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 .
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.
Priority
Acknowledgment is made of the present application as a proper National Stage (371) entry of PCT Application No. PCT/CA2021/051256, filed 09/10/2021, which claims benefit under 35 U.S.C. 119(e) to provisional application No. 63/163,695, filed 03/19/2021 and 63/076,918, filed 09/10/2020.
Information Disclosure Statement
The information disclosure statement (IDS) filed 08/04/2023 and 02/20/2026 are considered, initialed and are attached hereto.
Claim Objections
Claims 3, 8, 46, 49 and 55 are objected to because of the following informalities:
Claim 3 recites after each exemplary formula, a roman numeral/letter combination for each. It appears that that this is a numbering system, i.e., a numerical listing to indicate each distinct potential formula. Generally, when numbering/providing a numerical list, the number/Roman numeral is provided before the item to which it represents. The incorporation of each inside of parenthesis and following the item it represents is confusing as to whether this is intended as an abbreviation instead of a numerical listing. It is suggested that Applicant amend the claim to list each number/Roman numeral prior to the item/formula it represents, in order to improve clarity of the record.
Claims 8 and 55 recite limitations that refer to Table 1 in the originally filed specification. Where possible, claims are to be complete in themselves. Incorporation by reference to a specific figure or table "is permitted only in exceptional circumstances where there is no practical way to define the invention in words and where it is more concise to incorporate by reference than duplicating a drawing or table into the claim. MPEP 2173.05(s). Applicant should amend the claims to incorporate the information from Table 1 into the claims.
Claim 46 recites 4 steps labeled a-d, however c and d are not recited as steps, rather c. and d. appear to be a “wherein” clause (which further limits/narrows the step b) and a conclusory statement specific to step b. It is suggested that applicant omit “c.” and “d.” in the interest of clarity of the claim.
Claim 49 is objected to for reciting the limitation “the biological sample”, as previously the sample is only referred to in claims as “sample” (not “a biological sample”). While it is understood Applicant is referring to the sample referenced in the previous claim, it is suggested that applicant amend the language at independent claim 46 in order to recite “a biological sample” (and recite “the biological sample throughout) in order to rely on consistent claim language throughout the claims.
Appropriate correction is required.
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 2, 6-8, 14-16 and 42-43 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 2 recites “connected to the SBM or ISBP” in the alternative (see “or”). However, claim 1 specifies that the SBM comprises an ISBP. As a result, it is unclear from the recited language if the SBM and ISBP are one and the same structural component (i.e., the surface binding moiety is the inorganic surface binding peptide), or rather if these are structurally distinct components (i.e., the ISBP is only part of the SBM). Based on Applicant’s originally filed specification and examples, it appears that it is Applicant’s intention that the ISBP is the SBM (for example, gold binding protein is the surface binding moiety of the dual affinity probe), however this unclear from the recited claim language.
Claims 7 and 8 similarly to claim 2 recite “SBM or ISBP” in the alternative form. As a result, the claim language is indefinite for the same reasons as discussed above relative to claim 2.
Claim 42 recites “A method of analyte detection using the dual-affinity probe of claim 1 to analyze a medium for an analyte”. See MPEP 2173.05(q) , attempts to claim a process without setting forth any steps involved in the process generally raises an issue of indefiniteness. In the present case, the claim recites no active method steps to be positively performed which result in detection as claimed. The language is indefinite because it is not clear what steps/elements would or would not be encompassed by the claimed method.
Claim 48 recites the limitation "the subject" in 1. There is insufficient antecedent basis for this limitation in the claim. Claim 48 depends from claim 46, and claim 46 fails to recite “a subject”, as such it is unclear what “subject” the limitation “the subject” is in reference to.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claim(s) 1-3, 6-8, 14, 39, 42-43, 46, 54, 55 and 58 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Park et al., A self-assembled fusion protein-based surface plasmon resonance biosensor for rapid diagnosis of acute respiratory syndrome, 79, (2009), p. 295-301 (referring to hereinafter as Park et al. (2009), IDS entered 08/04/2023).
Park et al. (2009) teach a dual affinity probe for detecting an analyte, the probe comprising a surface binding moiety comprising an inorganic surface binding peptide (gold binding peptides) and a capture element (SARS coronaviral surface antigen), both present on the same polypeptide (a fused protein) (see abstract, and Figure 2, for example).
