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 .
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 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.
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 06/23/2026 has been entered.
Status of Claims
Claims 1, 6-7, 9, 13-17, 19 and 21 are pending. Claims 13-14 are withdrawn. Claims 1, 6-7, 9, 15-17, 19 and 21 are currently under examination.
Withdrawn Rejections
In light of the amendments, the 35 U.S.C. 112(a), enablement, rejection over claim 21 is hereby withdrawn.
New Rejection
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.
Claims 1, 6-7, 9, 15-17, 19 and 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 applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
The amended claims 1 and 21 recite the limitation of “monoclonal antibody specifically binds to alkaline-treated capsid polypeptide” is unclear to the metes and bounds of the claimed monoclonal structures. Based from the written description below, it is unclear to an ordinary artisan on how to distinguish structures of monoclonal antibodies that specifically bind to alkaline-treated capsid polypeptide from monoclonal antibodies that do not bind to alkaline-treated capsid polypeptide (denatured). Thus, what are the structures to establish the function of a monoclonal antibody that specifically binds to alkaline-treated capsid polypeptide?
Maintained Rejections
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1, 6-7, 9, 15-17, 19 and 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of an application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient.” MPEP § 2163. While all of the factors have been considered, a sufficient amount for a prima facie case are discussed below.
Further, to provide evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include: a) the scope of the invention; b) actual reduction to practice; c) disclosure of drawings or structural chemical formulas; d) relevant identifying characteristics including complete structure, partial structure, physical and/or chemical properties, and structure/function correlation; e) method of making the claimed compounds; f) level of skill and knowledge in the art; and g) predictability in the art.
Meanwhile, claims 1 and 21 are drawn to a method for detecting a capsid polypeptide of a non-enveloped virus of the family Parvoviridae in a sample from a subject in a sandwich immunoassay comprising contacting the sample with a base that comprises incubating said sample at a pH of at least 10.5 and at most 14; neutralizing the sample contacted with the base to a pH between 6 to 9 before or during detecting said capsid polypeptide; and detecting the capsid polypeptide of said virus in said sample by using with at least one monoclonal antibody that specifically binds to alkaline-treated capsid polypeptide.
These claims, as a whole, are generic to any monoclonal antibody for alkaline-treated capsid polypeptide or any detecting step for capsid polypeptides. Implicit in the claims is that such sandwich immunoassay must possess certain functional characteristics or explicitly any detecting step will capture said capsid polypeptides of the sample; namely, the ability to detect and/or binding to the denatured capsid polypeptides in the sample. Also note that the sandwich immunoassay is recited in the preamble and is not limited/connected to step (c). Thus, the monoclonal antibody directed to the sandwich immunoassay may be prior to step (a) and also incubated at high alkaline pH.
The specification discloses that previously immunological diagnosis of Parvovirus B19 in blood samples was used with acidic pretreatment, aimed at disassembling viral particles in order to increase sensitivity of the assay. However, acid treatment causes a reversible denaturation, allowing at least partial re-assembly of viral particles. Moreover, potentially confounding immunoglobulins from the blood sample may renature as well; and thus, are not effectively removed and the chaotropic salt may disturb the detection reaction and, if removed, may allow renaturation of capsids and confounders (see page 2, lines 6-15, as filed specification dated 05/05/2021). Thus, the specification has disclosed that when using harsh conditions to pretreat the sample certain unpredictable conditions may occur and incubating at high pH may be irreversible for viral proteins. Furthermore, the specification discloses only certain screened monoclonal Parvovirus B19 capsid antibodies would bind to denatured capsid polypeptides in a sample (see Table 1, after pretreated with high pH). Table 1 discloses that monoclonal Parvovirus B19 capsid antibodies with 100% binding to native capsid polypeptides had to be screened for alkaline-treated capsid polypeptides due to the denaturation of capsid polypeptides after the pretreatment at high pH levels (i.e., 2.053, 2.073, 2.077 antibodies do not recognize the capsid polypeptides). Meanwhile, Table 2 does not provide any information on which antibodies were used to detect the denatured capsid polypeptides.
