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 .
Detailed Action
Summary
This is the Non-Final Office Action based on application 17/041816 RCE filed 11/07/2025.
Claims 1-2, 7, 11, 14-15, 20, 25-29, & 31-37 are pending and have been fully considered.
Claims 36-37 were newly added.
Claims 3-6, 8-10, 12-13, 16-19, 21-24, & 30 are cancelled.
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 11/07/2025 has been entered.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
The claimed invention of Claims 11-13, 31-32 & 34-35 are directed to non-statutory subject matter.
Through 101, inquiry analysis:
Is the claim directed to a statutory category of invention?
Independent claims 11-13 are directed to a kit- which reads on the statutory category of a composition of matter for the instant claims, since no device parts are claimed.
Does the claim involve a Judicial Exception?
Yes. For claims 11-13, they are drawn towards a kit. However, as instantly claimed the components of the kit only contain natural compounds (antibodies, lectins, glycol-profile proteins and microperoxidases)- which read on the judicial exception of a product of nature. See MPEP 2106.04 (b).
Claims 11-13 also state that the antibodies are specific for particular diseases (inflammatory disease, prostate cancer, autoimmune disease). The intended use of a device/kit is not read into a claim however, which is what this is read as (that the kit is intended to help diagnose conditions/diseases). The examiner is noting this though because laws of nature/natural correlations (which is the amount of biomarker with the presence of a disease) are judicial exceptions as well.
Claims 11-13 further specify that the lectins are chemically modified with a detectable label, which is a microperoxidase. Microperoxidases are naturally-occuring heme proteins like cytochrome c (see paragraph 0250 of the instant PGPUB specification). Therefore, microperoxidases are natural compounds and the claiming that the lectins are “chemically modified,” with and without specifying if the microperoxidase claimed is some specific type of synthetic or non natural microperoxidase, or if the binding of compounds is done in a way which makes the compounds un-natural, is still considered a natural product.
Has the abstract idea or product of nature or natural correlation been integrated into a particular practical application?
No, there is no integration into a practical application for Claims 11-13. In addition to the judicial exceptions above, it is claimed that the antibody is conjugated to a magnetic carrier, and that a “detectable label,” chemically modifies the natural lectin However, as both magnetic carriers and detectable labels are well understood, routine and conventional in the art--- these do not make the composition markedly different from what is found in nature. Also—there is nothing claimed that practically applies.
Claims 11-13 further specify that the lectins are chemically modified with a detectable label, which is a microperoxidase. Microperoxidases are naturally-occuring heme proteins like cytochrome c (see paragraph 0250 of the instant PGPUB specification). Therefore, microperoxidases are natural compounds and the claiming that the lectins are “chemically modified,” with and without specifying if the microperoxidase claimed is some specific type of synthetic or non natural microperoxidase, or if the binding of compounds is done in a way which makes the compounds un-natural, is still considered a natural product. The natural product is not claimed as markedly different from the components found in nature, and thing is claimed here which adds practical application.
Do the claims recite any elements which are significantly more than the abstract idea or anything which makes the product of nature markedly different?
There are no features instantly claimed which result in significantly more than the judicial exceptions or which make them markedly different shown in Claims 11-13.
Nothing is claimed which changes the claimed natural biomarkers from their natural state or from a binding which occurs naturally (antibody/protein/lectin binding). The biomarkers are not claimed as being mixed with any specific reagents or being detected by any particular method. Nor are there any claimed device parts or structures that could be contained in a kit.
Both magnetic carriers and detectable labels are well understood, routine and conventional in the art--- these do not make the composition markedly different from what is found in nature. Further- antibody/protein/lectin, binding assays are routine and conventional in the art and therefore not be enough to move the claim past the judicial exception of natural correlation or natural compounds.
See MPEP 2106.05(d) which deals with what is considered “Well-Understood, Routine and Conventional” (WURC). The instant claimed subject matter is held WURC especially as it is claimed in a generic manner and at a high level of generality. It is also insignificant extra-solution activity.
For claims 11-13, they are drawn towards a kit. However, as instantly claimed the components of the kit only contain natural compounds (antibodies and lectins) and do not contain any additional elements so overall only what is considered the judicial exception is claimed. The inclusion of “magnetic carrier,” and “Detectable label,” has been addressed above.
