DETAILED ACTION
Status of the Application
Claims 1, 6-8, 10-16, 20-21 are pending.
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s amendment of claims 1, 6, 14, cancellation of claims 3-5, 17, and addition of claims 20-21 as submitted in a communication filed on 12/4/2025 is acknowledged.
Claims 20-21 are directed to the elected invention. Claims 10-16 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 5/13/2024. Claims 1, 6-8, 20-21 are at issue and are being examined herein.
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Rejections and/or objections not reiterated from previous office actions are hereby withdrawn.
Claim Objections
Claims 1 and 6 are objected to due to the recitation of “MjTET”, “PhTET1”, “PhTET2”, “PhTET3”, “PhTET4”. Abbreviations unless otherwise obvious and/or commonly used in the art, should not be recited in the claims without at least once reciting the entire phrase for which the abbreviation is used. Appropriate correction is required.
Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA )
Claims 1, 6-8, remain rejected and new claims 20-21 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 pre-AIA the applicant regards as the invention. New grounds of rejection are necessitated by amendment.
Claims 1 and 6 (claims 7-8, 20-21 dependent thereon) is indefinite in the recitation of “…X% MjTET”, “..X% PhTET1”, “..X% PhTET2”, “..X% PhTET3”, and “..X% PhTET4” for the following reasons. As written, it is unclear as to which is the basis for the % recited. Does it refer to weight % based on the total weight of the composition? Does it refer to the weight % based on the total weight of all the TET aminopeptidases in the composition? Does it refer to the weight % based on the total weight of the two TET aminopeptidases listed in sections (a)-(g) of claim 1? Does it refer to the weight % based on the weight of the three TET aminopeptidases listed in sections (a)-(d) of claim 6? Does it refer to volume % based on the total volume of the composition? If the intended basis for the % recited is the total weight of the composition, the claims should be amended accordingly. For examination purposes, no patentable weight will be given to the terms “…X% MjTET”, “..X% PhTET1”, “..X% PhTET2”, “..X% PhTET3”, and “..X% PhTET4” . Correction is required.
Claim 7 is indefinite in the recitation of “wherein said first, second and third aminopeptidases are in equimolar proportions” for the following reasons. The combinations of first, second and third aminopeptidases have been defined in claim 6 as having an exact % of each of the three aminopeptidases. As indicated above, it is unclear which is the basis for the % recited. If it is assumed that the % recited in claim 6 is based on the total weight of the composition, the composition of claim 7 is of different scope because the molecular weight of each of the aminopeptidases is different, thus 33.3% by weight for each of the three aminopeptidases is not the same as a composition that comprises equimolar amounts of each of the three aminopeptidases. Claim 7 does not further limit claim 6 and it is broader in scope. Correction is required.
Claim 21 is indefinite in the recitation of “wherein said first and second aminopeptidases are in equimolar proportions” for the following reasons. The combinations of first and second aminopeptidases have been defined in claim 1 as having an exact % of each of the two aminopeptidases. As indicated above, it is unclear which is the basis for the % recited. If it is assumed that the % recited in claim 1 is based on the total weight of the composition, the composition of claim 21 is of different scope because the molecular weight of each of the aminopeptidases is different, thus 50% by weight for each of the two aminopeptidases is not the same as a composition that comprises equimolar amounts of each of the two aminopeptidases. Claim 21 does not further limit claim 1 and it is broader in scope. Correction is required.
When amending the claims, applicant is advised to carefully review all examined claims and make the necessary changes to ensure proper antecedent basis and dependency.
Claim Rejections - 35 USC § 112(a) or First Paragraph (pre-AIA )
Claims 1, 6-8, 20-21 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. This rejection is necessitated due to the introduction of new matter.