Regarding claim 2, see the dual affinity probe, the ISBP and the CE are directly linked via an EGFP (enhanced green binding protein, an amino acid sequence/protein).
Regarding claim 3, Park et al. (2009) teach affinity probe is the formula SBM-LI-CE (gold binding peptide-EGFP-capture element).
Regarding claim 5, Park’s CE is an antigen.
Regarding claim 6, Park’s linker is an amino acid linker (i.e., a protein made up of amino acids).
Regarding claims 7 and 8, Park et al. (2009) is teaching ISBP that binds gold (see as cited above, binding peptide, further page 296, col. 1, para 2).
Regarding claim 14, see Park (2009) at page 296, col. 1, para 2, the gold binding peptide comprising triple repeats of particular 14 amino acid sequence able to bind gold (i.e., a gold binding motif).
Regarding claim 39, the preamble of the claim recites that the invention is a “system for detection of an analyte of known sequence”, the system comprising the dual affinity probe (no other limitations/elements recited. It appears, as claimed, the dual affinity probe is tantamount with the terminology “system”. “System” as recited at the preamble adds no additional structural component/feature/element to the claimed probe. As a result, the probe of Park also anticipates the claim.
Claim 42 recites a method of analyte detection “using the dual affinity probe of claim 1 to analyte a medium for an analyte”, the claim fails to recite any particular active method steps to be performed beyond merely “using” the probe. Park et al. (2009) is teaching “using” their dual affinity probe to detect an analyte in a medium (see for example, Figure 2, (c), page 298, col. 1, para 1, page 297, col. 1, para 3, antibody concentration samples).
Regarding claim 43, see Park et al. (2009) cited above, Park teach the analysis performed using SPR.
Regarding claim 46, Park’s method comprising contacting test sample with dual affinity probe under conditions and for time sufficient for analyte to bind the capture element, forming complex, Park’s methods then determining presence of complex indicating analyte in test sample.
Regarding claim 54, see as cited in detail above (e.g., 296, col. 1, para 2 and Figure 2) , the inorganic binding surface binding polypeptide of the surface in Park is a gold surface.
Regarding claim 55, see for example Park et al. (2009) at page 296, col. 1, para 2, referring to citation no. 10 of the references in Park, S. Brown, Nat. Biotechnol. 15 (1997) 269, which is the same as one of the peptides in Applicant’s table 1 (3rd peptide listed):
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Regarding claim 58, see as cited in detail previously above, Park is teaching analysis using SPR.
Claim(s) 1-8, 14, 39, 42-44, 54 and 58 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Ko et al., Directed self-assembly of gold binding polypeptide-protein A fusion proteins for development of gold nanoparticle-based SPR immunosensors, Biosensors and bioelectronics, 24, (2009), p.2592-2597. Ko et al. similarly teach another dual affinity probe comprising an ISBP (gold binding protein), a capture element (anti-Salmonella antibodies), present on the same protein (presented by Ko et al. as a fusion protein, see abstract, Figure 1, and Materials and Methods section).
Regarding claims 2-3, the ISBP and CE connected via an amino acid sequence (protein A as a linker, exhibiting the format ISBP-proteinA-CE formulate Ia as claimed).
Regarding claim 4, the CE of Ko et al. is an organic binding entity specific for analyte, analyte that is a pathogen (pathogenic bacterium).
Regarding claim 5, Ko et al. teach CE that is an antibody.
Regarding claim 6, Ko et al. is teaching linker that is an amino acid linker (protein A composition comprising a sequence of amino acids).
Regarding claim 7, see Ko cited above teaching ISBP that binds gold.
Regarding claims 8 and 14, the ISBP is a binding peptide (gold binding peptide).
Regarding claim 39, the preamble of the claim recites that the invention is a “system for detection of an analyte of known sequence”, the system comprising the dual affinity probe (no other limitations/elements recited. It appears, as claimed, the dual affinity probe is tantamount with the terminology “system”. “System” as recited at the preamble adds no additional structural component/feature/element to the claimed probe. As a result, the probe of Ko et al. also anticipates the claim.
