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 .
Claim Status
Claims 1-12 are pending and under consideration.
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.
Claims 1 is rejected under 35 U.S.C. 101, because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. The claims are directed to a judicial exception (natural phenomenon), specifically, the claims are drawn to an indicator molecule AFT-YJFZ01-YJFZ01 which is a natural product. Furthermore, the claims do not integrate said judicial exception into practical application, and the claims do not recite additional elements that amount to significantly more than said judicial exception.
The MPEP Section 2103 through 2106 provides a means of determining whether a particular claim is patent eligible under 35 U.S.C. 101.
Step 1 - Following a determination of the broadest reasonable interpretation of a claim, is the claim drawn to a process, machine, manufacture, or composition of matter? If the answer to this inquiry is “Yes,” the analysis moves on to step 2A.
Step 2A - A two-prong analysis. For prong one, does the claim recite an abstract idea, law of nature, or natural phenomenon? If “Yes,” the analysis proceeds to prong two, which asks whether the claim recites additional elements that integrate the judicial exception into a practical application. If “No,” the analysis moves on to step 2B.
Step 2B - Does the claim recite additional elements that amount to significantly more than the judicial exception? If “No,” the claim is not eligible subject matter under 35 U.S.C. 101.
In the instant case, claim 1 is drawn to composition of matter, so the answer to Step 1 is “Yes.”
With respect to prong one of Step 2A, the answer is “Yes,” because as indicated above, the claims are drawn to a natural phenomenon, specifically, the claims are drawn to an indicator molecule AFT-YJFZ01. As evidenced by instant specification (page 12, line 1-10), indicator molecule AFT-YJFZ01 was purified from cell culture of ten toxigenic strains, and therefore indicator molecule AFT-YJFZ01 is a natural product.
With respect to prong two of Step 2A, the claim does not recite additional elements that integrate the judicial exception into a practical application. Therefore, the answer to prong two of the Step 2A analysis is “No.”
With respect to Step 2B, instant claim 1 does not recite any additional elements that amount to significantly more than the recited judicial exception. Accordingly, the answer to the Step 2B analysis is “No,” and therefore the claims are not eligible subject matter under 35 U.S.C. 101.
A claim that focuses on use of a natural principle must also include additional elements or steps to show that the inventor has practically applied, and added something significant to, the natural principle itself. See Mayo, 101 USPQ2d at 1966. Patents cannot be obtained on subject matter identified by the courts as being exempted from eligibility (i.e., laws of nature, natural phenomenon, and abstract ideas).
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 1-12 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.
Claims 1-12 recites “an indicator molecule AFT-YJFZ01” and “having an amino acid sequence shown in SEQ ID NO: 1”. “An amino acid sequence of SEQ ID NO: X” is interpreted as two amino acid sequence or more in SEQ ID NO: X whereas “the amino acid sequence of SEQ ID NO: X” is interpreted as the full-length sequence of SEQ ID NO: X. Therefore, one of ordinary skill in the art would understand that the claimed molecule AFT-YJFZ01 has amino acid sequence which is a portion of SEQ ID NO: 1. Instant specification did not disclose the full-length sequence of the claimed AFT-YJFZ01 protein. Extensive search showed that the designation “AFT-YJFZ01” is an artificial laboratory designation from Applicant of instant application and is not a designation which is commonly recognized in the art. Because instant specification did not disclose the full-length amino acid sequence of AFT-YJFZ01, one of ordinary skill in the art would not be able to ascertain what protein is AFT-YJFZ01 recited by instant claims. As evidenced by instant sequence listing, SEQ ID NO: 1 has 33,172 amino acid residues. It is hard to believe that SEQ ID NO: 1 is amino acid sequence for a single molecule (i.e. a single polypeptide) as recited by instant claim 1. Instant SEQ ID NO: 1 (33,172 amino acid residues) has molecular weight of about 3,648 kDa (33,172 amino acid residues X 0.11 kDa per average amino acid residue) which is bigger than the prokayotic ribosome (about 2,500 kDa to about 2,700 kDa). However, ribosome is a complex which includes 52 polypeptide chains and 3 RNA molecules. Because instant specification did not disclose the full-length sequence of the claimed AFT-YJFZ01 protein and SEQ ID NO: 1 does not seem to be the full-length amino acid sequence of the claimed AFT-YJFZ01 protein and because the laboratory designation AFT-YJFZ01 is not commonly recognized notation for the specific protein well known in the art, one of ordinary skill in the art would not ascertain what protein is encompassed by the limitation “indicator molecule AFT-YJFZ01” recited by instant claims and what antibody is encompassed by “monoclonal antibody of the indicator molecule AFT-YJFZ01” and “polyclonal antibody of the indicator molecule AFT-YJFZ01” recited by instant claims.
