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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission, filed on 18 February 2026, has been entered.
Status of Application, Amendments and/or Claims
The amendment and Applicant’s arguments, filed 02 February 2026, has been entered in full. Claims 33-37 are withdrawn from consideration as being drawn to a non-elected invention. Claims 3 and 6 are canceled. Claims 1, 4, 5, 15-17, 22 and 24 are amended. Claims 1, 2, 4, 5, 7-32 are under examination.
Withdrawn Objections And/Or Rejections
The rejection to claims 1, 2, 4, 5, 7-15 and 22-32 under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception without significantly more, as forth at pages 3-8 of the previous Office Action (03 November 2025), is withdrawn in view of the amendment and Applicant’s arguments (02 February 2026).
Claim Rejections - 35 USC § 103
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.
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.
1. Claims 1, 2, 4, 5, 7-12, 16-19 remain rejected under 35 U.S.C. 103 as being unpatentable over Mutharia et al. (US 2016/0215028; published 7/28/16) in view of Willemsen et al. (Veterinary Microbiology 114:337-344; 2006) and Li et al. (Clinical and Vaccine Immunology, Volume 14, No. 1, pages 102-105, Jan. 2007).
The basis for this rejection is set forth at pages 8-12 and 13-16 of the previous Office Action (03 November 2025).
Mutharia et al. teach identifying a number of MAP derived antigens within the MAP culture filtrate (CF) proteome listed in Table 2. Mutharia et al. teach recombinantly producing MAP proteins (paras 0008-0011, 0093-0098)(applies to claim 1 and 16). Mutharia et al. teach four protein antigens (MAP0196c, MAP0471, MAP1981c and MAP1569) were identified that reacted with 35 serum samples from MAP-infected COWS ranging from low to high shedders (para 0007) (applies to claims 1, 7, 8 and 16).
Mutharia et al. teach a recombinant expression vector comprising a nucleic acid molecule encoding for MAP proteins as described herein. Mutharia et al. teach host cells transfected with a recombinant expression vector comprising a nucleic acid molecule encoding for a MAP protein as described herein. Mutharia et al. teach a method for the production of a MAP protein comprising culturing a host cell transfected with a vector comprising a nucleic acid molecule encoding for the MAP protein as described herein. Mutharia et al. teach recombinant proteins were purified by immobilized metal affinity chromatography and employing purification buffers (paras 0010, 0011 and 0095)(applies to claims 1 and 16).
Mutharia et al. teach proteins that are secreted into culture filtrate by MAP, including the proteins listed in Table 2. Mutharia teach that these proteins are useful as biomarkers for the detection of MAP in a sample from a subject. In one embodiment, these proteins are useful as antigens. In one embodiment, the protein binds to sera from an animal infected with MAP (paras 0009 and 0045)(applies to claims 1, 7, 9, 16 and 18). Mutharia et al. teach in some embodiments, the methods described herein use multiplex technology in order to determine the presence or absence of a plurality of proteins listed in Table 2. Mutharia et al. teach that this technology has the advantage of quantifying multiple proteins simultaneously in one sample (para 0059).
Table 2 teaches antigens MAP1272c, MAP1569, MAP1201c, MAP3531c, and MAP4143 (applies to claims 1, 2, 4, 5 and 17). Mutharia et al. teach the antigens reacted on immunoblotting with individual serum from 35 MAP-infected COWS (paras 0062 and 0093) (applies to claims 9-11, 18). Mutharia et al. teach in addition, sera from low MAP shedders (<10 CFU) also reacted with at least one of these antigens (para 0093) (applies to claim 8). Mutharia et al. teach the proteins represent useful biomarkers for the detection of MAP infections and the use of these antigens in an ELISA-based format may aid in the immediate management of Johne's disease by detecting those animals shedding low CFUs of MAP (para 0093) (i.e. MAP antigens immobilized on solid support; applies to claims 1, 12, 16 and 19). Mutharia et al. summarizes by teaching MAP proteins detected antibodies in cow sera using ELISA and that the results demonstrate that these proteins can differentiate infected from uninfected animals (para 0110).
Mutharia et al. do not teach using MAP2609 to detect an antibody indicative of infection with MAP in a sample obtained from an animal.