As set forth in MPEP 2163 (I)(B), new or amended claims which introduce elements or limitations that are not supported by the as-filed disclosure violate the written description requirement. See, e.g., In re Lukach, 442 F.2d 967, 169 USPQ 795 (CCPA 1971) (subgenus range was not supported by generic disclosure and specific example within the subgenus range); In re Smith, 458 F.2d 1389, 1395, 173 USPQ 679, 683 (CCPA 1972) (an adequate description of a genus may not support claims to a subgenus or species within the genus).
If one assumes that the % limitations recited in amended claims 1 and 6 refer to the total weight of the composition, amended claims 1, 6-8 and new claims 20-21, as interpreted are directed in part to compositions that require (a) at least 40% by weight of the total composition of the protein of SEQ ID NO: 5 (labeled as MjTET) and no greater than 60% by weight of the total composition of the protein of SEQ ID NO: 4 (labeled PhTET4), (b) at least 40% by weight of the total composition of the protein of SEQ ID NO: 4 (labeled as pHTET4) and no greater than 60% by weight of the total composition of the protein of SEQ ID NO: 5 (labeled as MjTET), (c) 90% by weight of the total composition of the protein of SEQ ID NO: 2 (labeled as pHTET2) and 10% by weight of the total composition of the protein of SEQ ID NO: 3 (labeled as pHTET3), (d) 33.33% by weight of the total composition of the protein of SEQ ID NO: 3 (labeled as pHTET3), 33.33% by weight of the total composition of the protein of SEQ ID NO: 5, and 33.33% by weight of the total composition of the protein of SEQ ID NO: 4, (e) 33.33% by weight of the total composition of the protein of SEQ ID NO: 1 (labeled as pHTET1), 33.33% by weight of the total composition of the protein of SEQ ID NO: 2 (labeled as pHTET2), and 33.33% by weight of the total composition of the protein of SEQ ID NO: 3, (f) 70% by weight of the total composition of the protein of SEQ ID NO: 2, 15% by weight of the total composition of the protein of SEQ ID NO: 3, and 15% by weight of the total composition of the protein of SEQ ID NO: 4, or (g) 70% by weight of the total composition of the protein of SEQ ID NO: 2, 15% by weight of the total composition of the protein of SEQ ID NO: 4, and 15% by weight of the total composition of the protein of SEQ ID NO: 5.
While the Examiner has found support for a composition where (i) the first aminopeptidase is PhTET4 and the second aminopeptidase is MjTET (PhTET4-MjTET), and (ii) the first aminopeptidase is PhTET2 and the second aminopeptidase is PhTET3, and the specification states that when the first and second aminopeptidases are not PhTET2 and PhTET3, the first aminopeptidase cannot represent more than 50% by weight of the composition, the Examiner has been unable to find support for a composition where the first aminopeptidase, which in the case of claim 1, parts (c) and (d) is PhTET4, can exceed 50%, as required by the term “at least 40%” in part (d), or by the term “no greater than 60%” in part (c). Please note that there is no support for the case where the first aminopeptidase is MjTET and the second aminopeptidase is PhTET4. In addition, while the specification discloses that when the composition has two aminopeptidases, the second aminopeptidase represents at least 60% by weight of the total composition, the Examiner has been unable to find support for a composition where the content of the second aminopeptidase, which in the case of claim 1, parts (f) and (g) is PhTET3, is 10% by weight of the total composition. Please note that there is no support for the case where the first aminopeptidase is PhTET3 and the second aminopeptidase is PhTET2. Also, while the Examiner has found support for a composition where (i) the first aminopeptidase is PhTET2, the second aminopeptidase is PhTET3, and the third aminopeptidase is PhTET4, (ii) the first aminopeptidase is PhTET2, the second aminopeptidase is PhTET4, and the third aminopeptidase is MjTET, (iii) the first aminopeptidase is PhTET1, the second aminopeptidase is PhTET2, and the third aminopeptidase is PhTET3, and (iv) the first aminopeptidase is PhTET3, the second aminopeptidase is PhTET4, and the third aminopeptidase is MjTET, and the specification discloses proportions by weight of the composition for the first, second and third aminopeptidases of 50/25/25, 40/30/30, 40/40/20, 10/10/80 and 10/20/70, the Examiner has not been able to find compositions where each of the 3 aminopeptidases in the composition represent 33.33% by weight of the composition, or any composition comprising three aminopeptidases, wherein the proportions by weight of the composition of the first, second and third aminopeptidases are 70/15/15. Thus there is no indication that the compositions required by the claims were within the scope of the invention as conceived by Applicant at the time of the invention. Accordingly, Applicant is required to cancel the new matter in the response to this Office Action.