Claim 42 recites a method of analyte detection “using the dual affinity probe of claim 1 to analyte a medium for an analyte”, the claim fails to recite any particular active method steps to be performed beyond merely “using” the probe. Ko et al. (cited above) is teaching “using” their dual affinity probe to detect an analyte in a medium (see for example, page 2592, col. 1, last para, page 2594, end of col. 1, to col. 2, Figure 6).
Regarding claim 43, Ko et al. teach SPR analysis (see e.g., abstract, Figure 1).
Regarding claim 46, Ko et al. teach methods comprising contacting test sample with dual affinity probe as claimed, allowing sufficient conditions/time for binding, detecting presence (page 2594, end of col. 1 to col. 2, GPB-Pro immobilized chips, introducing anti-Salmonella antibodies, introducing various concentrations of S. typhimurium in PBS).
Regarding claim 54, Ko et al. is teaching ISBP that is bold binding protein.
Regarding claim 58, Ko et al. is teaching SPR analysis (see as cited above).
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.
Claim(s) 18 is rejected under 35 U.S.C. 103 as being unpatentable over Ko et al. in view of Park et al., Rapid detection of aflatoxin B1 by a bifunctional protein cross-linker-based surface plasmon resonance biosensor, Food Control, 36, (2014), p. 183-190 (referring to hereinafter as Park et al. (2014)).
Ko et al. teach protein A (protein A genetically fused to GBP for simple, oriented sterically accessible immobilization of antibodies without an additional steps or chemical treatments (page 2593, col. 1, para 2), and a such fails to teach linker comprising protein G (claim 18).
However, see Ko et al., at 2592, col. 1, para 1, Ko teach it is known that protein A or G specifically recognize the Fc portion of antibodies contributing to highly oriented antibody immobilization on chip surfaces.
However, see extremely similar to Ko et al., is Park et al. (2014), Park et al. teach a similar example of a fusion binding protein, however Park et al. demonstrate a GBP genetically fused with protein G to interact with the Fc portion of antibodies (for same purpose as Ko’s use of protein A).
It would have been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the dual affinity probe of Ko et al., comprising GBP-protein A, for GBP-protein G of Park et al. (2014) as a simple substitution of one known Fc binding protein for another, both known and recognized in the art usable for the same purpose in the same type of dual affinity probe (see Ko et al. and Park (2014), both cited in detail above). Further, because each was recognized as usable for the same purpose in the prior art, one having ordinary skill in the art would have had a reasonable expectation of success in modifying to use one for the other.
Claim(s) 6, 12 and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Ko et al. in view of Zareie et al., Assembly of Gold-Binding Proteins for Biomolecular Recognition, Austin Journal of Biosensors & Bioelectronics, 1(1), (2015), (4 pages) and Shen et al. Site-Selective Oriented Immobilization of Antibodies and Conjugates for Immunodiagnostics Development, 116, (2017), p.95-111.
Ko et al. teach a dual affinity probe substantially as claimed. However, Ko et al. teach protein A binding protein as the linker system between the GBP and the antibody, and as such fails to teach linker comprising streptavidin (claims 6 and 12), or CE conjugated with biotin and linker comprising streptavidin (claim 18).
Zareie et al. teach ordered assembly of genetically engineered inorganic binding polypeptides on atomically flat solid surfaces by using gold binding protein (GBP1), specifically Zareie demonstrate ferritin (targeted analyte) assembled onto streptavidin labeled probe conjugated to biotinylated GBP1 (see abstract and figure 3). See specifically, Zareie teach self-assembled GBP1 as a functional molecular erector set by using it with immobilized protein on it (page 3, end of col. 1). The reference demonstrates the ability to link GBP with a biotinylated protein (see Figure 3, biotinylated GBP bound to biotinylated ferritin by way of streptavidin as a linker), see Zareie et al. at page 3, col. 2, para 1, end of paragraph, teach their immobilization technique as highly efficient compared to other immobilization self-assembled techniques used on gold surfaces for biosensor applications immobilizing probe proteins for targets.
See further Shen et al., page 5, section 2.3, paragraph 2, regarding immobilizing antibodies to solid support surfaces, Shen et al. teach it is known in the art that monoclonal antibodies can be immobilized to surfaces via biotin-streptavidin systems.
