35 USC § 112 (b)
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.
Claims 68-84 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.
Claim 68 recites ‘the cleavage of at least one propeptide’ which is indefinite for lacking antecedent basis because ‘cleavage’ is not recited within the claim.
Claim 76 recites ‘the feedback inhibition’ which is indefinite for lacking antecedent basis because ‘feedback inhibition’ is not recited within the claim or in claim 68 from which claim 76 depends.
One of ordinary skill in the art would not be able to determine the metes and bounds of the claims, and thus, could not clearly determine how to avoid infringement of claims 68 and 76.
In the interest of compact prosecution, claims 68 and 76 are interpreted to the broadest embodiment claimed.
Claim Rejections - 35 USC § 103
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.
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 factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
Determining the scope and contents of the prior art.
Ascertaining the differences between the prior art and the claims at issue.
Resolving the level of ordinary skill in the pertinent art.
Considering objective evidence present in the application indicating obviousness or nonobviousness.
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 68-84 are rejected under 35 U.S.C. 103 as being unpatentable over Mays (WO 95/31473, published on 11/23/1995), hereinafter ‘Mays’, in view of Wang et al. (“TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2”, published in 2006, Biochem. J. (2006) 398, pages 515–519), hereinafter ‘Wang’, as evidenced by Tracy et al. (“Extracellular Matrix and Dermal Fibroblast Function in the Healing Wound”; published on 03/01/2016, Adv Wound Care (New Rochelle), Vol. 5(3), pages 119-136), hereinafter ‘Tracy’, and by Miyahara et al. (“Formation of Collagen Fibrils in Vitro by Cleavage of Procollagen with Procollagen Proteinases”, published on 07/25/1982, J Biol Chem, Vol. 257(14), pages 8442-8448), hereinafter ‘Miyahara’.
Mays’ general disclosure relates to “a method for producing collagens from a collagen-producing cell in a cell culturing system” (see entire document, including abstract).
Regarding claim 68, pertaining to a method of producing cell-free animal collagen, May teaches a method of producing cell-free animal collagen (“This invention is directed to a method for producing collagens from a collagen-producing cell in a cell culturing system. This invention is also directed to the collagens synthesized in vitro from the cell cultures”, “The invention will be further described with reference to a
specific embodiment using human fibroblast cells”; see abstract, page 24 lines 1-2), comprising the steps of:
growing a plurality of collagen producing animal cells in a cell culture comprising
culture medium under conditions inducing collagen synthesis (“The collagen-producing cells are grown or incubated under conditions to promote the growth of the cells in either media supplemented with serum or in chemically defined media”, “To promote collagen synthesis the medium needs to be supplemented with sodium ascorbate or one of its more chemically stable derivatives”, “The invention will be further described with reference to a specific embodiment using human fibroblast cells; page 20, paragraph 2; page 24, paragraph 1), wherein soluble collagen comprising procollagen is secreted from the plurality of collagen producing animal cells to the culture medium (“Once the culture has ceased logarithmic growth, the medium is supplemented with an ascorbate to promote hydroxylation and secretion of procollagens”, “procollagens may be harvested from the spent cell culture medium”; page 21, lines 11-13; page 23, lines 13-14);
collecting the soluble collagen enriched medium (“procollagens may be harvested from the spent cell culture medium”; page 23, lines 13-14; page 24, paragraph 1) while maintaining the cell culture (“the cell layer is washed with a cold dilute neutral salt solution in order to dissolve and remove the synthesized non-crosslinked collagen … A requirement of this invention is that viable cells remain in the cell culturing system to resume synthesis of non-crosslinked collagen.”; page 21, paragraph 2).