Because it is unclear what protein and what antibody is encompassed by instant claims, proper search cannot be performed. Applicant is advised to provide the full-length sequence of the claimed AFT-YJFZ01 protein molecule and all 6 CDR sequences for the monoclonal antibody of the indicator molecule AFT-YJFZ01 for proper search for the prior art for the claimed antigen AFT-YJFZ01 and the monoclonal antibody of the indicator molecule AFT-YJFZ01.
Claim 2 recites “content” in line 2 and 4. It is unclear whether limitation “content” means “presence” or “concentration”. If Applicant intends to mean concentration by “content”, it is suggested that Applicant amend “content” to “concentration”.
Same reasoning applies to claim 3, claim 5, claim 6, claim 8, claim 10, and claim 12.
Claims dependent from claims 3 and 6 are also rejected because they depend from claims 3 or 6, and therefore they contain same claim limitation.
Claim 3 or 6 recites “based on the method according to claim 2” and therefore it seems that Applicant intend to claim claim 3 or 6 to be dependent from claim 2. The preamble of dependent claim should read “The method according to claim 2”. Therefore, it is unclear whether claim 3 or 6 depends from claim 2 or not. It is unclear whether claim 3 or 6 requires the process steps of “detecting a content of an indicator molecule” and “identifying the toxigenicity of aflatoxigenic fungi” recited by claim 2 because it is unclear whether claim 3 depends from claim 2. If Applicant intend that claim 3 requires only four steps recited by claim 3 or 6, then it is suggested that Applicant delete “based on the method according to claim 2, specifically” to make claim 3 or 6 an independent claim.
Claim 4 recites “taking a mixture of the medium and a culture to be well homogenized”. It is not clear what Applicant intends to mean by this limitation. Does Applicant intend to mean “homogenizing the cultured strain” by “taking a mixture of the medium and a culture to be well homogenized”?
Claim 3, 5-6, 8-9, and 11 contain the trademark/trade name “nanobody”. Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, the trademark/trade name is used to identify/describe single domain antibody and, accordingly, the identification/description is indefinite.
Claim 4 and 7 recite “conventional Czapek medium”. It is unclear how one of ordinary skill in the art can ascertain what type of Czapek medium is conventional and what type is unconventional. It is unclear what makes the medium conventional and how much can it be altered and still be within the scope of the claim.
Claims 5 and 8 recite “conventional phosphate buffer” and “conventional washing solution”. It is unclear how one of ordinary skill in the art can ascertain what phosphate buffer or washing solution are conventional and what are unconventional.
Claims 5 and 8 recite “pH close to be neutral”. It is unclear how close to neutral pH must be.
Claims 5 and 8 recite “appropriately diluting”. It is unclear what kind of “diluting” is considered as “appropriately diluting”.
Claim 7 recites “traditional Chinese medicine”. A person skilled in the art could not determine what is, and is not, included in this term. It is unclear what makes a medicine traditional. It is unclear what makes a medicine a Chinese medicine. If the medicine is used in China as well as other countries, is it still considered as a Chinese medicine?
It is unclear what step of claim 3 or 6 is described by wherein-clause of claims 10 and 12. Wherein-clause is used to describe the claim limitation which is already recited before. Claims 10 and 12 depend from claims 3 and 6, respectively, and wherein-clause of claims 10 and 12 will have to describe one of step (1)-(4) of claim 3 or claim 6. If Applicant intends to recite specific subprocesses of one of steps recited by claim 3 or 6, it is suggested that Applicant recites subprocesses like Applicant did in claim 5.
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 3-12 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.
“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991). See also MPEP 2163.04.
For a claim to a genus, a generic statement that defines a genus of substances by only their functional activity does not provide an adequate written description of the genus. Regents of the University of California v. Eli Lilly, 43 USPQ2d 1398 (CAFC 1997). The recitation of a functional property alone, which must be shared by the members of the genus, is merely descriptive of what the members of the genus must be capable of doing, not of the substance and structure of the members. The Federal Circuit has cautioned that, for claims reciting a genus of antibodies with particular functional properties (e.g., binding to antigen, high affinity, neutralization activity, competing with a reference antibody for binding), “[c]laiming antibodies with specific properties, e.g., an antibody that binds to human TNF-α with A2 specificity, can result in a claim that does not meet written description even if the human TNF-α protein is disclosed because antibodies with those properties have not been adequately described." Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1875, 1877-78 (Fed. Cir. 2011).
“[A] sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Ariad, 598 F.3d at 1350 (quoting Eli Lilly, 119 F.3d at 1568-69). A “representative number of species” means that those species that are adequately described are representative of the entire genus. AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (“The ’128 and ’485 patents, however, only describe species of structurally similar antibodies that were derived from Joe-9. Although the number of the described species appears high quantitatively, the described species are all of the similar type and do not qualitatively represent other types of antibodies encompassed by the genus.”). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species.