Alternative to the GBP-protein A binding protein system of Ko et al., it would have been further prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention, to have modified Ko et al. to instead use biotinylated GBP, as in Zareie et al. (in place of the GBP-protein A system of Ko), in order to link biotinylated antibodies via a streptavidin linker, as in Shen et al., for example, as an obvious matter of substituting one art recognized linking system for self-assembly of proteins on a surface for another, and further an obvious matter of applying a known technique to an art recognized system.
In particular, the base system/technique of providing oriented capture probe on a solid support surface was known in the prior art, see for example Ko et al. (and also Zareie, both teaching techniques for assembly of protein on solid support surface for biosensing purposes). The prior art further recognized the technique of using biotin-streptavidin binding to immobilized protein to solid support surfaces in an oriented/self-assembled manner (see for example Zareie, similar to Ko et al., differing merely in the type of linkage which links GBP to the protein, both resulting in assembly on a solid support surface for binding). Further, in addition to it being recognized in the prior art that self-assembled GBP1 was usable as a functional molecular erector set by using it with immobilized protein, it was similarly recognized in the prior art that streptavidin-biotin binding was a known a way of immobilizing antibodies to solid support surfaces (Shen et al.). One having ordinary skill in the art would have found it obvious to have to have relied on the technique of using streptavidin as a linker to assemble biotinylated antibodies by way of biotinylated GBP on the gold surface solid support surface for biosensing as in Ko et al. given that the modification is merely to the type of linkage employed to attach the GBP and the antibody/protein.
Further, given that both forms of linkage were recognized in the prior art as suitable for self-assembly at a gold solid surface support, the ordinarily skilled artisan would have a reasonable expectation of success.
Claim(s) 8, 14, 16 and 30 are rejected under 35 U.S.C. 103 as being unpatentable over Ko et al. in view of Masaru et al., JP2008268021-A (English translation obtained via PE2E search, attached).
Ko et al. teach a dual affinity probe substantially as claimed, however fails to teach the ISBP consists of an antibody (e.g., claims 8 and 16).
Gold binding peptides and gold specific antibodies were recognized as suitable alternatives of one another in the prior art, see for example Masaru et al. teach material affinity reagents, specifically teaching examples include reagents such as gold binding peptides, or alternatively gold binding antibody fragments (see e.g., translation attached, end of page 12 to page 13).
It would have been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified Ko et al., in order to substitute the gold binding peptide of their affinity probe for a gold binding antibody, as an obvious matter of a simple substitution of one art recognized affinity reagent for gold for another, considering the prior art recognized that either of gold binding peptides or specific gold binding proteins could be used for binding gold material (both are art recognized protein materials known for binding gold). Further one having ordinary skill in the art would have had a reasonable expectation of success using antibody in place of peptide for gold because the prior art recognized either binding reagent as usable for the same purpose (binding gold material), as a result achieved by the modification would be that binding would be unchanged (binding to gold would be achieved).
Regarding claim 30, the combination of the cited art above results in a bispecific antibody (antibody probe that is designed to bind two different antigens simultaneously).
Claim(s) 8, 14-16 and 30 are rejected under 35 U.S.C. 103 as being unpatentable over Ko et al. in view of Masaru et al., JP2008268021-A (English translation obtained via PE2E search, attached) and Watanabe et al., Human Anti-gold Antibodies Biofunctionalization of Gold Nanoparticles and Surfaces with Anti-Gold Antibodies, The Journal of Biological Chemistry, 283(51), (2008), p. 360131-36038.
Ko et al. teach a dual affinity probe substantially as claimed, however fails to teach the ISBP consists of an antibody (e.g., claims 8 and 16), further fails to teach the gold binding motif is VH gold binding motif (claims 14 and 15).
As noted previously above, gold binding peptides and gold specific antibodies were recognized as suitable alternatives of one another in the prior art, see for example Masaru et al. teach material affinity reagents, specifically teaching examples include reagents such as gold binding peptides, or alternatively gold binding antibody fragments (see e.g., translation attached, end of page 12 to page 13).