Claims 11-13 further specify that the lectins are chemically modified with a detectable label, which is a microperoxidase. Microperoxidases are naturally-occuring heme proteins like cytochrome c (see paragraph 0250 of the instant PGPUB specification). Therefore, microperoxidases are natural compounds and the claiming that the lectins are “chemically modified,” with and without specifying if the microperoxidase claimed is some specific type of synthetic or non natural microperoxidase, or if the binding of compounds is done in a way which makes the compounds un-natural, is still considered a natural product. The natural product is not claimed as markedly different from the components found in nature, and thing is claimed here which adds significantly more.
Nothing in any of the dependent claims change the matters above.
Claims 31-32 & 34-35 state what the lectins are- which basically means that they are attached to a surface (though this isn’t claimed). This is merely explanation of what the natural compound is not enough to move the claim past the judicial exception. Further lectin binding for protein detection is routine and conventional in the art.
Claim Rejections - 35 USC § 112
Claims 1-2, 7, 11, 14-15, 20, 25-29, & 31-37 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.
With respect to Claim 1, from the instant claim wording it is unclear how/ if an actual detection step for the glycoprofile of a protein is actually performed. The preamble is drawn to this, but there is no actual detection or determination of glycoprofile step. Step (c ) of claim 1 is drawn towards “contacting,” “to detect,” however there is no actual detecting claimed and it is unclear how the claim goes from forming some kind of a complex of magnetic carrier, antibody-protein complex, and lectin then leads to detection, or what exactly is being detected. Is it the magnetic carrier that is detected or is it some other entity? Does it’s signal change dependent on the magnetic carrier, antibody-protein, lectin, based on the lectin binding to any or specific glycoproteins in the protein? This is unclear from the claims and requires correction.
Further with respect to Claim 1, it is unclear what exactly is going on with the claimed chain of bound molecules. The parts of the chain as claimed are: 1. magnetic carrier, 2. antibody; 3. protein, and 4. lectin. The only complex, as claimed though is between the antibody and protein, “antibody-protein complex.”
Further into Claim 1, it is claimed that the lectin is “indirectly attached to the magnetic carrier through the antibody-protein complex,” indicating that the lectin binds or at least attaches in some way to the antibody-protein complex, however that it is “not immobilized on a solid surface.” The examiner notes that any particle including the claimed magnetic carrier (which can be particles as seen in instant PGPUB, paragraph 0248), can be considered a solid surface through broadest reasonable interpretation, and further that any kind of attachment can be considered immobilization.
Then, it is further claimed that the “one or more lectins are not immobilized in step ( c),” for which the same thing applies as the above. The examiner notes again that any kind of attachment can be considered immobilization through broadest reasonable interpretation (BRI).
On this note, all the claimed parts of a molecule chain including: 1. magnetic carrier, 2. antibody; 3. protein, and 4. lectin are claimed as being attached or bound or connected in some way to another part of the molecule chain, though the words including “complex,” “mixture,” “attached,” are claimed, and then “not immobilized.” Therefore, it is unclear if the claimed attachments then form further complexes, and it is unclear if the claimed attachments are preventing the claimed attachments or complexes. Further, it is claimed that the lectin is in a mixture with the antibody protein complex and that it is “indirectly,” attached to the magnetic carrier through the “antibody- protein complex,” but it isn’t claimed exactly how or really if the lectin attaches to the protein-antibody complex.
With respect to Claim 36, from the instant claim wording it is unclear how/ if an actual detection step for the glyco-profile of a protein is actually performed. The preamble is drawn to this, but there is no actual detection or determination of glyco-profile step. Step (c ) of claim 36 is drawn towards “contacting,” “to detect,” however there is no actual detecting claimed and it is unclear how the claim goes from forming some kind of a complex of magnetic carrier, antibody-PSA complex, and lectin then leads to detection, or what exactly is being detected. Is it the magnetic carrier that is detected or is it some other entity? Does it’s signal change dependent on the magnetic carrier, antibody-PSA, lectin, based on the lectin binding to any or specific glycoproteins in the PSA? This is unclear from the claims and requires correction.
Further, with respect to Claim 36, when applicant says, “the carrier-antibody-PSA complex,” in step (c ), it is unclear if applicant means the “ magnetic carrier- antibody-PSA complex,” already referred to in the claim. Also, it is claimed that the lectin is indirectly attached to the magnetic carrier, so it is assumed that for the end product that it is part of the claimed complex, but as claimed this isn’t clear since it isn’t claimed as so.
Claims 2, 7, 11, 14-15, 20, 25-29, 31-35 & 37 are rejected by virtue of being dependent on an unclear claim.
