Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
DETAILED ACTION
Claims 1 and 49-51 are pending and under examination on their merits. Claim 29 is now cancelled.
The statutory double patenting rejection of instant claim 1 over claim 1 of U.S. Patent No. 8,097,434 is withdrawn in view of the amendment.
The nonstatutory double patenting rejection of instant claim 1 over claim 4 of U.S. Patent No. 11,572,579 is withdrawn in view of the amendment.
Response to Arguments
Applicant's arguments filed 10/29/2025 have been fully considered but they are not persuasive.
Applicant requests that the nonstatutory double patenting rejections be held in abeyance (Arguments, paragraph 2 on page 5).
Per MPEP 804, part (I)(B)(1), only compliance with objections or requirements as to form not necessary for further consideration of the claims may be held in abeyance until allowable subject matter is indicated.
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.
(New Rejection Necessitated by Amendment) Claims 1 and 49-51 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.
In claim 1, the limitation “wherein each composition comprises lysozyme, trehalose and EDTA” renders the claim indefinite because it is uncertain whether each composition comprises lysozyme, trehalose and EDTA, or each composition further comprises lysozyme, trehalose and EDTA in addition to the respective components recited in (a)(i) and (a)(ii).
Claim 50 recites the limitation "the spectral change or fluorescent change of the compositions" in line 2. There is insufficient antecedent basis for this limitation in the claim.
Claims 49-51 are rejected for depending from a rejected base claim and not rectifying the source of indefiniteness discussed above.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
The following rejections are necessitated by the amendment.
Claims 1 and 49-51 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 7-9, and 16 of U.S. Patent No. 8,389,234 (hereafter ‘234) in view of Arakawa (WO 2006043558 A1; cited in the Non-Final Action mailed on 4/29/2025) and Matagne et al. (Biochem. J 295 (1993): 705-711) as evidenced by Drawz et. al (Clinical microbiology reviews 23.1 (2010): 160-201; cited in the Non-Final Action mailed on 4/29/2025).
Claim 1 of ‘234 is drawn to a kit for detecting the presence of a beta-lactamase comprising, in one or more containers, a first composition and a second composition. The first composition comprises a detectable beta-lactamase-substrate and an AmpC inhibitor. The second composition comprises a detectable beta-lactamase substrate, an AmpC inhibitor, and a serine beta-lactamase inhibitor in an amount sufficient to inhibit an extended-spectrum beta-lactamase and an original-spectrum beta-lactamase but not a class A serine carbapenemase.
Claim 7 of ‘234 recites that the detectable beta-lactamase substrate is nitrocefin.
Claim 8 of ‘234 recites that the AmpC inhibitor is cloxacillin.
Claim 9 of ‘234 recites that the serine beta-lactamase inhibitor is clavulanic acid.
Claim 16 of ‘234 recites that each composition comprises lysozyme, trehalose and EDTA.
Claims 1, 7-9, and 16 of ‘234 do not recite a method comprising:
contacting a first bacterial sample with the first composition and
contacting a second bacterial sample with the second composition,
wherein the first and second bacterial samples are from the same source; and detecting utilization of the substrate in the first composition and the second composition, such that a beta-lactamase is detected if the substrate has been utilized in the first and second compositions, wherein the beta-lactamase is a class A serine carbapenemase or a metallo-beta-lactamase.
Arakawa teaches contacting a system with bacterial cells or bacterial extract, allowing a reaction between the substrate and any beta-lactamases produced by the bacteria to occur in the system ([0016]). After the reaction, the activity of the analyte in each test system is assayed by a color development method ([0017]), such as by utilizing a chromogenic substrate ([0020]).
Arakawa teaches nitrocefin is a chromogenic substrate degraded by beta-lactamase ([0020]).
Arakawa teaches three test systems, each system comprising two inhibitors ([0014]). System A includes a class B beta-lactamase inhibitor and a class C beta-lactamase inhibitor so that system A has a color change when the bacteria produces a class A beta-lactamase ([0022]). System B contains a class A inhibitor and a class C inhibitor so that system B has a color change when the bacteria produces a class B beta-lactamase ([0022]). System C contains a class A and a class B beta-lactamase inhibitor, so that system C has a color change when the bacteria produces a class C beta-lactamase ([0022]). Arakawa teaches that AmpC is a class C beta-lactamase ([0035]), thus it necessarily follows that a class C beta-lactamase inhibitor is an AmpC inhibitor.