The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention. For antibodies, the Federal Circuit has found that possession of a mouse antibody heavy and light chain variable regions provides a structural "stepping stone" to the corresponding chimeric antibody, but not to human antibodies. Centocor, 97 USPQ2d at 1875 (“[T]he application only provides amino acid sequence information (a molecular description of the antibody) for a single mouse variable region, i.e., the variable region that the mouse A2 antibody and the chimeric antibody have in common. However, the mouse variable region sequence does not serve as a stepping stone to identifying a human variable region within the scope of the claims.”). A chimeric antibody shares the full heavy and light chain variable regions with the corresponding mouse antibody; that is, the structure shared between a mouse and chimeric antibody would generally be expected to conserve the antigen binding activity.
Even if a selection procedure is disclosed that was, at the time of the invention, sufficient to enable the skilled artisan to identify antibodies with the recited functional properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad, 94 USPQ2d at 1167; Centocor at 1876 (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”)
Additionally, “An adequate written description must contain enough information about the actual makeup of the claimed products—“a precise definition, such as by structure, formula, chemical name, physical properties, or other properties, of species falling within the genus sufficient to distinguish the genus from other materials,” which may be present in “functional” terminology “when the art has established a correlation between structure and function.” Ariad, 598 F.3d at 1350. But both in this case and in our previous cases, it has been, at the least, hotly disputed that knowledge of the chemical structure of an antigen gives the required kind of structure-identifying information about the corresponding antibodies.” Amgen Inc v. Sanofi 124 USPQ2d 1354, 1361 (Fed. Cir. 2017). “Further, the “newly characterized antigen” test flouts basic legal principles of the written description requirement. Section 112 requires a “written description of the invention.” But this test allows patentees to claim antibodies by describing something that is not the invention, i.e., the antigen. The test thus contradicts the statutory “quid pro quo” of the patent system where “one describes an invention, and, if the law's other requirements are met, one obtains a patent.” Ariad, 598 F.3d at 1345.” Amgen at 1362.
Claim Anaylsis
Instant claims are drawn to a method for identifying an aflatoxin-producing ability of aflatoxin-producing strains of genus Aspergillus, specifically comprising: (1) providing a nanobody or monoclonal antibody of the indicator molecule AFT- YJFZ01 for toxigenicity of aflatoxigenic fungi; (2) providing a polyclonal antibody of the indicator molecule AFT-YJFZ01 for toxigenicity of aflatoxigenic fungi; (3) preparation of a to-be-tested solution of a strain to be identified: culturing the strain to be identified, and diluting to obtain the to-be-tested solution of the strain to be identified; and (4) determination of the aflatoxin-producing ability of the strain to be identified.
It is noted that claim 3 and 6 recite “a nanobody or monoclonal antibody of the indicator molecule AFT- YJFZ01” and “a polyclonal antibody of the indicator molecule AFT-YJFZ01”. Therefore, claims 3 and 6 recite antibodies by the antigen they bind, i.e., the function they have. In this case, the specification does not adequately describe such antibodies as binding a well-characterized antigen as it does not describe representative structures of antibodies that have these functions.
The disclosure of a fully characterized antigen is not sufficient written description of an antibody that binds to that antigen because one could not envision the structure of other antibodies that bind the fully characterized antigen. Therefore, reciting an antibody that binds to a well-characterized antigen is insufficient to describe the genus of antibodies as any species of antibody that binds to an antigen is not representative of other antibodies that bind that antigen as the structure of one antibody that binds an antigen is not representative of the structure of antibodies in general that bind that antigen.
Notably, the Amgen decision holds that the existence of one or a few examples of an antibody having a specific combination of functional characteristics is not sufficient to describe the genus of antibodies having the same functional characteristics. These conclusions are supported by knowledge of antibody structure. It is known in the art that antibodies have a large repertoire of distinct structures and that a huge variety of antibodies can be made to bind to a single antigen.
For example, Lloyd et al (Protein Engineering, Design & Selection, 22:159-168, 2009) teach that hundreds of functional antibody fragments can be isolated from an antibody library that bind to the same antigen wherein these antibodies have distinct heavy and light chain sequences (see, e.g., Discussion). Similarly, Edwards et al (J Mol Biol, 14;334(1):103-118, 2003) found that over 1000 antibodies, all different in amino acid sequence, were generated to a single protein with 568 different amino acid sequences identified for the V(H) CDR3 domains of these antibodies (see Abstract). Furthermore, Goel et al. (The Journal of Immunology (2004) 173(12):7358-7367) showed that three antibodies that bind to the same 12-mer peptide have very different CDRs (see entire document, especially Abstract, Figure 3 and Table 1). Given that hundreds of unique antibody structures may bind a single antigen, the structure of an antibody cannot be predicted from the structure of the antigen, and a single species, or small group of species, cannot define a structure-function relationship so as to be representative of all the antibodies that bind to that antigen.