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 non-obviousness.
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.
Claims 1-2, 7, 14-15, 20, 25-27, & 29 are rejected under 35 U.S.C. 103 as being obvious by PIERCE in US 20110033875 in view of BRESALIER in US 20180031560.
With respect to Claim 1, PIERCE et al. teach of a method of detecting glycoproteins and cancer specific glycoforms (abstract). PIERCE teaches that the sample can be PSA (paragraph 0112).
PIERCE et al. further teach of contacting a sample comprising said protein with an antibody directed against said protein to form an antibody-protein complex, isolating the antibody-protein complex, and contacting the antibody-protein complex with one or more lectins. PIERCE teaches that the biological sample can first be contacted with a protein antibody to isolate the glycoprotein. The glycoprotein would be isolated by binding to the antibody to form a glycoprotein-antibody complex (as claimed). Then, the isolated glycoprotein (bound to the antibody) is contacted with a lectin (paragraph 0105). This reads on “forms a mixture comprising the antibody protein complex and said one or more lectins,” through broadest reasonable interpretation of the word “mixture.”
PIERCE et al. further teach of doing this in an assay where the antibody and lectin are not immobilized on a solid surface, and wherein said protein is not released from said antibody while performing the method (paragraphs 0096-0107). PIERCE teaches that that antibody can be bound to a magnetic carrier then washed with non-immobilized lectin (paragraph 0194 (reads on antibody/bead “conjugation,”)) (and the beads can be magnetic)( 0070, 0203, 0184).
PIERCE further teaches for the detection--that, “Any convenient method can be used to detect the cancer-specific glycoform. In one embodiment, the cancer-specific glycoform can be detected by contacting the biological sample with a glycan-binding molecule specific for the glycan, under conditions that permit binding of the cancer-specific glycoform of the glycoprotein to the glycan-binding molecule. Exemplary and preferred glycan-binding molecules include a lectin, a glycospecific antibody, a glycospecific aptamer, a glycospecific peptide, and a glycospecific small molecule. In other embodiments, other detection methods can be used, for example mass analysis methods such mass spectrometry,” (Paragraph 0009).
PIERCE further teaches that only “preferably,” and “typically,” a microtiter plate is used- but leaves the teachings open to cases where this is not the case---wherein the lectin is not immobilized on a microtiter plate as instantly claimed (paragraph 0116). For example--- PIERCE teaches of the claimed glycoprotein/antibody and lectin binding through a process that happens during a treatment of a patient (paragraphs 0122-0126).
PIERCE et al. further teach of the instant method being useful to characterize disease states for inflammatory conditions, cancers and autoimmune responses (paragraph 0081, 0108). PIERCE et al. even further teach of comparison to a control (paragraph 0013, 0069, 0076, 0079 among others), and of detected levels that deviate from normal indicate disease (paragraph 0169, 0173, 0185).
PIERCE further teaches methods of detecting or measuring the levels of a protein, including a glycoprotein, are well known in the art and include, without limitation, immunoprecipitation, immunohistochemistry, immunocytochemistry, ELISA, and immunoblotting (i.e. Western blotting). The glycoprotein biomarker can be conveniently detected using a detectably labelled antibody specific for the protein (a protein antibody) (paragraph 0100). Though PIERCE does not specifically use the words “non-immobilized,” immunoprecipitation takes place in solution and therefore would make it obvious to one of ordinary skill that the instant method can be performed “wherein one or more lectins are non-immobilized,” due to the advantage this offers of being a less expensive and equipment cumbersome method without the use of microtiter plates and allowing use of a bigger solution/sample size.
Though it is taught above, if it is not clear that the lectin and antibody are not immobilized, BRESALIER is used to remedy this.
BRESALIER teaches of a method for detection of cancer (abstract). BRESALIER further teaches of the method including obtaining a serum samples, contacting the serum with an antibody to form a complex between a bound molecule and the antibody, and then mixing the complex with a lectin to then perform detection (paragraph 0006). Specifically, the antibody binds to haptoglobin which is a glycoprotein (paragraph 0007) (again this is a mixture through broadest reasonable interpretation).
BRESALIER further teaches that only, “in some cases,” is the antibody immobilized to a surface (paragraph 0016), and only in some embodiments are the lectins immobilized (paragraphs 0109-0110, 0119, 0191).