Claim 3 was 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 and enablement requirements.
These rejections are now moot in view of the cancellation of this claim. Therefore, these rejections are hereby withdrawn.
Claim Rejections - 35 USC § 103 (AIA )
Claims 1, 6-8, remain rejected and new claims 20-21 are rejected under 35 U.S.C. 103 as being unpatentable over Appolaire et al. (Molecular Microbiology 94(4):803-814, 2014; cited in the IDS) in view of Tavano (Journal of Molecular Catalysis B: Enzymatic 90:1-11, 2013) as evidenced by UniProt accession No. P43133 (published 11/1/1995), and further in view of Persichetti et al. (J. Am. Chem. Soc. 117:2732-2737, 1995).
This rejection has been discussed in the previous Office action. It is maintained and further applied to new claims 20-21 for the reasons of record and those set forth below.
Applicant argues that Appolaire et al. disclose at most the aminopeptidases of PhTET2 and PhTET3 from P. horikoshii and only states that TET aminopeptidases occur in the form of large dodecameric complexes and that another reference of the prior art teach that PhTET1, PhTET2 and PhTET3 work together to break down intracellular polypeptides. Applicant states that Appolaire et al. also discloses an equimolar mixture of homo-oligomers of PhTET2 and PhTET3 and hetero-oligomers of PhTET2 and PhTET3 but fails to disclose or suggest the claimed combinations, much less the percentages set forth in the claims as currently presented.
Applicant states that the examples included in the specification show that the claimed compositions provide advantageous and surprisingly unexpected benefits including acceleration of the reaction speed and thus greatly increase the efficiency of hydrolysis of said peptides, particularly with low concentrations of 10% or 5% by weight relative to the total weight of the composition of aminopeptidases that are not specific to said peptides. Applicant states that the claimed combinations made it possible to overcome problems associated with the degradation of long and complex peptides and recovery after the degradation reaction and reuse of the aminopeptidases. Applicant states that the particular concentrations of the combinations of at least two or three aminopeptidases recited in the claims advantageously and unexpectedly allow the total hydrolysis of long peptides. Applicant submits that the examples in the specification demonstrate a surprising and unexpected effect with regard to a change in the degree of hydrolysis depending on the ratio/percentage by weight of the different TETs, the speed and efficiency of hydrolysis, the degradation of whey proteins, the hydrolysis of native gluten proteins, the overall efficiency of using a composition comprising several TET aminopeptidases, and the recovery and reuse of TET aminopeptidases in the form of cross-linked crystals.
With regard to the teachings of Tavano, Applicant states that this reference refers to loss of the enzyme thermolysin and is completely silent with regard to the aminopeptidases PhTET1, PhTET2, PhTET3, PhTET4 or MjTET. Applicant states that this reference does not disclose or suggest a composition comprising two aminopeptidases at the specific concentration recited in the claims. Applicant states that Tavano relates to the hydrolysis of proteins using proteases in the area of food biotechnology and does not teach TET aminopeptidases or cross-linked crystals. With regard to the teachings of Persichetti et al., Applicant states that Persichetti et al. do not teach the missing elements in the Appolaire and Tavano references. Applicant states that Persichetti et al. is silent with regard to the recited TET aminopeptidases or cross-linked crystals of these aminopeptidases and only refers to crystals of endopeptidases, in particular thermolysin. Applicant states that Persichetti et al. do not prompt a skilled artisan to apply cross-linked crystals of TET aminopeptidases. Applicant states that processes for crystallizing protein depend on the protein itself and the crystallization of one protein does not disclose or suggest a process for another protein. Applicant refers to the teachings of Doukov et al. (J. App. Cryst. 53:1493-1501, 2020) previously presented in support of the argument that the stability and other properties of crystalized proteins will always depend the specific crystal and enzyme used, and that the stability is dependent upon many factors that cannot be generalized to other proteins.