However, the specification fails to provide a representative number of polyclonal and monoclonal species for the claimed generic detection of having the desired binding properties for detecting denatured capsid polypeptides (claims 1 and 21) after pretreatment with extremely high pH conditions. Based on Table 1 of the instant specification, the skilled artisan would not be able to visualize or recognize the identities of members of the genus based on merely examples of specific monoclonal anti-Parvovirus B19 capsid antibodies for detecting denatured capsid polypeptides because the specification has provided evidence that not all monoclonal antibodies bind to denatured capsid polypeptides. In particular, the specification did not use any monoclonal Parvovirus B19 antibody for Table 2 but had to screen and select specific monoclonal Parvovirus B19 capsid antibodies. Thus, it is not possible to conclude that a skilled artisan would be able to visualize and distinguish/separate monoclonal antibodies capable of also binding to alkaline-treated capsid polypeptides without the screening process of specific monoclonal antibodies.
Protein chemistry is unpredictable. In particular, the specification discloses a prescreening for monoclonal antibodies in (see (c-d) of pages 27 and 28, as filed dated 05/05/2021). The pre-screening process has selected monoclonal antibodies that are 100% reactive to native VLP. However, Table 1 also shows that when pretreated VLPs were added against the selected antibodies, low binding affinities for certain antibodies such as antibodies of 2.053, 2,073, 2.077 or inconclusive data (-). Even at a small scale of selected monoclonal antibodies that are 100% reactive to native VLP, these antibodies may lack the binding affinity to pretreated basic solution sample. Thus, the specification fails to describe a representative number of species with respect to the claimed generic antigenic properties to detect the capsid polypeptide with the claimed pH treatment.
For example, Matikainen et al. teach that antibodies bound readily to antigen from pH 4 to 9 but had a reduced binding efficiency at more extreme pH conditions (see abstract). Binding was reduced at extreme pH conditions, possibly due to denaturation of antibodies and such denaturation, as well as dissociation of antibody-antigen complexes at extreme pH conditions (see pg. 215, para. 1 of Discussion). (“Effect of pH on Reactivity of Monoclonal Antibodies to Chlamydia”, Journal of Immunological Methods, vol. 75 (1984), pgs. 211-216, of record 892 dated 07/17/2025). Cuellar et al. teach at pH 10 the capsids lost their stability and were irreversibly destroyed after one single indentation (“Size and mechanical stability of norovirus capsids depend on pH: a nanoindentation study”, Journal of General Virology, vol. 91, issue 10, published 01/10/2010, only Abstract).
As stated in the prior art, the nature and integrity of proteins (i.e., antibody and/or capsid polypeptide) are impacted by high pH conditions. In other words, certain structures of these proteins are irreversibly denatured. As evidenced by Table 1 (as disclosed), not all monoclonal antibodies bind to denatured capsid polypeptides after high pH pretreatments. Meanwhile, the specification has not provided enough evidence that (1) an skilled artisan is able to distinguish and separate monoclonal antibodies that bind to high alkaline-treated capsid polypeptide without screening and (2) any generic monoclonal antibody against native parvovirus would be able to detect denatured capsid polypeptide after claimed high pH pretreatment.
In summary, the specification fails to provide adequate written description for the genus of monoclonal antibodies that specifically bind to alkaline-treated capsid polypeptide and the genus of the detecting step in terms of desired functional properties (i.e., detecting the capsid polypeptide of a sample during or after a high pH treatment). Based on the nature of the invention and a disclosure of a small subset of specific monoclonal antibodies, a skilled artisan would not be able to envision the genus of chemical structures for detecting a capsid polypeptide in a sample with a high pH treatment such that certain chemical structures are irreversibly denatured. The person would not be able to predict the outcome of detecting denatured capsid polypeptide without a representative number of species. Therefore, the specification does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
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.
Claims 1, 6-7, 9, 15-17, 19 and 21 are rejected under 35 U.S.C. 103 as being unpatentable over Kumagai et al. (JP2008145181, published 06/26/2008, of record 892 07/17/2025) in view of Yuan et al. (“Canine Parvovirus Capsid Assembly and Differences in Mammalian and Insect Cells”, Virology, vol. 279, pgs. 546-557, published 2001, see IDS submitted on 02/09/2018).