It would have been obvious to one of ordinary skill in the art to use the lectin and antibody non-immobilized option as is given in BRESALIER in the method of PIERCE due to the advantage this offers for simplicity and decreasing cost as less equipment is needed (BRESALIER, paragraph 0038) and further as BRESALIER points out that in light of their disclosure, one of ordinary skill should appreciate that many changes can be made in the specific embodiments which are disclosed and still obtain similar or like results without departing from the concept, spirit, and scope of the invention (BRESALIER, paragraph 0119).
With respect to Claim 2, PIERCE et al. teach of comparison to a control (paragraph 0013, 0069, 0076, 0079 among others) to monitor deviations.
With respect to Claim 7, PIERCE et al. teach of the lectins being specific for core fucose (paragraph 0011) and other compounds including antennary N-glycans (paragraph 0025 & Table I).
With respect to Claims 14-15, PIERCE et al. teach of using AAL (paragraph 0011, 0034), Con A (paragraph 0032), MAA and SNA, which read on the claimed lectins (paragraph 0074).
With respect to Claim 20, PIERCE et al. teach of tagging with radiolabels or fluorescence-based beads (paragraph 0070) and further that antibodies can be tagged (paragraph 0097).
With respect to Claims 25-27, PIERCE et al. teach of using AAL (paragraph 0011, 0034), Con A (paragraph 0032), MAA and SNA-I, which read on the claimed lectins (paragraph 0074, 0067) and optionally other lectins. This makes the instant claimed lectins obvious.
With respect to Claim 29, PIERCE teaches of using a detectable marker/tag/label (paragraph 0070). PIERCE also teaches of using AAL (paragraph 0011, 0034), Con A (paragraph 0032), MAA and SNA, which read on the claimed lectins (paragraph 0074). This means the sensitivity or specificity would be improved as instantly claimed as they are material properties.
Claims 28, 33 & 36-37 are rejected under 35 U.S.C. 103 as being obvious over PIERCE in US 20110033875 in view of BRESALIER in US 20180031560 and further in view of GIDWANI in US 20210278411.
With respect to Claims 28, PIERCE et al. teach of using a panel (one or more) of lectins including, AAL (paragraph 0011, 0034), Con A (paragraph 0032), MAA and SNA, which read on the claimed lectins (paragraph 0074). PIERCE also teach of the antibody being specific to PSA (0112).
PIERCE and BRESALIER do not teach of the use of MAA-II specifically.
GIDWANI is used to remedy this and teaches of glycoproteins (paragraph 0081), and detecting glycoforms in PSA (paragraph 0004) and further of detecting the MAA II lectin which binds (paragraph 0092-0093). It would have been obvious to use MAA II as is done in GIDWANI in the methods and compositions/kits of PIERCE and BRESALIER due to the advantages GIDWANI offers in improving specificity (GIDWANI, paragraph 0331).
With respect to Claims 33 PIERCE et al. teach of using a panel (one or more) of lectins including, AAL (paragraph 0011, 0034), Con A (paragraph 0032), MAA and SNA, which read on the claimed lectins (paragraph 0074). PIERCE also teach of the antibody being specific to PSA (0112). PIERCE and BRESALIER do not teach of the use of MAA-II specifically.
GIDWANI is used to remedy this and teaches of glycoproteins (paragraph 0081), and detecting glycoforms in PSA (paragraph 0004), and further of detecting the MAA II lectin which binds (paragraph 0092-0093). It would have been obvious to use MAA II as is done in GIDWANI in the methods and compositions/kits of PIERCE and BRESALIER due to the advantages GIDWANI offers in improving specificity (GIDWANI, paragraph 0331).
With respect to Claim 36, PIERCE et al. teach of a method of detecting glycoproteins and cancer specific glycoforms (abstract). PIERCE teaches that the sample can be PSA (paragraph 0112).
PIERCE et al. further teach of contacting a sample comprising said protein with an antibody directed against said protein to form an antibody-protein complex, isolating the antibody-protein complex, and contacting the antibody-protein complex with one or more lectins. PIERCE teaches that the biological sample can first be contacted with a protein antibody to isolate the glycoprotein. The glycoprotein would be isolated by binding to the antibody to form a glycoprotein-antibody complex (as claimed). Then, the isolated glycoprotein (bound to the antibody) is contacted with a lectin (paragraph 0105). This reads on “forms a mixture comprising the antibody protein complex and said one or more lectins,” through broadest reasonable interpretation of the word “mixture.”