Applicant’s arguments have been fully considered but not deemed persuasive to overcome the instant rejection. The Examiner acknowledges the amendments made to the claims, the teachings of the specification and the prior art. However, the examine disagrees with Applicant’s contention that the claimed invention is not obvious over the cited prior art.
With regard to the argument that neither Appolaire et al., Tavano nor Persichetti et al. teach the recited combination of aminopeptidases at the recited % values, it is noted that as interpreted, no patentable weight has been given to the % values recited. See Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA ) for claim interpretation and the reasons why the limitations regarding % in the composition are indefinite. The aminopeptidases required in the claimed compositions are taught by the Appolaire et al., Tavano and Persichetti et al.
Contrary to Applicant’s assertions, Appolaire et al. teach not only the TET aminopeptidases of SEQ ID NO: 1, 3, and 3, labeled PhTET1, PhTET2 and PhTET3, respectively, but they also teach a composition comprising them by virtue of teaching that these three aminopeptidases are produced by Pyrococcus horikoshii and that the combined action of these three aminopeptidases allow the destruction of a vast variety of intracellular polypeptides. As previously indicated and admitted by Applicant, Appolaire et al. specifically teach an equimolar mixture (composition) of homo-oligomers of PhTET2 and PhTET3 and iso-stoichiometric hetero-oligomers between PhTET2 and PhTET3 monomers that significantly enhance the catalytic activity of the TET system (page 807, left column, lines 3-24; Figure 5). Therefore, while it is agreed that Appolaire et al. do not teach cross-linked crystals of these aminopeptidases, a composition that comprises PhTET1, PhTET2 and PhTET3, and a composition that comprises PhTET2 and PhTET3 are clearly taught by Appolaire et al.
With regard to the argument that Appolaire et al. do not teach a composition where the aminopeptidases are PhTET2 and/or PhTET3 with recited % content by weight, it is noted that while this limitation has not been considered in view of the indefiniteness of the recited limitation, modifying the concentration of the aminopeptidases to find one set of concentrations that works best for the intended use is deemed obvious since this is considered routine optimization. As set forth in MPEP § 2144.05 (II). it is well settled that routine optimization is not patentable, even though it results in significant improvement over the prior art. In the instant case, the prior art as evidenced by Appolaire et al. teach that equimolar compositions of the PhTET2 and PhTET3 aminopeptidases are beneficial for increased proteolytic activity, thus providing a starting point to find that optimal concentration.
In response to applicant's arguments stating that Appolaire et al. do not teach the claimed composition and that neither Tavano nor Persichetti et al. teach the claimed composition, Applicant is reminded that one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986).