It would have been obvious to the person of ordinary skill in the art before the effective filing date of the claimed invention based upon the preamble of claim 1 of ‘234 (“a kit for detecting the presence of a beta-lactamase”), which makes clear the intended use of the kit, to use the kit of claims 1, 7-9, and 16 of ‘234 in the manner suggested by Arakawa. In particular, it would have been obvious to a person of ordinary skill in the art to process a bacterial sample in parallel in the containers of the kit of claim 1 of ‘234 in order to both detect and classify any beta-lactamases produced by the bacterial sample by measuring the color change in each container, as suggested by Arakawa. The person of ordinary skill in the art would have recognized that if the bacteria produced a beta-lactamase, there would have been a detectable color change in the first and/or the second containers of the kit of claims 1, 7-9, and 16 of ‘234.
Metallo-beta-lactamases are class B beta-lactamases, which have a different mechanism of hydrolysis than serine beta-lactamases, as evidenced by Drawz (Classification, left column, bottom paragraph, page 164).
Therefore, substrate utilization in the first and second containers of the kit of claims 1, 7-9, and 16 of ‘234 would have necessarily indicated the presence of a class A serine carbapenemase or a metallo-beta-lactamase (class B beta-lactamase).
Claims 1, 7-9, and 16 of ‘234 do not recite the concentration of cloxacillin, nitrocefin, or clavulanic acid.
Matagne teaches that clavulanic acid displays potent beta-lactamase inhibitory properties (page 707, right column, Results, Clavulanic acid, paragraph 1). Matagne teaches that clavulanic acid transiently inhibits beta-lactamase from S. cacaoi at low concentration but irreversibly inactivates the beta-lactamase at higher concentrations (page 707, right column, Results, Clavulanic acid, bottom paragraph). Furthermore, Matagne teaches assaying samples for beta-lactamase activity against 100 µM nitrocefin after various periods of time (Figure 2 caption).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to optimize by routine experimentation the concentration of cloxacillin and clavulanic acid in the method of claims 1, 7-9, and 16 of ‘234. The person of ordinary skill in the art would have had a reasonable expectation of success given that dependent claim 8 of ‘234 recites that the AmC inhibitor is cloxacillin and dependent claim 9 of ‘234 recites that the serine beta-lactamase inhibitor is clavulanic acid.
It would have been further obvious to use 100 µM nitrocefin per the teaching of Matagne as the detectable beta-lactamase substrate in the method of claims 1, 7-9, and 16 of ‘234 modified by Arakawa. The person of ordinary skill in the art would have had a reasonable expectation of success in applying Matagne’s teaching regarding the specific choice of detectable beta-lactamase substrate and the concentration.
Regarding claim 49, Arakawa teaches that the reaction time for the degradation of the chromogenic substrate (nitrocefin) is about 5 min to 30 min ([0016] and [0020]), which overlaps with the claimed range of 2 min to 5 hours.
Regarding claim 50, Arakawa teaches detecting substrate utilization by assessing color change in each of the systems ([0020]) and [0022]), which is assessing spectral change because visual color change is a specific spectral change.
Regarding claim 51, claims 1, 7-9, and 16 of ‘234 do not recite that the sample is from a human suspected of having a bacterial infection. However, Arakawa refers to the prevalence of resistant bacteria as a serious clinical problem ([0004]).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to apply the method of claims 1, 7-9, and 16 of ‘234 modified by Arakawa and Matagne to a sample from a human suspected of having a bacterial infection in order to better determine a course of antibiotic treatment for the patient. The person of ordinary skill in the art would have had a reasonable expectation of success in applying the method to a sample from a human suspected of having a bacterial infection.
Claim 1 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 6, 8, 10-13, and 15-16 of U.S. Patent No. 8,097,434 (hereafter ‘434) Although the claims at issue are not identical, they are not patentably distinct from each other because instant claim 1 is obvious over claims 1, 6, 8, 10-13, and 15-16 of ‘434.
Claim 1 of ‘434 is drawn to a method for detecting the presence of a beta-lactamase, comprising step (a) and (b). Steps (a) and (b) are identical to the active steps of the method recited in instant claim 1.
Claim 6 of ‘434 recites that each composition comprises a lysis reagent and optionally an agent that promotes stabilization of the lysis reagent or an agent that enhances lysis of a bacterial cell by a lysis reagent.