PIERCE et al. further teach of doing this in an assay where the antibody and lectin are not immobilized on a solid surface, and wherein said protein is not released from said antibody while performing the method (paragraphs 0096-0107). PIERCE teaches that that antibody can be bound to a magnetic carrier then washed with non-immobilized lectin (paragraph 0194 (reads on antibody/bead “conjugation,”)) (and the beads can be magnetic)( 0070, 0203, 0184).
PIERCE further teaches for the detection--that, “Any convenient method can be used to detect the cancer-specific glycoform. In one embodiment, the cancer-specific glycoform can be detected by contacting the biological sample with a glycan-binding molecule specific for the glycan, under conditions that permit binding of the cancer-specific glycoform of the glycoprotein to the glycan-binding molecule. Exemplary and preferred glycan-binding molecules include a lectin, a glycospecific antibody, a glycospecific aptamer, a glycospecific peptide, and a glycospecific small molecule. In other embodiments, other detection methods can be used, for example mass analysis methods such mass spectrometry,” (Paragraph 0009).
PIERCE further teaches that only “preferably,” and “typically,” a microtiter plate is used- but leaves the teachings open to cases where this is not the case---wherein the lectin is not immobilized on a microtiter plate as instantly claimed (paragraph 0116). For example--- PIERCE teaches of the claimed glycoprotein/antibody and lectin binding through a process that happens during a treatment of a patient (paragraphs 0122-0126).
PIERCE et al. further teach of the instant method being useful to characterize disease states for inflammatory conditions, cancers and autoimmune responses (paragraph 0081, 0108). PIERCE et al. even further teach of comparison to a control (paragraph 0013, 0069, 0076, 0079 among others), and of detected levels that deviate from normal indicate disease (paragraph 0169, 0173, 0185).
PIERCE further teaches methods of detecting or measuring the levels of a protein, including a glycoprotein, are well known in the art and include, without limitation, immunoprecipitation, immunohistochemistry, immunocytochemistry, ELISA, and immunoblotting (i.e. Western blotting). The glycoprotein biomarker can be conveniently detected using a detectably labelled antibody specific for the protein (a protein antibody) (paragraph 0100).
PIERCE et al. teach of using a panel (one or more) of lectins including, AAL (paragraph 0011, 0034), Con A (paragraph 0032), MAA and SNA, which read on the claimed lectins (paragraph 0074). PIERCE also teach of detecting PSA (0112).
Though PIERCE does not specifically use the words “non-immobilized,” immunoprecipitation takes place in solution and therefore would make it obvious to one of ordinary skill that the instant method can be performed “wherein one or more lectins are non-immobilized,” due to the advantage this offers of being a less expensive and equipment cumbersome method without the use of microtiter plates and allowing use of a bigger solution/sample size. Though it is taught above, if it is not clear that the lectin and antibody are not immobilized, BRESALIER is used to remedy this.
BRESALIER teaches of a method for detection of cancer (abstract). BRESALIER further teaches of the method including obtaining a serum samples, contacting the serum with an antibody to form a complex between a bound molecule and the antibody, and then mixing the complex with a lectin to then perform detection (paragraph 0006). Specifically, the antibody binds to haptoglobin which is a glycoprotein (paragraph 0007) (again this is a mixture through broadest reasonable interpretation).
BRESALIER further teaches that only, “in some cases,” is the antibody immobilized to a surface (paragraph 0016), and only in some embodiments are the lectins immobilized (paragraphs 0109-0110, 0119, 0191).
It would have been obvious to one of ordinary skill in the art to use the lectin and antibody non-immobilized option as is given in BRESALIER in the method of PIERCE due to the advantage this offers for simplicity and decreasing cost as less equipment is needed (BRESALIER, paragraph 0038) and further as BRESALIER points out that in light of their disclosure, one of ordinary skill should appreciate that many changes can be made in the specific embodiments which are disclosed and still obtain similar or like results without departing from the concept, spirit, and scope of the invention (BRESALIER, paragraph 0119).
If it is unclear that PIERCE and BRESALIER teach of detecting PSA and the glycoprofile or glycoforms in it, with one of the claimed lectins, GIDWANI is used to remedy this. Further, PIERCE and BRESALIER do not teach of chemically modifying the lectin with a peroxidase.
GIDWANI teaches of a method for diagnostics of cancer (abstract) including detection of glycoproteins (paragraph 0081), and detecting glycoforms in PSA (paragraph 0004), and further using the MAA II lectin which binds (paragraph 0092-0093, Table I). GIDWANI further teaches of chemically modifying the lectin with a peroxidase (paragraph 0226).