As previously indicated, Tavano teaches that some of the many positive effects of food processing with proteases are improved digestibility, modifications of sensory quality, improvement of antioxidant capability, and reduction in allergenic compounds. Tavano teaches that the use of proteases in industrial processes can be advantageous compared to chemical processes because of increased hydrolysis specificity, product preservation and purity, and reduction in environmental impact. Tavano teaches that differences in specificity among proteases are very important to take into consideration as a guide for the choice of proteases according to the protein source to be hydrolyzed page 1, Abstract). Tavano teach that proteases include exopeptidases or aminopeptidases, and endopeptidases (page 2, right column, third full paragraph). Tavano teaches mixes of aminopeptidases and endopeptidases which would produce different hydrolysis products when applied to the same protein (page 2, right column, last 9 lines-page 3, left column, lines 1-13). Tavano teaches thermolysin as an endopeptidase that has been used for the production of peptides (page 8, right column, lines 1-3) as well as a thermolysin that is thermostable with higher hydrolysis potential (page 5, right column, lines 6-14). Tavano teaches that thermolysin preferentially releases C-terminal Leu and Phe at P1 position (page 3, Table 1). As evidenced by UniProt accession No. P43133, thermolysin (also called nprS, nprM or neutral protease) comprises SEQ ID NO: 6. See alignment below. Tavano teaches that thermostable enzymes obtained from thermophilic organisms have attracted the interest of scientists and a number of commercial applications have been developed as a result. Tavano teaches that thermostable proteases provide an advantage at higher temperatures since they are rigid enough to resist denaturation and avoid unfolding compared to mesophilic proteases. Tavano teach that for treatment of industrial wastes that contain hard to degrade animal proteins generated by the meat industry, thermostable enzymes from thermophilic microorganisms can be used at high temperature to induce thermal denaturation of the proteins, which would result in greater proteolysis susceptibility (page 5, left column, Using proteases from thermophilic microorganisms). In the instant case, the teachings of Tavano strongly suggest the use of thermosable proteases in food applications, and there is nothing in the prior art teaching or suggesting that the thermostable proteases of Appolaire et al. cannot be used in a protease composition for the degradation of food peptides as described by Tavano.
With regard to the argument that Persichetti et al. do not prompt a skilled artisan to apply cross-linked crystals of TET aminopeptidases, it is noted that the courts have made clear that the teaching, suggestion, or motivation test is flexible and an explicit suggestion to combine the prior art is not necessary. The motivation to combine may be implicit and may be found in the knowledge of one of ordinary skill in the art, or, in some cases, from the nature of the problem to be solved (MPEP § 2143 (G)). In the instant case, it is reiterated herein that while it is agreed that Persichetti et al. do not teach crosslinked crystals of the aminopeptidases of Appolaire et al., Persichetti et al. provide a clear motivation to use these aminopeptidases in crystal form. As previously indicated, Persichetti et al. teach cross-linked enzyme crystals of an endopeptidase (thermolysin) and disclose that these cross-linked crystals (CLECs) exhibit functional characteristics that are superior to those found in soluble or conventionally immobilized enzymes (page 2732, Abstract; left column, second paragraph). Persichetti et al. teach that these cross-linked enzyme crystals remain active in environments that are otherwise incompatible with enzyme function, such as prolonged exposure to high temperature, near-anhydrous organic solvents, and aqueous organic solvent mixtures. Persichetti et al. teach that these CLECs are highly stable against autolysis and exogenous protease degradation, thus making CLECs attractive as catalysts (page 2732, left column, second paragraph). One of skill in the art would have been highly motivated to use crosslinked crystals of the aminopeptidases of Appolaire et al. for the benefit of using a catalyst that remains active in environments that are otherwise incompatible with enzyme function, and is highly stable against autolysis and exogenous protease degradation, as taught by Persichetti et al. It is noted that thermolysin and the aminopeptidases of Appolaire et al. are both thermostable peptide-cleaving enzymes.
With regard to the argument that processes for crystallizing protein depend on the protein itself and the crystallization of one protein does not disclose or suggest a process for another protein., it is noted that nowhere in the specification, there is any indication that the crystallization of the proteins of SEQ ID NO: 1, 2, 3, 4, or 5 required a method not known in the art, or that crystallization of these proteins posed a challenge. In fact, the specification only mentions that the protein of SEQ ID NO: 3 was crystalized using the method of drops suspended on 24-well plates. As evidenced by Bauer et al. (Acta Cryst. D58, page 2216, 2002), protein crystallization using plates having wells where a solution comprising the desired protein is dropped into the wells is well known in the art (middle column). While the specification merely states the method by which the protein of SEQ ID NO: 3 was crystalized and cross-linked, in view of the knowledge of the art with regard to crystallization and cross-linked crystals, the Examiner has found that the claims are fully enabled and described with regard to the crystallization and cross linking of the crystals of the proteins of SEQ ID NO: 1-5. If Applicant is arguing that the crystallization and cross-linking of crystals is unexpected or that there is no reasonable expectation of success in making crystals of the proteins of SEQ ID NO: 1-5 and cross-linking them, the Examiner will have to reconsider the enablement and written description of the claims as currently presented.