Further, Watanabe et al. teach the construction of bivalent and bispecific antibodies with the selected anti-gold antibody with high affinity and specificity allowed highly ordered protein patterning and accumulation on a gold surface (page 36031, end of col. 2). Watanabe et al. report an anti-gold antibody product that exhibits strong binding as a result of the interaction of the VH chain with the gold surface (see e.g., Results and Discussion, particularly page 36033, col. 2, para 1).
It would have been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified Ko et al., in order to substitute the gold binding peptide of their affinity probe for a gold binding antibody, as an obvious matter of a simple substitution of one art recognized affinity reagent for gold for another, considering the prior art recognized that either of gold binding peptides or specific gold binding proteins could be used for binding gold material (both are art recognized protein materials known for binding gold).
Further one having ordinary skill in the art would have had a reasonable expectation of success using antibody in place of peptide for gold because the prior art recognized either reagent as usable for the same purpose (binding gold material), as a result achieved by the modification would be that binding would be unchanged (binding to gold would be achieved), see further Watanabe additionally supporting the modification as it was known that gold binding antibodies similarly allow highly ordered protein patterning and accumulation on a gold surface.
Additionally, it would have been prima facie obvious to one having ordinary skill before the effective filing date of the claimed invention to have modified to rely on the specific example gold binding antibody as taught by Watanabe (the antibody having a VH gold binding motif) as an obvious matter of using a known material for its art recognized purpose. In particular one having ordinary skill in the art would have a reasonable expectation of success using a known reagent for its art recognized intended purpose.
Regarding claim 30, the combination of the cited art above results in a bispecific antibody (antibody probe that is designed to bind two different antigens simultaneously).
Claim(s) 33 is rejected under 35 U.S.C. 103 as being unpatentable over Ko et al. in view of Iankov et al., Production and characterization of monoclonal immunoglobulin A antibodies directed against Salmonella H:g,m flagellar antigen, FEMS Immunology and Medical Microbiology, 33, (2002), p.107-113.
Ko et al. teach a dual affinity probe substantially as claimed (see above); however, Ko et al. fails to teach the dual affinity probe as a bispecific immunoglobulin A (see for example, Ko is teaching CE that is an IgG antibody for Salmonella).
However, Iankov et al. teach monoclonal IgA antibodies against Salmonella antigen (see abstract). Iankov et al. teach IgA Mabs stability, along with their specificity make them useful as a tool for serotyping Salmonella strains (abstract, see also page 112, col. 1, para 2 to col. 2).
It would have been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified Ko et al., in order to use IgA antibody as the CE (rather than Ko’s IgG type antibody), as a simple substitution of one art recognized Salmonella antigen binding antibody for another (both recognized by the prior art as having the ability to bind and detect Salmonella bacterium), one further motivated to make the substitution because the IgA antibodies of Iankov et al. are taught as having utility for serotyping strains. One having ordinary skill in the art would have a reasonable expectation of success using the IgA antibodies in place of the IgG resulting in an IgA bispecific dual affinity probe) because the modification would not change the concept of the probe (still dual affinity for both target and a gold surface), the change merely changing one isotype antibody for another.
Claim(s) 48-50 are rejected under 35 U.S.C. 103 as being unpatentable over Ko et al. in view of Kortright et al., US 4,886,742.
Although Ko et al. teach their chip (system comprising dual affinity probe as cited in detail previously above), has utility for detection in real biological samples (page 2596, col. 2, para 2), and in detection of various real targeted analytes of interest, including foodborne pathogens, HIV and disease biomarkers (page 2596, end of col. 2), Ko et al. does not specifically report their methods comprising using the system/probe to detect in a subject that is a mammal or human (claim 48), or in a sample comprising any of those biological samples as recited (see at claim 49, serum, plasma, whole blood, saliva, mucus, sweat, urine or a combination). Ko, although suggesting their probe concept as usable for real targeted analytes including HIV (a virus) does not specifically disclose an example of their probe for this target, rather their example is teaching a pathogen that is a bacterium, and as such fails to teach a pathogen such as a virus, fungi, protozoa, worm or prion (claim 50).
As noted (immediately above), Ko does suggest their dual affinity probe for detection analytes including HIV (a virus).