Willemsen et al. teach MAP is the causative agent of paratuberculosis or Johne’s disease, a chronic enteritis in ruminants. Willemsen et al. teach the overexpression and purification of recombinant antigens MAP2609, MAP2942c and MAP0210c (page 338, right column, last paragraph)(applies to claims 1, 2, 4, 5, 10, 16 and 17). Willemsen et al. teach incubating MAP2609, MAP2942c and MAP0210c with serum from cows infected with MAP (applies to claims 1, 2, 4, 5, 7, 9, 17 and 18). . Willemsen et al. teach that MAP2609, MAP2942c and MAP0210c were shown to be recognized by antibodies from sera of subclinical infected cattle and infected cattle (abstract)(applies to claim 8). Willemsen et al. teach the reactivity of antibodies in the infected serum using ELISA (abstract, Figure 2 and page 341)(i.e. MAP antigens immobilized on solid support; applies to claim 1, 7, 9-12, 16, 18 and 19).
Li et al. teach Johne’s disease as a chronic gastrointestinal inflammatory disease caused by mycobacterium avium subsp. paratuberculosis (MAP) which occurs in domestic ruminants such as dairy cattle. Li et al. teach the recombinant production and purification of MAP derived antigen proteins MAP1272c and MAP2121c (pages 102, right column-page 103)(applies to claims 4, 5 and 17). Li et al. teach incubating MAP derived antigen proteins MAP1272c and MAP2121c with serum from cattle infected with MAP (page 103, right column, last paragraph and Figure 1)(applies to claims 4, 5 and 17). Li et al. teach MAP1272c and MAP2121c proteins were able to detect MAP antibodies in ELISA, using serum from cattle infected with MAP compared to cattle not infected with MAP (Table 1 and page 104, first full paragraph)(i.e. MAP antigens immobilized on solid support).
It would have been oblivious for one of ordinary skill in the art before the effective filling date to modify a method of detecting antibodies indicative of infection with MAP or detecting antibodies which are associated with MAP in a biological sample comprising detecting antibodies in a biological sample, using MAP derived antigens MAP1569, MAP1201c, MAP3531c, and MAP4143, as taught by Mutharia et al., by including MAP derived antigens MAP2609, MAP2942c, as taught by Willemsen et al. and MAP1272c and MAP2121c, as taught by Li et al., wherein the MAP derived antigens are recombinant and are immobilized on a solid support wherein specific binding between the immobilized MAP derived antigens and the antibody are detected, as taught by Mutharia, Willemsen and Li.
One of ordinary skill in the art before the effective filing date, would have been motivated to make such modifications and expect success for the following reasons.
The Mutharia, Willemsen and Li references all teach specific MAP derived antigens that positively bind antibodies in biological samples of infected animals. Using the MAP derived antigens, as taught by Mutharia, Willemsen and Li, allows different types of antibodies associated with MAP infection to be identified because there is a chance that a single MAP-specific antigen may not be recognized in every infected cattle.
APPLICANT’S ARGUMENT ONE: Applicant discusses MPEP 2141, MPEP 2141.02, MPEP 2143.01 and cites case law. Applicant states that as currently amended, the claims are NOT obvious over any of the cited combinations because the rejections fail to establish:
(i) a reasoned motivation to combine the specific antigens in the manner claimed; (ii) a reasonable expectation of success in doing so; and (iii) disclosure or suggestion of the claimed diagnostic configuration.
Applicant argues that the Office Improperly Conflates Disclosure of Individual Antigens with a Motivation to Combine. Applicant discusses the pending rejection. Applicant cites case law and MPEP 2143. Applicant argues that the Office never articulates a reasoned motivation-grounded in the art to select those two antigens from among numerous disclosed candidates and to use them together, in purified recombinant form and immobilized on a solid support, to detect MAP antibodies.
Applicant argues that as amended, the independent claims require all of the following in combination: purified recombinant MAP1569; purified recombinant MAP2609 and use of the immobilized antigens to detect specific antibody binding in a diagnostic assay.
Applicant argues that none of the cited prior art references either individually or in combination teach or suggest this configuration. Applicant argues that Willemsen identifies three secreted antigens but does NOT disclose MAP1569, NOR does it teach immobilizing purified recombinant MAP2609 on a solid support. Mutharia identifies MAP1569 among numerous culture-filtrate proteins but does NOT teach recombinant expression, purification, or immobilization with MAP2609. Li examines recombinant MAP1272c and MAP2121c, NOT MAP1569 or MAP2609. Applicant cites case law.
Applicant’s arguments have been fully considered but are not found persuasive for the following reasons:
a. As was stated above, the instant rejection is a 103 rejection NOT a 102 rejection. One cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references.