It is well established in the art that the formation of an intact antigen-binding site in an antibody usually requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs (or hypervariable regions), which provide structure of the antigen binding site and the majority of the contact residues for the binding of the antibody to its target epitope (Malia et al., Proteins 2016; 84;427-434; entire document, especially see Abstract). Malia et al. cocrystallized anti-tau antibody AT8 Fab with a phosphorylated peptide and showed that the interaction interface involves all six CDRs.
As discussed above, it is apparent that all six CDRs that form the antigen binding site of a conventional antibody are needed to describe the particularly identifying structural features of an antibody that correlates with the antibody's ability to bind to the antigen. Absent a description of at least minimal structural features correlating with a functional ability to bind to a particular antigen, which are shared by members of a genus commonly sharing this function, it is submitted that the skilled artisan could not immediately envision, recognize or distinguish antibodies that bind to the indicator molecule AFT-YJFZ01 from those that do not bind to the indicator molecule AFT-YJFZ01. For these reasons, the specification would not reasonably convey to the skilled artisan that Applicant had possession of the claimed invention at the time the application was filed. It is for this reason that claims that recite only antigen AFT-YJFZ01 without specific amino acid sequences for 6 CDRs of the antibody that binds to AFT-YJFZ01 are included in this rejection.
As discussed above, different antibodies that bind to the same antigen need not share any CDR sequences. It is six CDRs of an antibody that define the structure required for the specific binding and each different antibody raised independently to the same antigen will have a different set of six CDRs. Accordingly, defining antibodies by the antigen it binds is insufficient to describe the structure of the genus of antibodies that binds that antigen.
Accordingly, it is submitted that the specification would not reasonably convey to the skilled artisan that Applicant had possession of the claimed invention at the time the application was filed.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 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 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Abad et al (WO2008/070179; PTO-892).
Regarding claim 1, Abad teaches Aspergillus phoenicis protein, SEQ ID 13050 which has 24.4 % identity to the region of residues 15001 to 15200 of SEQ ID NO: 1 (see SCV; result 4 of 15001_15200.rag; see below for the sequence alignment). SEQ ID NO: 1 of instant application has 33,172 amino acid residues. Claim 1 recites an amino acid sequence shown in SEQ ID NO: 1. “An amino acid sequence of SEQ ID NO: X” is interpreted as two amino acid sequence or more in SEQ ID NO: X whereas “the amino acid sequence of SEQ ID NO: X” is interpreted as the full-length sequence of SEQ ID NO: X. As shown below in sequence alignment, Aspergillus phoenicis protein, SEQ ID 13050 has several consecutive amino acid sequences of SEQ ID NO: 1.
result 4 of 15001_15200.rag
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670
925
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Greyscale
Claim(s) 1 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Zhang (Master’s thesis, 2019, Chinese Academy of agricultural Sciences, “Study on the distribution, toxigenicity and infection of Aspergillus Flavus in typical peanut producing areas in China”; 11/28/2023 IDS).
As evidenced by instant specification, the claimed indicator molecule AFT-YJFZ01 was prepared from ten published strains. Paragraph 0052 at page 11-12 of instant specification disclosed “Ten published toxigenic strains, including HLJ-1, HeNZY-2, HuBha-24, JXZS-29-2, LNct-6, GXfc-34, GDZJ-122-2, JSnt-1, HuNdx-7, and HBHA-8-17 were randomly selected from Page 33 of the published literature "Study on Distribution, Toxigenicity and Infection of Aspergillus flavus in Typical Peanut Producing Areas of China"--Master's Thesis of Chinese Academy of Agricultural Sciences, of which the author is Zhang Xing, were separately inoculated into the above-mentioned Czapek medium to be cultured at 280C at 200 rpm/min for 5 days, were homogenized well in a conventional manner to disrupt cells, and were purified by using a conventional protein purification system, protein electrophoresis, immunoaffinity, etc. to obtain the indicator molecule AFT-YJFZ01 for toxigenicity of aflatoxigenic fungi. The test results show that AFT-YJFZ01 can be prepared in10 cultures of the above toxigenic strains. Under the same culture conditions, HBHA-8-17 produces the greatest amount of AFT-YJFZ01 and HLJ-1 produces the least amount of AFT-YJFZ01.” Therefore, the ten published toxigenic strains in the published Master’s thesis contain the claimed indicator molecule AFT-YJFZ01. Thus, the claimed indicator molecule AFT-YJFZ01 is same molecule as what is inside the ten published toxigenic strains and instant claim 1 is anticipated by Zhang.
Conclusion
No claim is allowed.
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/CHEOM-GIL CHEONG/Examiner, Art Unit 1645
/DANIEL E KOLKER/Supervisory Patent Examiner, Art Unit 1645