GIDWANI further teaches that the methods and compositions/kits improve specificity of detection (GIDWANI, paragraph 0331).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the instant invention to detect PSA and to use MAA II as is done in GIDWANI in the methods and compositions/kits of PIERCE and BRESALIER due to the advantages GIDWANI offers in improving specificity for detection of PSA (GIDWANI, paragraph 0331). Further, it would have been obvious to one of ordinary skill in the art before the effective filing date of the instant invention to label the lectin with a peroxidase as is done in GIDWANI in the methods of PIERCE and BRESALIER due to the advantage this would have in aiding in colorimetric detection (GIDWANI, paragraph 0226).
With respect to Claim 37, PIERCE teaches of the above and further of using ConA and AAL lectin (paragraph 0074). Even further, PIERCE teaches of using a detectable marker/tag/label such as a peroxidase (paragraph 0070, 0039).
BRESALIER also teaches of using peroxidase reporters for lectins (paragraph 0019, 0084, 0087, 0117, 0118, 0164).
Therefore- PIERCE teaches of using one of the claimed lectins chemically modified with peroxidase, but does not teach of the second, which is claimed.
GIDWANI teaches of a method for diagnostics of cancer (abstract) including detection of glycoproteins (paragraph 0081), and detecting glycoforms in PSA (paragraph 0004), and further using the MAA II lectin which binds (paragraph 0092-0093, Table I). GIDWANI further teaches of chemically modifying the lectin with a peroxidase (paragraph 0226)—therefore chemically modifying MAA II lectin with peroxidase reads on the second chemically modified lectin as claimed.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the instant invention to detect PSA and to use MAA II as is done in GIDWANI in the methods and compositions/kits of PIERCE and BRESALIER due to the advantages GIDWANI offers in improving specificity for detection of PSA (GIDWANI, paragraph 0331). Further, it would have been obvious to one of ordinary skill in the art before the effective filing date of the instant invention to label and detect the lectin with a peroxidase as is done in GIDWANI in the methods of PIERCE and BRESALIER due to the advantage this would have in aiding in colorimetric detection (GIDWANI, paragraph 0226).
Claims 11, 31-32, & 34-35 are rejected under 35 U.S.C. 103 as being obvious over PIERCE in US 20110033875 in view of GIDWANI in US 20210278411 and further in view of KUSLICH in AU 2011205230.
With respect to Claim 11, PIERCE et al. teach of the claimed invention as shown above. PIERCE et al. further teach of diagnosing pancreatic cancer and of the invention containing antibodies specific for cancer and also a lectin (paragraph 0009, 0067, 0156-0157, 0187) and further of using IgG (paragraph 0089, 0093, 0194) and further of using ConA and AAL lectin (paragraph 0074). PIERCE teaches of using a detectable marker/tag/label (paragraph 0070). This binding of compounds together can read on the claimed “chemically-modified,” through broadest reasonable interpretation.
PIERCE et al. also teach of the lectins being specific for core fucose (paragraph 0011) and other compounds including antennary N-glycans (paragraph 0025 & Table I), and also teach of binding to a magnetic carrier (paragraph 0184, 0070, 0203).
PIERCE does not call out that that the lectin is associated with PSA antibody or the use of a kit.
GIDWANI et al. is used to remedy this.
GIDWANI teaches of a method for detection of cancer (abstract), and of detecting glycoproteins (paragraph 0081), and further of detecting the MAA II lectin which binds (paragraph 0092-0093), and of detection of specifically PSA glycoforms (paragraph 0004) and detection using a PSA specific antibody in a kit (paragraph 0250), and also of the lectins being modified with peroxidases (paragraph 0226). GIDWANI further teaches of the techniques taught therein improving cancer detection specificity (paragraph 0331). It would have been obvious to one of ordinary skill in the art to use the compounds and techniques of GIDWANI in the methods and kits of PIERCE and BRESALIER due to the advantage they offer in improving specificity (GIDWANI, paragraph 0331).
Further- it is noted that the claimed “wherein,” clause in Claim 11 with respect to supposed improvement,” of sensitivity and specificity are a material property and an intended use of the claimed kit/compounds. Since the claimed compounds in the kit are taught, it would have this material property.
PIERCE and GIDWANI do not teach of the use of a microperoxidsase as claimed.