Claim 8 of ‘434 recites that each composition comprises lysozyme, trehalose and EDTA. Claim 10 of ‘434 recites that the serine beta-lactamase inhibitor is clavulanic acid and claim 11 of ‘434 recites that the amount of clavulanic acid is about 0.01 mM to about 100 mM.
Claim 12 of ‘434 recites that the AmpC inhibitor is cloxacillin and claim 13 of ‘434 recites that the concentration of cloxacillin is 0.01 mM to 100 mM, which matches the presently claimed range.
Claim 15 of ‘434 recites that the detectable beta-lactamase substrate is nitrocefin and claim 16 of ‘434 recites that the concentration of nitrocefin is 1 µM to about 1 mM, which matches the presently claimed range.
Therefore, each of the limitations recited in instant claim 1 is claimed in dependent claims 8, 10-13, and 15-16 of ‘434, which each depend from independent claim 1 of ‘434.
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to use nitrocefin at a concentration of 1 µM to about 1 mM as the detectable beta-lactamase substrate in the method of claim 1 of ‘434. It would have been further obvious to use cloxacillin at a concentration of 0.01 mM to 100 mM as the AmpC inhibitor and to use clavulanic acid at a concentration of 0.01 mM to 100 mM as the serine beta-lactamase inhibitor in the method of claim 1 of ‘434. The person of ordinary skill in the art would have recognized each of the compounds as fulfilling the requirements of the detectable beta-lactamase substrate, AmpC inhibitor, and serine beta-lactamase inhibitor since the dependent claims 8, 10-13 and 15-16 of ‘434 each recite these compounds and concentrations. Likewise, it would have been obvious to include trehalose, EDTA, and lysozyme in each composition, which the person of ordinary skill in the art would have recognized as components of a lysis reagent or additives to a lysis reagent (see claim 6 of ‘434).
Claims 49-51 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 6, 8, 10-13, and 15-16 of U.S. Patent No. 8,097,434 (hereafter ‘434) in view of Arakawa (WO 2006043558 A1; cited in the Non-Final Action mailed on 4/29/2025).
See discussion of claims 1, 6, 8, 10-13, and 15-16 of ‘434 above, which is incorporated into this rejection.
Claims 1, 6, 8, 10-13, and 15-16 of ‘434 do not recite how long after contacting the compositions with the bacterial samples the utilization of the substrate is detected (claim 49), that substrate utilization is detected by spectral change (claim 50), or that the bacterial sample is obtained from a human suspected of having a bacterial infection (claim 51).
Arakawa teaches contacting a system with bacterial cells or bacterial extract, allowing a reaction between the substrate and any beta-lactamases produced by the bacteria to occur in the systems ([0016]). After the reaction, the activity of the analyte in each test system is assayed by a color development method ([0017]), such as by utilizing a chromogenic substrate ([0020]).
Arakawa teaches nitrocefin is a chromogenic substrate degraded by beta-lactamase ([0020]).
Regarding claim 49, Arakawa teaches that the reaction time for the degradation of the chromogenic substrate (nitrocefin) is about 5 min to 30 min ([0016] and [0020]), which overlaps with the claimed range of 2 min to 5 hours.
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to optimize by routine experimentation the timing of detecting the degradation of the nitrocefin in the method of claims 1, 6, 8, 10-13, and 15-16 of ‘434. The person of ordinary skill in the art would have had a reasonable expectation of success in optimizing the timing based upon the reaction times suggested by Arakawa.
Regarding claim 50, Arakawa teaches detecting substrate utilization by assessing color change in each of the systems ([0020]) and [0022]), which is assessing spectral change because visual color change is a specific spectral change.
Since Arakawa teaches the utilization of the nitrocefin (chromogenic substrate) results in a color change, then it would have been obvious to the person of ordinary skill in the art before the effective filing date of the claimed invention to assess color change (spectral change) in the method of claims 1, 6, 8, 10-13 and 15-16 of ‘434 because claim 15 of ‘434 recites that the detectable beta-lactamase substrate is nitrocefin and step (b) of claim 1 of ‘434 recites detecting substrate utilization.
Regarding claim 51, claims 1, 6, 8, 10-13 and 15-16 of ‘434 do not recite that the sample is from a human suspected of having a bacterial infection. However, Arakawa refers to the prevalence of resistant bacteria as a serious clinical problem ([0004]).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to apply the method of claims 1, 6, 8, 10-13 and 15-16 of ‘434 to a sample from a human suspected of having a bacterial infection in order to better determine a course of antibiotic treatment for the patient. The person of ordinary skill in the art would have had a reasonable expectation of success in applying the method to a sample from a human suspected of having a bacterial infection.