In the instant case, Mutharia teaches MAP1569 and Willemsen teaches MAP2609 to detect antibodies indicative of infection (applies to claim 1). In addition, Li et al. teach other cited MAP derived antigens that detect antibodies indicative of infection.
b. In response to Applicant’s argument that the Office never articulates a reasoned motivation-grounded in the art to select those two antigens from among numerous disclosed candidates and to use them together, in purified recombinant form and immobilized on a solid support, to detect MAP antibodies;
The Office Action clearly stated that Mutharia, Willemsen and Li, all teach specific MAP derived antigens that positively bind antibodies in biological samples of infected animals. That is to say, Mutharia, Willemsen and Li teach the claimed MAP antigens AND that those particular MAP antigens bind to antibodies in samples from infected animals. Using the MAP derived antigens, as taught by the combined references, allows different types of antibodies associated with MAP infection to be identified because there is a chance that a single MAP-specific antigen may not be recognized in all infected cattle.
The Examiner also notes that MPEP 2144 IV teaches: The reason or motivation to modify the reference may often suggest what the inventor has done, but for a different purpose or to solve a different problem. It is not necessary that the prior art suggest the combination to achieve the same advantage or result discovered by applicant. See, e.g., In re Kahn, 441 F.3d 977, 987, 78 USPQ2d 1329, 1336 (Fed. Cir. 2006) (motivation question arises in the context of the general problem confronting the inventor rather than the specific problem solved by the invention); Cross Med. Prods., Inc. v. Medtronic Sofamor Danek, Inc., 424 F.3d 1293, 1323, 76 USPQ2d 1662, 1685 (Fed. Cir. 2005) ("One of ordinary skill in the art need not see the identical problem addressed in a prior art reference to be motivated to apply its teachings."); In re Linter, 458 F.2d 1013, 173 USPQ 560 (CCPA 1972).
Obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596..
c. In response to Applicant’s argument that none of the cited prior art references either individually or in combination teach or suggest the configuration;
As was stated above, the instant rejection is a 103 rejection based on the combination of references.
Secondly, all of the cited references teach the use of purified recombinant MAP derived antigens and the use of ELISA.
The Examiner notes that an enzyme-linked immunosorbent assay (ELISA) relies on the specific binding between an antigen and an antibody in order to detect and quantify target substances in a sample. In these assays, antigens are coated/immobilized on a solid surface and used to capture antibodies.
APPLICANT’S ARGUMENT TWO: Applicant maintains that antigen Selection in Mycobacterial Diagnostics Is Highly Unpredictable. Applicant argues that Li expressly describes high-throughput screening of recombinant MAP proteins to identify candidate antigens, underscoring that antigen suitability cannot be predicted a priori. Applicant argues that Mutharia identifies multiple antigens reactive with infected sera without ranking, preference, or suggestion that any particular antigen should be combined with another. Applicant argues that Willemsen similarly evaluates antibody reactivity to individual antigens, without any teaching or suggestion of combinatorial use.
Applicant maintains that No cited prior art reference teaches or suggests immobilization of purified recombinant MAP1569 with MAP2609 on a solid support for antibody detection, NOR does any cited prior art reference report performance characteristics for this particular pair, such as improved sensitivity or specificity for subclinical infection. Applicant argues that in unpredictable biological diagnostics, combining known components does NOT render outcomes predictable absent guidance. Applicant cites In re Cyclobenzaprine, 676 F.3d 1063, 1070-71 (Fed. Cir. 2012) (no reasonable expectation of success where the prior art gave no indication of which parameters were critical); Leo Pharm. Prods. v. Rea, 726 F.3d 1346, 1356-57 (Fed. Cir. 2013).
Applicant argues that the instant specification reports superior diagnostic performance for the MAP1569 + MAP2609 combination, including detection of subclinical infection (Figures 8C-14); which constitute unexpected results that rebut any prima facie case of obviousness. In re Soni, 54 F.3d 746, 750-51 (Fed. Cir. 1995); MPEP § 2145. Applicant argues that even if a motivation to combine were assumed, the cited prior art references provides NO reasonable expectation of success.
Applicant argues that the solid-support immobilization requirement is a critical implementation detail NOT taught or suggested by the cited prior art references. Applicant argues that a rejection cannot fill a missing claim element with conjecture or general knowledge. Applicant argues that the cited prior art does NOT disclose or suggest immobilization of recombinant MAP1569 and MAP2609 on a single solid support.