Regarding claim 69, pertaining to inducing collagen synthesis, Mays teaches wherein the conditions inducing collagen synthesis comprise growing the cells in a culture medium comprising insulin and a salt of ascorbic acid that induce collagen synthesis (“To promote collagen synthesis the medium needs to be supplemented with sodium ascorbate or one of its more chemically stable derivatives e.g. L-ascorbic acid phosphate magnesium salt n-hydrate.”, “production medium, which contained Dulbecco’s modified Eagle’s medium …supplemented with …bovine insulin [5μg/ml], … L-ascorbic acid phosphate magnesium salt n-hydrate”; page 20, lines 24-27; page 25, lines 23-32). It is noted that claim 69 and the instant specification describe insulin and ascorbic acid or salt thereof as agents that induce collagen synthesis (see instant specification, page 29, lines 17-19).
Regarding claim 73, pertaining to the collagen enriched medium, Mays teaches wherein collecting the soluble collagen enriched medium is performed by intermittently removing the soluble collagen enriched medium (“After an appropriate period of time in which the cells are secreting collagen, typically from about two days to about seven days, the conditions are changed to solubilize the collagen. In one embodiment, the medium is removed from the culture.”, “(b) removing said cell culture medium containing
procollagen from said cell culture … (f) removing said cell culture medium containing procollagen from said cell culture”, “”, “procollagens may be harvested from the spent cell culture medium; page 15, lines 25-35; page 21, lines 14-17; page 23, lines 13-14, claim 33, steps (b)-(g)).
Regarding claims 74 and 75, pertaining to furnishing the cell culture with a collagen-free culture medium, Mays teaches furnishing the cell culture with a collagen-free culture medium comprising insulin and a salt of ascorbic acid which induce collagen synthesis by the cells (“The same collagen-producing cells, are then recultured using fresh medium, thus providing for a repeated culturing and collagen production cycling system.”, “The Dulbecco's phosphate buffered saline, containing collagens solubilized from the cell layer, was removed and fresh production medium at 37°C was added to the vessel”, “production medium, which contained Dulbecco’s modified Eagle’s medium …supplemented with …bovine insulin [5μg/ml], … L-ascorbic acid phosphate magnesium salt n-hydrate”; page 15, lines 28-30; page 25, lines 23-32; it is noted that claim 69 and the instant specification describe insulin and ascorbic acid or salt thereof as agents that induce collagen synthesis (see instant specification, page 29, lines 17-19)) (instant claim 74), wherein the culture medium further comprises beta-aminopropionitrile which inhibits cross-linking of soluble collagen secreted to the medium (“production medium, which contained Dulbecco’s modified Eagle’s medium …supplemented with …bovine insulin [5μg/ml], …beta-aminopropionitrile [50μg/ml] …, … L-ascorbic acid phosphate magnesium salt n-hydrate”, “The preferred lysyl oxidase inhibitor is β-aminopropionitrile”; page 15, lines 28-30; page 20, line 34; page 25, lines 23-32; it is noted that the instant specification describes wherein the inhibition of crosslinking of the soluble collagen comprises supplementing the medium with lysyl oxidase inhibitor (page 10, lines 1-4)) (instant claim 75).
Regarding claim 76, pertaining to a genetically modified cell, Mays teaches wherein the cells are genetically modified (“Further, the cells may be recombinant or genetically-engineered cells”; page 18, lines 5-7; claim 42), to:
enhance collagen synthesis (“the cells may be recombinant or genetically-engineered cells that express collagens which are either 'normal' but expressed at high levels”; page 18, lines 5-7), and/or inhibit collagen cross-linking (“Examples of genetic engineering approaches including, …, “knocking-out” the lysyl oxidase gene locus”, “lysyl oxidase-mediated crosslinks in collagens”; page 6, lines 32-34; page 19, lines 21-30; claim 47); and/or
reduce the expression of at least one Lysyl oxidase (LOX) (“wherein said
collagen-producing cell is genetically engineered such that said cell’s ability to
produce lysyl oxidase is prevented or reduced”; claim 47; page 19, lines 21-30).