Claims 1 and 49-51 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 8 and 19-22 of U.S. Patent No. 9,902,989 (hereafter ‘989) in view of Arakawa (WO 2006043558 A1; cited in the Non-Final Action mailed on 4/29/2025), Matagne et al. (Biochem. J 295 (1993): 705-711), Raquet et al. (Proteins: Structure, Function, and Bioinformatics 27.1 (1997): 47-58), and Poirel et al. (Journal of Clinical Microbiology, Aug. 2003, p. 3542–3547).
Claims 19-22 of ‘989 depend from claims 1-3. Claims 1-3 are drawn to a method for detecting the presence of a beta-lactamase comprising contacting a single volume of a liquid bacterial sample comprising intact bacterial cells with a solid support containing a dried composition comprising an amount of a detectable beta-lactamase substrate and detecting beta-lactamase substrate utilization. Claim 19 requires that each composition comprises a lysozyme, trehalose, and EDTA. Claims 19-22 of ‘989 require that the dried composition further comprises a serine beta-lactamase inhibitor in an amount sufficient to inhibit an extended spectrum beta-lactamase and an original-spectrum beta-lactamase but not a class A serine carbapenemase.
Claim 8 of ‘989 recites that the detectable beta-lactamase substrate is nitrocefin.
Claims 8 and 19-22 of ‘989 do not recite that the dried composition (“second composition”) comprises the AmpC inhibitor. Claims 19-22 of ‘989 do not recite a first composition comprising a detectable beta-lactamase substrate and an AmpC inhibitor.
Claims 8 and 19-22 of ‘989 do not recite that the AmpC inhibitor is cloxacillin or that the serine beta-lactamase inhibitor is clavulanic acid.
Claims 8 and 19-22 of ‘989 do not recite the concentration of the AmpC inhibitor, the concentration of the detectable beta-lactamase substrate, or the exact amount of the serine beta lactamase inhibitor.
Arakawa teaches contacting a system with bacterial cells or bacterial extract, allowing a reaction between the substrate and any beta-lactamases produced by the bacteria to occur in the systems ([0016]). After the reaction, the activity of the analyte in each test system is assayed by a color development method ([0017]), such as by utilizing a chromogenic substrate ([0020]).
Arakawa teaches three test systems, each system comprising two inhibitors ([0014]). System A includes a class B beta-lactamase inhibitor and a class C beta-lactamase inhibitor so that system A has a color change when the bacteria produces a class A beta-lactamase ([0022]). System B contains a class A inhibitor and a class C inhibitor so that system B has a color change when the bacteria produces a class B beta-lactamase ([0022]). System C contains a class A and a class B beta-lactamase inhibitor, so that system C has a color change when the bacteria produces a class C beta-lactamase ([0022]). Arakawa teaches that class A beta-lactamase inhibitors include clavulanic acid ([0011]). AmpC is a class C beta-lactamase ([0035]), thus it necessarily follows that a class C beta-lactamase inhibitor is an AmpC inhibitor.
Arakawa teaches nitrocefin is a chromogenic substrate degraded by beta-lactamase ([0020]).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to add a step of contacting a bacterial sample with a container comprising a detectable beta-lactamase substrate, a class B beta-lactamase inhibitor, and a class C beta-lactamase inhibitor, per the teachings of Arakawa regarding system A. It would have been further obvious to add a class C beta-lactamase inhibitor to the dried composition (“second composition”) in the method of claims 8 and 19-22 of ‘989 in order to inhibit a class C beta-lactamase, per the teachings of Arakawa regarding system B. The person of ordinary skill in the art would have been motivated to detect whether or not the bacteria produced a class A beta-lactamase (determined by a color change in the system A of Arakawa) and if so, whether or not the class A beta-lactamase was a class A serine carbapenemase.
Regarding the concentration of nitrocefin, it would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to optimize by routine experimentation the concentration of nitrocefin (detectable beta-lactamase substrate) in the method of claims 8 and 19-22 of ‘989. The person of ordinary skill in the art would have had a reasonable expectation of success in optimizing the concentration of nitrocefin given that claim 8 of ‘989 recites that nitrocefin is the detectable beta-lactamase substrate.