Applicant maintains that immobilization fundamentally alters antigen presentation and antibody binding behavior. Applicant submits that the specification provides experimental data demonstrating significantly improved sensitivity and specificity, particularly for subclinical MAP infection. Applicant argues that these results constitute compelling objective evidence of non-obviousness under Graham V. John Deere, 383 U.S. 1 (1966).
Applicant states that Fig. 8C; Table 5 from the instant specification demonstrates that the combined use of MAP1569 and MAP2609, as part of immobilized antigen configurations, provides materially improved diagnostic performance compared to the use of individual antigens alone. In particular, at the M+2SD cutoff, antigen combinations that include both MAP1569 and MAP2609 exhibit substantially higher sensitivity while maintaining high specificity (≥96.7%), whereas individual antigens show markedly lower sensitivity (often ≤48.3%) under the same conditions.
Applicant maintains that the specification further shows that individual MAP antigens are insufficient on their own to reliably detect subclinical infection, underscoring the importance of combining specific antigens to achieve clinically meaningful performance. Applicant argues that nothing in the prior art provides guidance that MAP1569 and MAP2609, when immobilized and used together, would yield this level of improved sensitivity and specificity, particularly for subclinical MAP infection. The observed enhancement therefore constitutes objective evidence of non-obviousness under In re Soni. Applicant argues that the superior diagnostic performance of the recombinant MAP1569 + MAP2609 combination, as demonstrated in Figures 8C-14 of the specification, was unforeseen and contradicts the expectations set by the cited art. Under In re Soni, 54 F.3d 746, 751 (Fed. Cir. 1995), unexpected results alone can overcome a prima facie case of obviousness. The data of the present application directly rebuts the Office's assumption that combining known MAP antigens would yield predictable results.
Applicant’s arguments have been fully considered but are not found persuasive for the following reasons:
a. The Examiner disagrees with Applicant’s assessment regarding the cited prior art and the unpredictability of antigen selection in mycobacterial diagnostics. The cited references clearly teach MAP derived antigens that detect antibodies indicative of MAP infection.
b. Regarding Applicant’s argument that solid-support immobilization requirement is a critical implementation detail NOT taught or suggested by the cited prior art references;
The cited references clearly teach ELISA, which involves solid-support immobilization.
c. Regarding Applicant’s argument that No cited prior art reference teaches or suggests immobilization of purified recombinant MAP1569 with MAP2609 on a solid support for antibody detection;
As was stated above, the instant rejection is a 103 rejection based on the combination of references. Mutharia teaches MAP1569 and Willemsen teaches MAP2609 to detect antibodies indicative of MAP infection.
The Examiner notes that multiplex bead-based immunoassay allows the ability to immobilize more than one antigen on a solid support. The Examiner notes that only instant claims 13, 20 and 31 recite multiplex bead-based immunoassay. These claims were rejected in view the Despres et al. reference, which teaches multiplex bead-based immunoassay.
d. Regarding Applicant’s arguments that the superior diagnostic performance of the recombinant MAP1569 + MAP2609 combination was unforeseen and contradicts the expectations set by the cited art., that unexpected results alone can overcome a prima facie case of obviousness, that the specification further shows that individual MAP antigens are insufficient on their own to reliably detect subclinical infection and that nothing in the prior art provides guidance that MAP1569 and MAP2609, when immobilized and used together, would yield this level of improved sensitivity and specificity, particularly for subclinical MAP infection;
The Examiner notes the following:
The Examiner does not see a dual combination of MPA1569 + MAP2609 in the sections discussed by Applicant.
The Examiner sees wherein Table 5 teaches the combination of MAP1272c, MAP1569, MPA2942c and MAP2609 OR the combination of MAP1272c, MAP1569, MPA2942c, MAP2609, MAP2121c and MAP1201c +2942c. The Examiner notes that the description for FIG. 8C teaches “..sensitivity and specificity with individual MAP recombinant protein and combined 4 proteins at M+2SD cutoff.
Thus, Applicant’s arguments of unexpected results and the dual combination of MAP1569 + MAP2609 are not commensurate in scope with the data taught in the Examples.
The Examiner submits that even if the instant specification taught a combination of MPA1569 + MAP2609, there is no evidence of unexpected results.