With respect to claims 1, 15, 17 and 21, Kumagai teaches a parvovirus B19 antigen test comprising treating blood sample (see abstract). Kumagai teaches an attempt to increase the sensitivity of the parvovirus B19 antigen test, an immunological measurement method was used and the sample was treated with an acid or denaturing agent to increase the reactivity of the antigen (see para. [0004] of page 4). Kumagai teaches measuring anti-parvo virus IgM antibody in the sample (see abstract). Kumagai teaches the parvovirus B19 has no envelope, single-stranded DNA and structural proteins (VP1 and VP2), which make up the capsid (see para. [0002] of page 1). Hence it would read on the capsid polypeptide is VP1, VP2 or combinations. Kumagi teaches an acid or denaturing agent to increase the reactivity of the antigen (see para. [0004] of para. 4). Kumagai teaches immunological measurement that reacts with human parvovirus B19 antigen after pre-treating the sample with a solution containing guanidine, guanidine salt or a derivative thereof (see pgs. 10 and 15). Kumagai also teaches guanidine hydrochloride dissolved in critic acid/phosphate buffer and pH was adjusted to 5.5 and sodium hydroxide (see para. [0026] of pgs. 36-37). Kumagai teaches detecting using a sandwich immunoassay (see page 8 or para. [0036] of page 52). Kumagi teaches for each sample, mouse monoclonal anti-parvovirus B19 antibodies Mab8 (mouse IgG2b) and Mab10 (mouse IgG1) were used as antibodies (see pg. 17, para. [0014] and pg. 27, para. [0027]). Kumagi teaches preparation of parvovirus antigen-immobilized in reaction solution pH 7.0 buffer solution (see para. [0033] of pg. 47). Kumagai teaches during the ARCHITECTTM assay, the pH is at 7.0 (see bottom of pg. 48). Meanwhile, Kumagi teaches guanidine, quinidine salt, or a derivative thereof added for the sample has a pH range 4.5 to 6.5 (see para. [0012] of pg. 15). Kumagi also teaches physiological measurement results were obtained (see pg. 14, middle of para. 1) and preparation of parvovirus antigen-immobilized microparticles is in solution with pH 7.0 (see pg. 47, bottom of para. [0033]).
Kumagai does not teach contacting the sample with a base comprises incubating the sample at a pH of at least 10.5 and at most 14 and does not explicitly teach neutralizing the sample contacted with the base to a pH between 6 to 9 before or during detecting said capsid polypeptide and wherein denatured polypeptides generated in step (a) are not solubilized by addition of a chaotropic agent.
Yuan teaches examining a capsid polypeptide with the expression of VP1 and VP2 or only VP2 of a non-enveloped virus from the family Parvoviridae (Abstract and Fig. 6). Yuan teaches capsids treated with pH < 3.0 or pH > 11.0 to release VP1 and VP2 monomers, as well as complexes with the sizes of VP dimers, trimers, and pentamers (see pg. 550, right col., para. 1; and Fig 6 C, empty capsid and Fig. 6D). Yuan further teaches that although full capsids released VP1 and VP2 monomers, after low pH treatment, no multimeric forms were seen, whereas after high-pH treatment only small amounts of the trimer were seen (see pg. 550, right col., para. 1 and Fig. 6C). Yuan teaches detecting VP1 or VP2 with rabbit anti-VP1/VP2 antibodies (see Fig. 6, caption and pg. 555, left col., para. 2). Yuan teaches monoclonal antibody (see pg. 554, right col., para. 2).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to have pretreated the parvovirus B19 sandwich immunoassay as taught by Kumagai with a high-pH pretreatment as taught by Yuan because Kumagai recognizes a pH-controlled pretreatment increases the sensitivity of detecting parvovirus B19 polypeptides (VP1 VP2) and Yuan teaches the parvovirus capsids are pretreated with low pH < 3.0 (acid) and high pH > 11.0 (base) to release VP1, VP2, VP3, and trimer subunits (see Fig. 6C). In particular, Yuan teaches multimeric subunits are released and detected with high-pH pretreatment (basic). Thus, the person would have pretreated the sample of Kumagai with high pH to release VP1, VP2, VP3 and multimeric subunits because (1) high-pH conditions effectively release both the monomeric and multimeric subunits and (2) Yuan has established the success of releasing polypeptide subunits with pH-controlled conditions of low pH < 3.0 (acid) and high pH > 11.0 (base) pretreatments prior to immunoassays. Furthermore, the person would have neutralized the sample to pH 6-9 prior to or during detection through buffer solution because Kumagai teaches that the sandwich assays were pretreated at low pH condition and adjusted to detect at around physiological pH for antibody sensitivity in detecting polypeptide subunits.
Additionally, it would have been obvious to the person to have not solubilized the sample with a chaotropic agent because Kumgai and Yuan teach the pH-controlled conditions to release the polypeptide subunits, as pH-controlled conditions disrupt the native protein’s structure to release the subunits.