KUSLICH is used to remedy this and teaches of methods for detection of biomarkers for diseases including cancers (Abstract), including detections of PSA (paragraph 0053), through detection of wherein a binding agent to the biomarker can be a lectin (paragraph 0021), and wherein a detectable label can be bound thereto which can include a microperoxidase (paragraph 0069, 0090).
It would have been obvious to one of ordinary skill in the art prior to the effective filing date of the instant invention to use the detectable label of microperoxidase as is done in KUSLICH in the methods of PIERCE and GIDWANI due to the advantage it offers in altering the fluorescence or chemiluminescence of the substrate (paragraph 0090).
With respect to Claims 31-32, PIERCE et al. teach of using a panel (one or more) of lectins including, AAL (paragraph 0011, 0034), Con A (paragraph 0032), MAA and SNA, which read on the claimed lectins (paragraph 0074). PIERCE also teach of the antibody being specific to PSA (0112).
PIERCE does not teach of the use of MAA-II specifically.
GIDWANI is used to remedy this and teaches of glycoproteins (paragraph 0081), and detecting glycoforms in PSA (paragraph 0004) and further of detecting the MAA II lectin which binds (paragraph 0092-0093). It would have been obvious to use MAA II as is done in GIDWANI in the methods and compositions/kits of PIERCE due to the advantages GIDWANI offers in improving specificity (GIDWANI, paragraph 0331).
With respect to Claims 34-35, PIERCE et al. teach of using a panel (one or more) of lectins including, AAL (paragraph 0011, 0034), Con A (paragraph 0032), MAA and SNA, which read on the claimed lectins (paragraph 0074). PIERCE also teach of the antibody being specific to PSA (0112). PIERCE does not teach of the use of MAA-II specifically.
GIDWANI is used to remedy this and teaches of glycoproteins (paragraph 0081), and detecting glycoforms in PSA (paragraph 0004), and further of detecting the MAA II lectin which binds (paragraph 0092-0093). It would have been obvious to use MAA II as is done in GIDWANI in the methods and compositions/kits of PIERCE due to the advantages GIDWANI offers in improving specificity (GIDWANI, paragraph 0331).
Response to Arguments
Applicant's arguments filed 11/07/2025 have been fully considered but they are not persuasive.
With respect to the 112 rejection, some of them have been overcomes, however the claims are still unclear for the reasons shown above.
The examiner notes that with respect to Claim 1, after further consideration it has been found to be unclear for the reasons shown in the above 112 rejection. It is noted that newly added Claim 39 has far less clarity problems in in than in independent Claim 1, however there are some.
Further, it is noted that amendments have been made to all pending independent Claims. Therefore, the grounds of rejections have changed with respect to these amendments as shown above. Therefore, applicant should see the rejections above and the examiner has not substantially replied to their comments regarding the prior art art and amendments made.
If applicant can clear up the claims for Claims 1 & 39 and the claims that depend therefore, applicant will be much more likely to also overcome the instantly cited prior art.
For the pending kit claims including Claim 11 and those dependent therefrom, if applicant is able to specify in the claims a component which is markedly different from what is found in nature, then they will be much more likely to overcome the 101 rejection.
The examiner notes for Claim 11, that the kit requires, an antibody specific to PSA antigen, a chemically modified lectin, which is chemically modified with a microperoxidase. The kit also requires that the antibody is bound to a magnetic carrier.
The examiner notes that the natural components in this are the antibody, the lectin, and the microperoxidase. Magnetic carriers/particles *could be considered as a product of nature as well. The test for whether components are markedly different or not is whether they have markedly different properties than what is found in nature, for each of combined products of nature. In this claim, the antibody does not have markedly different properties as it binds to the PSA antigen. The lectins do not have markedly different properties as they bind to glycoforms on PSA. The microperoxidase does not have markedly different properties as it binds to lectins. The magnetic carriers also do not have a markedly different characteristic from when magnetic particles are found in nature. Further- applicant has provided no specific argument if they do not think this is the case, other than general argument to this affect.
With respect to the prior art, the examiner notes that applicant agues about the term “immobilized,” and “not immobilized,” in the claim. The examiner notes that this term and the binding of the components in the claim is unclear as shown in the rejection above.
If applicant is able to clear up the claims, then it will be easier to overcome the prior art.
Applicant argues that PIERCE does not teach of the antibody being conjugated to a magnetic carrier, and also of use of non-immobilized lectins. First of all the examiner notes that the exact connections between the claimed components is unclear as shown in the above 112 rejections. Applicant seemingly claims that components are both attached, connected or conjugated to other components, but then also non immobilized. If applicant can clear up the claims to this affect, then the prior art will likely be overcome.