This is because Mutharia et al. teach four protein antigens MAP0196c, MAP0471, MAP1981 and MAP1569 were identified that reacted with 35 serum samples from MAP-infected cows ranging from low shedders to high shedders AND Willemsen et al. teach that MAP2609, MAP2942c and MAP0210c were shown to be recognized by antibodies from sera of subclinical infected cattle. In addition, both references teach the necessity of using multiple recombinant antigens when establishing an ELISA for diagnostic purposes.
APPLICANT’S ARGUMENT THREE: Applicant argues that the diagnostic-guided treatment is not obvious. Applicant argues that Click teaches administration of Dietzia but does NOT disclose the claimed diagnostic method, the use of purified recombinant MAP1569 and MAP2609, or solid-support antigen immobilization. Applicant submits that Claim 22 expressly ties the diagnostic step (detection using immobilized purified recombinant MAP1569 + MAP2609) to a MAP-targeted therapeutic intervention. Applicant argues that the "diagnose-and-treat" nexus is NOT taught or suggested by Willemsen, Mutharia, and/or Click in combination and weighs strongly against obviousness. Applicant argues that the Office's reliance on secondary references such as Speer and Després does NOT cure the deficiencies of the primary references. Applicant argues that at most, these references describe generic assay formats or treatment approaches that presuppose the existence of a suitable diagnostic antigen configuration, which is precisely what is missing from the art..
Applicant’s arguments have been fully considered but are not found persuasive for the following reasons:
a. The Examiner has already explained how the combination of Mutharia, Willemsen and Li teach the claimed diagnostic method that uses purified recombinant MAP1569 and MAP2609 and solid-support antigen immobilization to detect antibodies indicative of infection with MAP in samples obtained from animals and detecting antibodies which are associated with MAP in a biological samples.
The combination of Mutharia, Willemsen and Li do not teach administering a MAP-targeted pharmaceutical composition to the animal.
Click teaches Johne's disease as a chronic debilitating disease in ruminant animals caused by mycobacterium avium subspecies paratuberculosis (MAP). Click teaches there are no preventive therapies or curative therapies for paratuberculosis. Click teaches administering Dietzia (gram-positive bacteria) to treat cattle infected with MAP. Click teaches oral treatment with viable Dietzia effectively controlled diarrhea in Stage IV animals although daily treatment was required to maintain this status.
b. Additionally, the Examiner notes that the Examples from the instant application fail to teach administering any type of pharmaceutical composition to reduce the number of MAP bacteria in the intestinal system of the subject.
The scientific reasoning and evidence as whole indicates that the rejection should be maintained.
1a. Claims 13, 14, 20 and 21 remain rejected under 35 U.S.C. 103 as being unpatentable over Mutharia et al. in view of Willemsen et al. and Li et al., as applied to claim 1 above, and further in view of Speer et al. (US 2007/0054334; published 3/8/07) and Despres et al. (US 2013/0309747; published Nov, 21, 2013).
The basis for this rejection is set forth at page 12 and pages 16-17 of the previous Office Action (03 November 2025).
Applicant incorporates their response to the above rejection under 35 U.S.C. 103 as being unpatentable over Mutharia et al. in view of Willemsen et al. and Li et al., in response to the instant rejection.
Applicant's arguments have been fully considered but are not found persuasive for the reasons discussed above and reasons of record.
Despres et al. teach multiplex bead-based immunoassay to detect antibodies in biological fluids. Despres et al. teach that antigen-coated microspheres as capture reagents for specific antibodies. Despres teaches in the context of the invention, a multiplex bead-based immunoassay was developed for rapid and simultaneous detection of antibodies (para 0406).
Speer et al. teach taking samples from animals and exposing the sample to an antigen in order to detect antibodies. Speers et al. teach that the antibody-free surface antigen binding can be determined by flow cytometry (para 0050) .
It would have been oblivious for one of ordinary skill in the art before the effective filling date to modify a method of detecting antibodies indicative of infection with MAP or detecting antibodies which are associated with MAP in a biological sample comprising detecting antibodies in a biological sample, using MAP derived antigens MAP1569, MAP1201c, MAP3531c, and MAP4143, MAP2609, MAP2942c, MAP1272c and MAP2121c, as taught by Mutharia, Willemsen and Li et al., wherein the employed assays are multiplex bead-based immunoassay and flow cytometry, as taught by Despres et al. and Speer et al., respectively. One of ordinary skill in the art before the effective filing date, would have been motivated to make such modifications and expect success because multiplex bead- based immunoassay allows for rapid and simultaneous detection of antibodies. Flow cytometry allows one to analyze antibody-antigen binding
The scientific reasoning and evidence as whole indicates that the rejection should be maintained.