Regarding claim 77, pertaining to the method, Mays teaches wherein the method further comprises one or more of the following steps:
genetically modifying the cells to increase collagen production (“the cells may
be recombinant or genetically-engineered cells that express collagens which are either 'normal' but expressed at high levels”; page 18, lines 5-7); and/or
genetically modifying the cells to reduce collagen crosslinking (claim 47; page 6, lines 32-34; page 19, lines 21-30).
Regarding claim 78, pertaining to the cells, Mays teaches wherein the cells are non-genetically modified cells (“Human fibroblast cell strains”; page 17, lines 19-32).
Regarding claim 79 and 80, pertaining to inhibiting crosslinking, Mays teaches wherein the method further comprises a step of inhibiting crosslinking of soluble collagen within the soluble collagen-enriched culture medium (“continued incubation of said cells in a culture medium containing an agent to inhibit or interfere with collagen crosslinking”; claims 1 and 33), wherein inhibiting crosslinking of the soluble collagen further comprises one or more of the following steps:
depleting copper ions from the medium by supplementing the medium with penicillamine (“continued incubation of said cells in a culture medium containing an agent to inhibit or interfere with collagen crosslinking”, “wherein said agent to inhibit or to interfere with collagen crosslinking is D-penicillamine”, “Other agents are known to interfere with the formation and/or
maturation of lysine-derived lysyl oxidase-mediated crosslinks in
collagens, including D-penicillamine”; see claims 1, 13, and 33; page 6, lines 32-34; it is noted that the instant specification describes penicillamine as a copper chelating agent (see specification, page 10, lines 5-7));
supplementing the medium with the lysyl oxidase inhibitor β-aminopropionitrile (“production medium…supplemented with …beta-aminopropionitrile [50μg/ml]”, “The preferred lysyl oxidase inhibitor is β-aminopropionitrile”; page 15, lines 21-25; page 20, line 34, page 25, lines 25-32; claims 1 and 12).
Regarding claim 81, the instant specification describes that “the term “production cycle” as used herein refers to a production of soluble collagen from the same batch of cells without a step of passing or replacing the cells. The production cycle may include several replacements of the soluble-collagen enriched medium with a new medium.” (specification, page 31, lines 21-24).
Pertaining to the production cycle, Mays teaches wherein the cell culture is maintained for a production cycle of 133 days (“The culture was maintained for 133 days after the introduction of production medium to the cell culture system”; see Example 1 on page 26, lines 11-13).
Regarding claim 82, the claim recites wherein the method results in cell-free animal soluble collagen production of at least 100, at least 200, at least 300, at least
400, at least 500 or at least 600 μg/106 cells per production cycle. It is noted that the recited yielded amounts of soluble collagen per 106 cells per production cycle naturally result from performing the instantly claimed method steps, and therefore, the recited obtained amounts of soluble collagen are inherent to the method. As such, performing the method steps a, b and c recited in claim 68 inherently results in cell-free animal soluble collagen production of at least 100, at least 200, at least 300, at least
400, at least 500 or at least 600 μg/106 cells per production cycle.
Regarding claim 83, pertaining to soluble collagen production, Mays teaches wherein the soluble-collagen enriched medium further comprises an additional ECM component (“Similarly, this approach will allow for elastin to be produced in vitro and harvested from cultured cells for use in biomedical applications, …. Therefore, elastin may be isolated and purified from the cell culture system of this invention”; page 19, paragraph 3). It is noted that elastin is an ECM component, as evidenced by Tracy (“ECM proteins such as collagen, hyaluronan (HA), or elastin”; see entire document , including abstract).