The teachings of Doukov et al. have been previously addressed. It is reiterated herein that this reference refers to collecting X-ray diffraction data from protein crystals across physiological temperatures. While it is agreed that Doukov et al. teach that crystals are more sensitive to radiation damage at room temperature compared to cryo-temperatures, the crystals of the composition of the claims are not being subjected to X-ray or radiation damage. The “stability” issue argued by Applicant refers to the effect of radiation damage as a function of temperature and how to obtain X-ray diffraction data at and above room temperature at resolutions approaching those available at cold temperatures (cryo-temperatures; page 1494, right column, Experimental). Nowhere in the reference by Doukov et al. there is a teaching or suggestion indicating that (i) it is highly likely that crystals of thermostable enzymes are enzymatically inactive at temperatures known to be optimal for such enzymes in solution, or (ii) it is highly likely that crystals of thermostable enzymes such as aminopeptidases cannot be obtained. Therefore, the teachings of Doukov et al. are deemed irrelevant to the instant discussion.
With regard to the arguments that the examples included in the specification show that the claimed compositions provide advantageous and surprisingly unexpected benefits including acceleration of the reaction speed and thus greatly increase the efficiency of hydrolysis of peptides, particularly with low concentrations of 10% or 5% by weight relative to the total weight of the composition of aminopeptidases that are not specific to said peptides, it is noted that the claims appear to require concentrations of up to 95% by weight of composition of an aminopeptidase. None of the compositions claimed require solely 10% or 5% by weight of aminopeptidases in total. There are compositions that require 95% of one aminopeptidase and 5% of another. With regard to the argument that the claimed combinations made it possible to overcome problems associated with the degradation of long and complex peptides such as gluten proteins and whey proteins, and recovery after the degradation reaction and reuse of the aminopeptidases, it is noted that the synergistic effect on degradation of long peptides by combining aminopeptidases having different specificity is clearly taught by Tavano who teaches mixes of aminopeptidases and endopeptidases which would produce different hydrolysis products when applied to the same protein. In the instant case, Appolaire et al. teach that PhTET1, PhTET2 and PhTET3 have different specificities. Moreover, this effective degradation is clearly suggested by Appolaire et al. who teach that the complementary action of these TET aminopeptidases allow the destruction of a vast variety of intracellular polypeptides (page 804, left column, lines 21-33). Therefore, it is not surprising that by combining different aminopeptidases like in the compositions of the claims, one of skill in the art would reasonably expect to observe better degradation of long and complex peptides, compared to the degradation observed when only one aminopeptidase is used. With regard to the issue of reuse and recovery of the aminopeptidases, this is not surprising in view of the teachings of Persichetti et al. who teach that cross-linked enzyme crystals (CLECs) remain active in environments that are otherwise incompatible with enzyme function, such as prolonged exposure to high temperature, near-anhydrous organic solvents, and aqueous organic solvent mixtures, and are highly stable against autolysis and exogenous protease degradation, thus making CLECs attractive as catalysts (page 2732, left column, second paragraph).
Therefore, for the reasons of record and those set forth above, one of skill in the art would conclude that the claimed invention is obvious over the prior art of record.
Conclusion
No claim is in condition for allowance.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a). A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the date of this final action.
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Any inquiry concerning this communication or earlier communications from the examiner should be directed to DELIA M RAMIREZ, Ph.D., whose telephone number is (571) 272-0938. The examiner can normally be reached on Monday-Friday from 8:30 AM to 5:00 PM. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert B. Mondesi, can be reached at (408) 918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
/DELIA M RAMIREZ/Primary Examiner, Art Unit 1652
DR
January 5, 2026