1b. Claim 15 remains rejected under 35 U.S.C. 103 as being unpatentable over Mutharia et al. in view of Willemsen et al. and Li et al., as applied to claim 1 above, and further in view of Click (Virulence, 2:2, 131-143, 2011). The basis for this rejection is set forth at pages 12-13 of the previous Office Action (03 November 2025).
Applicant incorporates their response to the above rejection under 35 U.S.C. 103 as being unpatentable over Mutharia et al. in view of Willemsen et al. and Li et al., in response to the instant rejection.
Applicant's arguments have been fully considered but are not found persuasive for the reasons discussed above and reasons of record. The scientific reasoning and evidence as whole indicates that the rejection should be maintained.
2. Claims 22-30 remain rejected under 35 U.S.C. 103 as being unpatentable over Willemsen et al. (Reference of record) in view of Mutharia et al. (Reference of record) and Click (Reference of record; Virulence, 2:2, 131-143, 2011).
The basis for this rejection is set forth at pages 18-20 of the previous Office Action (03 November 2025).
Applicant incorporates their response to the above rejection under 35 U.S.C. 103 as being unpatentable over Mutharia et al. in view of Willemsen et al. and Li et al., in response to the instant rejection.
Applicant's arguments have been fully considered but are not found persuasive for the reasons discussed above and reasons of record. The scientific reasoning and evidence as whole indicates that the rejection should be maintained.
2a. Claims 23, 31 and 32 remain rejected under 35 U.S.C. 103 as being unpatentable over Willemsen et al. in view of Mutharia et al. and Click, as applied to claim 22 above, and further in view of Li et al. (Reference of record), Speer et al. (Reference of record), and Despres et al. (Reference of record).
The basis for this rejection is set forth at pages 20-22 of the previous Office Action (03 November 2025).
Applicant incorporates their response to the above rejection under 35 U.S.C. 103 as being unpatentable over Mutharia et al. in view of Willemsen et al. and Li et al., in response to the instant rejection.
Applicant's arguments have been fully considered but are not found persuasive for the reasons discussed above and reasons of record. The scientific reasoning and evidence as whole indicates that the rejection should be maintained.
NEW CLAIM REJECTIONS/OBJECTIONS
Claim Rejections - 35 USC § 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 25 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 25 recites the limitation "..wherein the biomarker is an antibody..". Claim 25 depends from claim 22. There is insufficient antecedent basis for the limitation ”biomarker” in the claim. Amending claim 25 to recite “..wherein the antibody is an antibody..” would obviate this rejection.
ART OF RECORD
The art made of record is considered pertinent to Applicant's disclosure as it defines the general state of the art.
Gastaldelli et al. teach that serology is an important tool for Johne's disease (JD) control and that the Luminex suspension array allows the simultaneous detection of antibodies against multiple antigen targets. Gastaldelli et al. teach that they optimized the test with 3 recombinant proteins (MAP0210c, MAP2942, MAP2609), coupling each antigen with a bead set and modifying the standard protocol. Gastaldelli et al. teach that they analyzed 737 sera (510 negative and 227 positive). Gastaldelli et al. teach the comparison with a commercial ELISA showed good agreement (23.8 vs 27.3%). Gastaldelli et al. teach that they have standardized a JD-Luminex serological assay for cattle, with comparable performance to current ELISAs that can be easily implemented with additional antigens.
Gastaldelli et al. (JD-Luminex: detection of antibodies against multiple antigens of Mycobacterium avium subsp. paratuberculosis by means of liquid phase arrays. ABSTRACT. XVII Congresso Nazionale S.I.Di.L.V., Pacengo di Lazise (VR), Italia,
28-30 September 2016 (2016), 55 p., 2 refs. Published by: Societa Italiana di Diagnostica di Laboratorio Veterinaria (SIDiLV), Parma Conference: XVII Congresso Nazionale S.I.Di.L.V., Pacengo di Lazise (VR), Italy, 28-30 September 2016).
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to REGINA M DEBERRY whose telephone number is (571)272-0882. The examiner can normally be reached M-F 9:00-6:30 pm (alt Fri).
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/R.M.D/Examiner, Art Unit 1647 6/9/2026
/BRIDGET E BUNNER/Primary Examiner, Art Unit 1647
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