Regarding claim 84, pertaining to soluble collagen assembly, Mays teaches wherein the method further comprises subjecting the soluble collagen obtained from the collected soluble-collagen enriched medium to (1) conditions enabling the soluble collagen assembly to collagen fibrils (“The thus collected procollagen may then be treated with the specific C- and N-proteinases to cleave the propeptides leaving intact fully processed, telopeptide containing collagen.”, “The extracted collagen can be treated with enzymes, such as lysyl oxidase, to allow it to crosslink. Further, the non-crosslinked collagen may be crosslinked by chemical means such as carbodiimides, glutaraldehyde, sugars and UV irradiation”; page 16, lines 7-11; page 23, lines 22-25). It is noted that cleavage of the propeptides leads to formation of fibrils, as evidenced by Miyahara et al. (“A partially purified enzyme preparation containing both procollagen N-proteinase and C-proteinase (EC 3.4.24.00) activities was used to initiate fibril formation by removal of the N and C-propeptides from type I procollagen in a physiological buffer at 35-37 °C.”; see entire document, including abstract)
Additionally, Mays teaches wherein “the cleaved propeptides are believed to negatively-feedback to inhibit procollagen gene expression.” (page 3, lines 19-21). Mays further discloses wherein cells for collagen synthesis “need not be limited to fibroblasts, but may include, although not limited to, human smooth muscle cells, human endothelial cells, and human epithelial cells of pulmonary and dermal origin” (page 17, lines 25-28).
Mays does not teach
wherein the method comprises the step of inhibiting or reducing the cleavage of at least one propeptide from the procollagen N- terminus, the procollagen C- terminus or from a combination thereof, thereby obtaining a soluble collagen-enriched medium (instant claim 68 (b)).
wherein inhibiting or reducing the cleavage of the at least one propeptide from the procollagen N- or C- terminus comprises supplementing the medium with at least one agent selected from: a small molecule, an antibody, a protein, a peptide and an siRNA (instant claim 70).
wherein the small molecule, antibody, protein, peptide or siRNA inhibits or reduces the activity of at least one procollagen peptidase (instant claim 71).
wherein the small molecule, antibody, protein, peptide or siRNA is a matrix metalloprotease (MMP) inhibitor (instant claim 72).
wherein the method further comprises furnishing the cell culture with a collagen-free culture medium comprising at least one agent inhibiting the cleavage of at least one propeptide from procollagen N- or C- terminus (instant claim 74).
wherein at least one of the cells are genetically modified to inhibit or reduce the cleavage of at least one propeptide from the procollagen N- or C- terminus (instant claim 76 (2)).
wherein the method further comprises the step of genetically modifying the cells to reduce the cleavage of a propeptide from the procollagen N- or C- terminus (instant claim 77 (3)).
Wang’s general disclosure relates to “the abilities of the TIMPs to affect biosynthetic processing of procollagens” (see entire document, including abstract).
Regarding claims 68, 70-72, 74, and 76(2), and 77(3), pertaining to inhibiting cleavage of at least one propeptide from the procollagen N-Terminus, Wang teaches that “[t]he major fibrillar collagens, which constitute the major fibrous components of vertebrate ECM (extracellular matrix), are synthesized as procollagens, with N- and C-propeptides that must be cleaved to produce mature monomers capable of assembling into fibrils” (page 515, left column, paragraph 1), wherein “ADAMTS-2, an extracellular ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) metalloproteinase, is capable of providing the pNP (procollagen N-proteinase)
activity that cleaves the N-propeptides of procollagens I–III in vitro” (page 515, left column, paragraph 1). Wang further teaches “TIMPs (tissue inhibitors of matrix metalloproteinases)”, that “TIMP-3 inhibits the pNP ADAMTS-2”, that “[i]t can also inhibit the processing of procollagen I by cells” (page 515, left column, paragraph 2 - page 515, right column, paragraph 1), and discloses in vitro inhibition of cleavage of the propeptide from the procollagen N-terminus in the presence of recombinant TIMP-3 (“page 516, right column, paragraph 3). Wang’s teachings indicate that TIMP-3 is a protein (“NTIMP-3, the active N-terminal domain of TIMP-3” (page 515, right column, paragraph 2)).