The person would have reasonably expected success in using high pH-controlled preteatment in Kumagai’s sandwich immunoassay because Kumagai recognizes using pH-controlled pretreatment in immunoassay detection and it has been recognized by Yuan that acidic and basic treatments release VP1 and VP2 structures for immunoassay detection.
With respect to claim 6, Kumagai teaches a parvovirus B19 antigen test comprising treating the sample i.e. blood serum plasma (see abstract and para. [0002] of pg. 2).
With respect to claim 7, Kumagai teaches a preparation of activator solution with sodium hydroxide (see pg. 37, para. [0026]). As stated above, Kumagai does not explicitly teach step (a). Because NaOH has been recognized to control pH conditions for immunoassays and NaOH is a strong base, it would have been obvious to have used the already established NaOH to produce high pH conditions as claimed.
With respect to claim 9, Kumagi teaches incubateing to specifically react the antigen in the sample with the antibody on the microparticle (see pg. 33, para. [0023]). Yuan teaches detecting VP1 or VP2 with rabbit anti-VP1/VP2 antibodies after pH conditions (see Fig. 6, caption and pg. 555, left col., para. 2). However, Kumagi and Yuan do not teach incubating the sample in the presence of the base for at least 2 minutes.
It has long been settled to be no more than routine experimentation for one of ordinary skill in the art to discover an optimum incubation time for a result effective variable in denaturing/dissociating for immunoassay detection. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum of workable ranges by routine experimentation” Application of Aller, 220 F.2d 454, 456, 105 USPQ 233, 235-236 (C.C.P.A. 1955). “No invention is involved in discovering optimum ranges of a process by routine experimentation.” Id. at 458, 105 USPQ at 236-237. The “discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art.” As stated above, Kumagi recognizes pH controlled pretreatment for immunoassay and Yuan teaches an effective basic condition to release VPI and VP2 for immunoassay detection. Thus, it would have been obvious for the person of ordinary skill to discover the optimum effective pretreatment time of at least 2 minutes for releasing capsid polypeptide subunits.
With respect to claim 16, Kumagai teaches a parvovirus B19 antigen test comprising treating the sample i.e. blood serum plasma (see abstract and para. [0002] of pg. 2).
With respect to claim 19, Kumagi does not explicitly teach not removing any polypeptide denatured by said contacting from said sample. Yuan teaches after treated with pH > 11.0 to release VPI and VP2 structures, not removing any polypeptides denatured by said contacting from said sample (see Fig. 6C and caption).
With respect to claim 21, see above in claim 1.
Response to Arguments
Applicant's arguments filed 06/23/2026 have been fully considered but they are not persuasive.
35 U.S.C. 112(a) rejection:
With respect to written description, Applicant argues on pages 8-9, under sections 3-4, that the working examples provide strong demonstrative support for the amended claims. Applicant argues that the claims are directed to a method and not a genus of antibody compositions. The specification demonstrates possession of the claimed method through working examples in Table 2 showing successful detection of Parvovirus B19 capsid polypeptides after alkaline pretreatment and neutralization. Applicant further argues on page 9 that the written description and obviousness positions are internally inconsistent. Applicant argues that the Office relies on unpredictable at extreme pH and that the specification fails to demonstrate that any generic antibody would detect capsid polypeptides after alkaline pretreatment. Yet under obviousness, the office asserts that a person would have had a reasonable expectation of success in combining alkaline pretreatment with Kumagai’s sandwich immunoassay. Applicant also argues page 10 that Matikainen is inapposite because the claim recites the detection occurs at neutral pH of 6-9.
The arguments are not found persuasive for the following reasons. Table 2 is dependent on Table 1. Meanwhile, Table 1 of the instant specification clearly demonstrates that monoclonal antibodies must be screened to determine binding capability after high pH pretreatment for specific Parvovirus species. The specification has only provided Parvovirus B19 capsid polypeptides and a limited examples of monoclonal antibody that is capable of binding to alkaline-treated capsid polypeptide. There is no way to determine monoclonal or polyclonal antibodies directed at other Parvovirus species would be detectable knowing that a small number of specific monoclonal antibodies bind to denatured capsid polypeptides (denatured proteins). Although the enablement rejection has been withdrawn in view of the neutralizing step, the neutralizing step does not necessarily reverse denatured capsid polypeptides. The neutralizing step is for antibodies. Meanwhile, the detection step (c) encompasses generically the ability to bind/detect denatured capsid polypeptides after the high pH pretreatment. Additionally, Table 2 is very limited and does not provide any context to which antibodies are used and does not disclose, for example, that antibody 2.053, 2.073, or 2.077 of Table 1 is used for detecting denatured capsid polypeptides.