Further with respect to the prior art, applicant argues that the examiner seems to pick from different embodiments in the same reference with respect to PIERCE, and further with respect to the combination of references, that any assertion to that the references can be combined by the examiner is hindsight reasoning. The examiner sees applicant’s point, however as claimed, the rejection is maintained as due to how the claim terms can be interpreted, it is actually unclear what exactly is being claimed.
Further, applicant argues that PIERCE teaches of an assay where the antibody of step is not immobilized on a solid surface, and wherein said protein is not released from said antibody while performing the method (paragraphs 0096-0107). The examiner notes that PIERCE teaches that that antibody can be bound to a magnetic carrier then washed with non-immobilized lectin (paragraph 0194 (reads on antibody/bead “conjugation,”) )( and the beads can be magnetic)( 0070, 0203, 0184).
The examiner further notes that PIERCE further teaches that only “preferably,” and “typically,” a microtiter plate is used- but leaves the teachings open to cases where this is not the case---wherein the lectin is not-immobilized on a microtiter plate as instantly claimed (paragraph 0116). For example--- PIERCE teaches of the claimed glycoprotein/antibody and lectin binding through a process that happens during a treatment of a patient (paragraphs 0122-0126). This language leaves the interpretation of PIERCE open plain and simple to not immobilizing the taught components.
Further, it is noted in response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
Applicant further cites paragraph 0184 of PIERCE and argues that PIERCE teaches the opposite ordering of binding from what is claimed. With respect to this--- while the examiner see this, the examiner points applicant’s attention to paragraph 0194, which is also cited and claims the correct order of binding as claimed. The examiner notes that lectin blot can be done with or without immobilizing lectins (in solution is non-immobilized). The examiner again further notes that the non-immobilization or not to a “solid surface,” as claimed in confusing/unclear as instantly claimed.
Applicant further goes through the PIERCE reference and generally recites all sections of PIERCE that they think contradict the claimed “non-immobilized,” which is claimed. The examiner again notes that the language in PIERCE leaves the interpretation open to other methods than immobilization working for detection. It is suggested that if applicant means something more specific, they should amend it into the claims.
With respect to the BRESALIER reference applicant seemingly argues that the lectins in BRESALIER are not “non- immobilized,” as instantly claimed. Specifically, the examiner notes that BRESALIER teaches that the lectins can be immobilized or non immobilized, since only “in some cases,” is the antibody immobilized to a surface (paragraph 0016), and only in some embodiments are the lectins immobilized (paragraphs 0109-0110, 0119, 0191). So- this makes the instant claims obvious, especially due to broadest reasonable interpretation and in light of the 112 rejections made above.
The examiner further notes, it would have been obvious to one of ordinary skill in the art to use the lectin and antibody non-immobilized option as is given in BRESALIER in the method of PIERCE due to the advantage this offers for simplicity and decreasing cost as less equipment is needed (BRESALIER, paragraph 0038). Applicant argues that this reason for combination only applies to immobilized lectins and antibodies, and not the non-immobilized claimed. With respect to this- again the examiner notes that it is very unclear what applicant means by non-immobilized in the claim. For example, from the instant pgpub specification, it seems that non-immobilized, is just with respect to things like microtiter plates or flat substrates, and non-immobilized can include things like binding to a bead(paragraph 0248). This, binding to a bead, is exactly the same thing, but is considered “immobilized,” by BRESALIER. Therefore, both references seem to teach the same thing, but using different terminology. Therefore, applicant’s argument regarding the reason for combination is not convincing, especially in light of the clarity issues in the claims.
With respect to the kit claims, the examiner notes that a new reference was used and one was taken out to teach of these claims. With respect to the kits claims, applicant further seems to argues that the use of the kit is different in the instant claims versus in the prior art. With respect to this, the examiner note that the use of a kit claim is not limiting, and the kit itself is either a device or composition, and in this case is claimed as only containing compositional components. Therefore, a method of use or its intended result is not limiting. Applicant should see the rejection above for more information.
All claims remain rejected.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to REBECCA M FRITCHMAN whose telephone number is (303)297-4344. The examiner can normally be reached 9:30-4:30 MT Monday-Friday.
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/REBECCA M FRITCHMAN/Primary Examiner, Art Unit 1758
Prosecution Insights