However, see Kortright et al., antibody reagents are known and available to those of ordinary skill. Kortright is an example teaching use of antibody that recognizes a common antigenic determinant of a group of HIV core antigens (abstract, col. 2, lines 64-66). Kortright teach detection of HIV antigen in biological samples such as plasma or serum (see col. 2, lines 11-26). Kortright teach it is desirable to detect HIV infection (see col. 1, line 31, to col. 2), as it commonly results in AIDS, in order to screen, for example for blood and organ donors, blood products that could spread the disease).
It would have been prima facie obvious to one having ordinary skill in the art to have modified the dual affinity probe/system comprising the probe of Ko et al. in order to target HIV, namely by modifying the CE of the probe to rely on binding reagent such as anti-HIV antigen antibody, as in Kortright et al., in order to detect HIV in a human sample such as plasma or serum (Kortright). Specifically, one would be motivated to try because Ko et al. teach HIV as a specific antigen to which their system is suggested for, one further motivated to detect HIV given that it is desirable to be able to screen blood products (e.g., for blood or organ donation) in order to prevent the spread of the virus. The modification would be a simple substitution of one know binding reagent for another, and one would reasonably expect success because Ko specifically suggest their system for detection of other targets including viral target that is HIV.
Additionally, one having ordinary skill in the art would have a reasonable expectation of success detecting in a sample such as blood or serum because it was known that these are suitable samples containing HIV antigen for detection and because Kortright’s methods supports success detecting HIV in such samples using antibody binding reagents.
Claim(s) 8, 14 and 55 is rejected under 35 U.S.C. 103 as being unpatentable over Ko et al. in view of Park et al. (2009) (cited previously above).
Ko et al. teach a method substantially claimed, including the use of a gold binding peptide as part of the dual affinity probe (see as cited in detail above); however, Ko et al. fails to teach a gold binding peptide selected from any of those listed at the instant Table 1 (claim 55, which also overlaps with alternatively recited limitations recited at claims 8 and 14).
Park et al. (2009) teach a dual affinity probe extremely similar to that presently claimed, see Park et al. (2009) teach a dual affinity probe for detecting an analyte, the probe comprising a surface binding moiety comprising an inorganic surface binding peptide (gold binding peptides) and a capture element (SARS coronaviral surface antigen), both present on the same polypeptide (a fused protein) (see abstract, and Figure 2, for example). Regarding Park (2009), Park teach a gold binding peptide (see at page 296, col. 1, para 2) that is known in the prior art referred to as that of Park’s citation no. 10, S. Brown, Nat. Biotechnol. 15 (1997) 269), which addresses one of the peptides in Applicant’s table 1 (claimed peptide) (see Applicant’s table 1, 3rd peptide listed):
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It would have been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified Ko et al., in order to use the gold binding peptide of Park (Park’s peptide is the same as shown in the present application Table 1, peptide 3) as a simple substitution of one know/art recognized gold binding peptide for another, both known, available and used in the prior art for the same purpose (in dual affinity probes as that taught by Ko and Park). One having ordinary skill in the art would have a reasonable expectation of making the modification since both are known usable for the same purpose (as a component in a dual affinity probe for binding/immobilization/orientation on a gold substrate surface.
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.
Claims 1-3, 5-8, 12, 14-15, 16, 18, 30, 33, 39, 42, 43, 46 , 54-55, and 58 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5-6, 8-9, 11, 12, 17-19, 24-25, 33, 35, 47, 61-65, 72, 91, 131, 161, 192, 193, 207 and 227-230 of copending Application No. 18/181,325. Although the claims at issue are not identical, they are not patentably distinct from each other because:
Copending ‘325 recites a dual affinity probe for detecting an analyte in a sample, comprising a SBM comprising an ISBP, a CE, all part of the same polypeptide (see copending claims 1, 9, 11).
Regarding claim 2, see copending ‘325 recites CE directly or indirectly connected via linker (LI) (see copending claim 2).
Regarding claim 3, see copending claim 3 (2 of the same formulas recited).
Regarding claim 5, copending claim 3 recites CE that is antibody or antigen (see copending claim 5).
Regarding claim 6, see copending claim 6 regarding linker as claimed.
Regarding claims 7, 14 and 54-55, see copending ‘325 at claims 227, 228, 229, 131, , teaching SMB that binds material as claimed.