Also, the claims are broad in the sandwich immunoassay, as the step (c) of detecting does not necessarily perform the sandwich immunoassay. Because the claim recites “comprising” and the sandwich immunoassay is in the preamble and not connected to the detecting of the capsid polypeptide, the sandwich immunoassay may be performed prior to contacting to the sample with a base of step (a). Thus, the monoclonal antibody may be treated with the base. Thus, the Matikainen is used to provide context of denatured proteins in the presence of a base at a high pH.
With respect to written description and obviousness rejection, Kumagai teaches Parvovirus B19 monoclonal antibodies which have all the chemical structures of the claimed monoclonal antibody. Because the contacting with a base (a) has a wide range in pHs and detecting step (c) are broad, the claim would also read on the ability to detect non-denatured capsid polypeptides and Kumagi’s monoclonal antibodies have all the chemical structures of the recited “monoclonal antibody”.
35 U.S.C.103 rejection:
With respect to the obviousness rejection, Applicant argues pages 12-13 that the office’s reliance on Kumagai’s sodium hydroxide use as supporting the obviousness of alkaline sample pretreatment is incorrect. Applicant further argues that the prior art combination fails to teach the critical neutralization step because Kumagai’s acid pretreatment is inherently self-neutralizing in a buffered system. Applicant argues that Yuan’s Methodology provides no teaching about protein solubility after alkaline treatment for sandwich immunoassay use. Solubility of the antigen is an absolute prerequisite for sandwich immunoassay function. Thus, Kumagai and Yuan fail to provide a complete basis for the claimed method, as the critical discovery that capsid polypeptides uniquely remain soluble after alkaline treatment. Applicant further argues that Kumagai and Yuan address fundamentally different research problems with no motivation to combine. Applicant argues pages 14-15 that the rejection improperly relies on hindsight reconstruction.
The arguments are not found persuasive for the following reasons. With respect to argument (1), Kumagai recognizes that samples were pre-treated by controlling pH condition prior to immunoassay detection (see above or pg. 10 lines 399 and pg. 36, para. [0026]) and measurement results were performed from an Architect assay at physiological pH (i.e., about 7.0). Meanwhile, as previously stated in enablement rejection, the skilled artisan recognizes antibodies/proteins are sensitive to pH conditions to retain their structural integrity for immunoassay detection. The term pretreated is prior to an immunoassay reaction. As stated above, Kumagai teaches the pH was adjusted to 5.5 (see pg. 36, para. [0026]) prior to immunoassay reaction. Adding a buffer to a solution/sample has been well understood in the art as providing a specific pH condition for immunoassay reaction and would read on the phrase “neutralizing”. Therefore, Kumagai’s method embraces and provides a blueprint to perform a pretreatment by controlling pH conditions and the sandwich assay is performed near physiological conditions or in a range that antibodies can perform the reaction, which would read on the neutralizing step (b).
With respect to argument (2), Yuan does teach detecting the released VP1 or VP2 polypeptides subunit with rabbit anti-VP1/VP2 antibodies after pH controlling conditions, i.e., high and low pH treatments (Fig. 6 and pg. 555, left col., para. 2). Even though Yuan does not teach sandwich assay, Yuan and Kumagai both recognize the ability to release and separate the Provovirus capsid polypeptides through pH controlling conditions and detecting capsid polypeptide subunits with antibodies.
With respect to arguments (3)-(5), although Yuan does not explicitly teach sandwich assay for detecting VP1 and VP2, the obviousness rejection is not employing the assay of Yuan (western blot) but rather Yuan recognizes using pH (acidic and basic) conditions to control the release of the polypeptide subunits. Also, western blots and sandwich immunoassays are recognized in the art for immunoassay detections. On a similar note, Kumagai recognizes sandwich immunoassay for detecting the polypeptide subunits through a pH-controlled pretreatment condition, i.e., acidic condition prior to immunoassay detection. When recognized low and high pH conditions release the polypeptide subunits and detectable under immunoassay (i.e., western blot and sandwich immunoassay), it would have been obvious to the person to have utilized the controlled conditions for the purpose of releasing the capsid polypeptide subunits. Therefore, it is not hindsight because Kumagai recognizes a pH-controlled pretreatment condition for releasing and detecting VP1 and VP2 subunits and Yuan teaches that both acidic and basic solutions release VP1 and VP2 for immunoassay detection.
Conclusion
No claim is allowed.
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/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
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