Regarding the serine beta-lactamase inhibitor, Matagne teaches that clavulanic acid displays potent beta-lactamase inhibitory properties (page 707, right column, Results, Clavulanic acid, paragraph 1). Matagne teaches that clavulanic acid transiently inhibits beta-lactamase from S. cacaoi at low concentration but irreversibly inactivates the beta-lactamase at higher concentrations (page 707, right column, Results, Clavulanic acid, bottom paragraph). Furthermore, Matagne teaches assaying samples for beta-lactamase activity against 100 µM nitrocefin after various periods of time (Figure 2 caption).
Raquet teaches that the beta-lactamase from S. cacaoi is a class A carbapenem-hydrolyzing beta-lactamase (“carbapenemase”): see Title and page 55, right column first full paragraph).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to specifically use clavulanic acid as the serine beta-lactamase inhibitor in the method of claims 8 and 19-22 of ‘989 modified by Arakawa. The person of ordinary skill in the art would have been motivated by the teaching of Matagne, which suggests that at low concentrations clavulanic acid only transiently inactivates class A carbapenemase. Thus, at low concentrations and after sufficient time, clavulanic acid does not inhibit class A carbapenemase. It would have been further obvious to optimize by routine experimentation the concentration of the clavulanic acid in the method of claims 8 and 19-22 of ‘989 modified by Arakawa, Matagne, and Raquet.
It would have been further obvious to use 100 µM nitrocefin per the teaching of Matagne as the detectable beta-lactamase substrate in the method of claims 8 and 19-22 of ‘989 modified by Arakawa. The person of ordinary skill in the art would have had a reasonable expectation of success in applying Matagne’s teaching regarding the specific choice of beta-lactam and the concentration. 100 µM nitrocefin is within the claimed range of 1 μm about 1 mM.
Regarding the AmpC inhibitor and its concentration, Poirel teaches that cloxacillin counteracts the effects of high-level expression of AmpC-type beta lactamase at a concentration of 200 µg/ml (page 3543, left column, top paragraph), which is equivalent to 0.5 mM. 0.5 mM is within the claimed range of 0.01 mM to 100 mM.
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to use Poirel’s cloxacillin as the AmpC inhibitor the method of claims 8 and 19-22 of ‘989 modified by Arakawa, Matagne, and Raquet. The person of ordinary skill in the art would have been motivated by the teaching of Poirel, which demonstrates that cloxacillin is capable of inhibiting AmpC at a concentration of 200 µg/ml (equivalent to 0.5 mM).
Regarding the requirement that the serine beta-lactamase inhibitor is capable of inhibiting ordinary-spectrum beta-lactamase (OSBL) and extended-spectrum beta-lactamase (ESBL), Poirel teaches that clavulanic acid inhibits ESBL (Abstract) at a concentration of 2 µg/mL (Footnote Table 1 on page 3544), which is equivalent to 0.01 mM. This concentration is far less than the amount shown by Matagne to permanently inhibit the class A serine carbapenemase from S. cacaoi (see Matagne Figure 2 caption). Furthermore, Matagne teaches that clavulanic acid displays potent beta-lactamase inhibitory properties (page 707, right column, Results, Clavulanic acid, paragraph 1), so clavulanic acid also inhibits ordinary-spectrum beta-lactamases.
Regarding claim 49, Arakawa teaches that the reaction time for the degradation of the chromogenic substrate (nitrocefin) is about 5 min to 30 min ([0016] and [0020]), which overlaps with the claimed range of 2 min to 5 hours.
Regarding claim 50, Arakawa teaches detecting substrate utilization by assessing color change in each of the systems ([0020]) and [0022]), which is assessing spectral change because visual color change is a specific spectral change.
Regarding claim 51, claims 8 and 19-22 of ‘989 do not recite that the sample is from a human suspected of having a bacterial infection. However, Arakawa refers to the prevalence of resistant bacteria as a serious clinical problem ([0004]).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to apply the method of claims 8 and 19-22 of ‘989 modified by Arakawa, Matagne, Raquet, and Poirel to a sample from a human suspected of having a bacterial infection in order to better determine a course of antibiotic treatment for the patient. The person of ordinary skill in the art would have had a reasonable expectation of success in applying the method to a sample from a human suspected of having a bacterial infection.
Conclusion
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 nonprovisional extension fee (37 CFR 1.17(a)) 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 mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CANDICE LEE SWIFT whose telephone number is (571)272-0177. The examiner can normally be reached M-F 8:00 AM-4:30 PM (Eastern).
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/CANDICE LEE SWIFT/Examiner, Art Unit 1657
/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657