Regarding claim 8, see copending ‘325 at claim 8 and further claim 9.
Regarding claim 12, see copending claims 11 and 12, regarding AL as claimed.
Regarding claim 15 and 16, see copending ‘325 at claims 1 and 35.
Regarding claim 18, see copending ‘325 at claims 18 and 19.
Regarding claims 30 and 33, see copending ‘325 at claims 34-35 and 230 .
Regarding claim 39, the preamble of the claim recites that the invention is a “system for detection of an analyte of known sequence”, the system comprising the dual affinity probe (no other limitations/elements recited. It appears, as claimed, the dual affinity probe is tantamount with the terminology “system”. “System” as recited at the preamble adds no additional structural component/feature/element to the claimed probe. As a result, the probe and kit (claims cited above, and further copending claim 192 address the claim.
Regarding claim 42, copending ‘325 also recites methods of analyte detection as claimed, see copending claim 47.
Regarding claims 43 and 58, see copending claim 207 describing methods performed via lateral flow.
Regarding claim 46, the methods of the copending application comprise the claimed step of contacting as claimed, determining presence and/or quantity as claimed, see for example copending claims 47 and 207.
Claims 4 and 48-50 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5-6, 8-9, 11, 12, 17-19, 24-25, 33, 35, 47, 61-65, 72, 91, 131, 161, 192, 193, 207 and 227-230 of copending Application No. 18/181,325 in view of Ko et al. and Kortright et al.
Although the claims at issue are not identical, they are not patentably distinct from each other because:
The copending application recites a dual affinity probe and method of using such substantially as claimed, however fails to teach CE specific for analyte that is a pathogen (claim 4); fails to teach the method on a subject that is mammal or human (claim 48), sample comprising serum, plasma, whole blood, saliva, mucus, sweat, urine or a combination (claim 49), pathogen comprising virus, fungi, protozoa, worm, prion (claim 50).
Although see Ko et al. teach a dual affinity probe substantially as claimed, namely Ko et al. teach their chip (system comprising dual affinity probe as cited in detail previously above), has utility for detection in real biological samples (page 2596, col. 2, para 2), and in detection of various real targeted analytes of interest, including foodborne pathogens, HIV and disease biomarkers (page 2596, end of col. 2). Ko, although suggesting their probe concept as usable for real targeted analytes including HIV (a virus) does not specifically disclose an example of their probe specifically used for this target (merely suggests applying it for such).
However, see Kortright et al., antibody reagents are known and available to those of ordinary skill. Kortright is an example teaching use of antibody that recognizes a common antigenic determinant of a group of HIV core antigens (abstract, col. 2, lines 64-66). Kortright teach detection of HIV antigen in biological samples such as plasma or serum (see col. 2, lines 11-26). Kortright teach it is desirable to detect HIV infection (see col. 1, line 31, to col. 2), as it commonly results in AIDS, in order to screen, for example for blood and organ donors, blood products that could spread the disease).
It would have been prima facie obvious to one having ordinary skill in the art to have modified the dual affinity probe/system of the copending application in order to target HIV (as suggested by Ko, Ko teaching this type of probe useful for antigens that are viral, like HIV), namely by modifying the CE of the probe to rely on binding reagent such as anti-HIV antigen antibody, as in Kortright et al., in order to detect HIV in a human sample such as plasma or serum (Kortright). Specifically, one would be motivated to try because Ko et al. (which is teaching a substantially similar dual affinity probe) teach HIV as a specific antigen to which their system is suggested for, one further motivated to detect HIV given that it is desirable to be able to screen blood products (e.g., for blood or organ donation) in order to prevent the spread of the virus (Kortright). The modification would be a simple substitution of one know binding reagent (CE) for another, and one would reasonably expect success because Ko specifically suggest their system (same type as recited by the copending application) for detection of other targets including viral target that is HIV.
Additionally, one having ordinary skill in the art would have a reasonable expectation of success detecting in a sample such as blood or serum because it was known that these are suitable samples containing HIV antigen for detection and because Kortright’s methods supports success detecting HIV in such samples using antibody binding reagents.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Correspondence
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/ELLEN J MARCSISIN/ Primary Examiner, Art Unit 1677