While Mays does not teach wherein the method comprises the step of inhibiting or reducing the cleavage of at least one propeptide from the procollagen N- terminus, the procollagen C- terminus or from a combination thereof, thereby obtaining a soluble collagen-enriched medium (instant claim 68 (b)), wherein inhibiting or reducing the cleavage of the at least one propeptide from the procollagen N- or C- terminus comprises supplementing the medium with at least one agent selected from: a small molecule, an antibody, a protein, a peptide and an siRNA (instant claim 70), wherein the small molecule, antibody, protein, peptide or siRNA inhibits or reduces the activity of at least one procollagen peptidase (instant claim 71), wherein the small molecule, antibody, protein, peptide or siRNA is a matrix metalloprotease (MMP) inhibitor (instant claim 72), and wherein the method further comprises furnishing the cell culture with a collagen-free culture medium comprising at least one agent inhibiting the cleavage of at least one propeptide from procollagen N- or C- terminus (instant claim 74), it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, to have combined Mays’ method of producing cell-free animal collagen with Wang’s teachings on TIMP3 inhibiting procollagen proteinase AdamTS-2, in order to create a method of producing cell-free animal collagen, wherein the method further comprises the step of inhibiting or reducing the cleavage of at least one propeptide from the procollagen N- terminus, thereby obtaining a soluble collagen-enriched medium, wherein inhibiting or reducing the cleavage of the at least one propeptide from the procollagen N- terminus comprises supplementing the medium with a protein, wherein the protein inhibits or reduces the activity of at least one procollagen peptidase, wherein the protein is a matrix metalloprotease (MMP) inhibitor, and wherein the method further comprises furnishing the cell culture with a collagen-free culture medium comprising an agent inhibiting the cleavage of at least one propeptide from procollagen N- terminus. One would have been motivated to do so, in order to increase the amount of produced procollagen that can be used for controlled cell-free processing into fibrils (see Mays above).
While Mays does not teach wherein the method comprises the step of inhibiting or reducing the cleavage of at least one propeptide from the procollagen N-terminus, the procollagen C- terminus or from a combination thereof, thereby obtaining a soluble collagen-enriched medium (instant claim 68 (b)), wherein at least one of the cells are genetically modified to inhibit or reduce the cleavage of at least one propeptide from the procollagen N- or C- terminus (instant claim 76 (2)), and wherein the method further comprises the step of genetically modifying the cells to reduce the cleavage of a propeptide from the procollagen N- or C- terminus (instant claim 77 (3)), it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have combined Mays’ method with Mays’ teachings on genetically engineered cells and with Wang’s teachings on inhibiting procollagen proteinase AdamTS-2, to have created a method of producing cell-free animal collagen, wherein the method further comprises the step of inhibiting or reducing the cleavage of at least one propeptide from the procollagen N- terminus, thereby obtaining a soluble collagen-enriched medium, wherein at least one of the cells are genetically modified to inhibit or reduce the cleavage of at least one propeptide from the procollagen N- terminus, and wherein the method further comprises the step of genetically modifying the cells to reduce the cleavage of a propeptide from the procollagen N- terminus. One would have been motivated to do so in order to increase the amount of produced procollagen that can be used for controlled cell-free processing into fibrils (see Mays above).
A skilled artisan would have reasonably expected success in combining Mays’ and Wang’s teachings since both references are directed to procollagen.
Regarding claim 82, the combination of Mays’ and Wang’s teachings would implicitly result in the same or similar amount of obtained cell-free animal soluble collagen per 106 cells per production cycle. Since both, Mays and Wang teach on the impact of enzymatic processing of procollagen, and Wang further teaches inhibition of procollagen cleavage in the presence of a matrix metalloprotease inhibitor, it is highly expected that the method taught by Mays in view of Wang, would result in the same or similar, i.e. obvious, amounts of cell-free soluble collagen as described in claim 82.
Conclusion
No claims are allowed.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SANDRA ZINGARELLI whose telephone number is (703)756-1799. The examiner can normally be reached M-F 9-5.
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/SANDRA ZINGARELLI/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653