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
Claims 1-18 are pending.
During a preliminary amendment of this application, the applicant, on date 10/14/2025 elected without traverse Group I (claims 1-14 ), drawn to modified ferritin comprising a human ferritin H chain, wherein the human ferritin H chain contains a modifying group covalently bonded specifically to a cysteine residue at position 91 and/or position 103 according to a reference position of a natural human ferritin H chain. Claims 15-18 of election/restriction-office action of date 8/14/2025 is withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected inventions.
The requirement is therefore made FINAL.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 12//7/2022 in compliance with the provisions of 37 CFR 1.97. Accordingly, the examiner has considered the IDS statements.
Claim Rejections
35 USC 112(b) Rejection
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.
Claims 1, 7, 2-14( depend on claim 1) is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claim 1 is rejected for reciting “a cysteine residue at position 91 and/or position 103 according to a reference position of a natural human ferritin H chain”. It is unclear which position 91 and 103 is? Without sequence identifier by a SEQ ID NO: to natural human ferritin H chain, the position NO: 91 and 103 are indefinite. . Correction is required.
Claim 7 is rejected for reciting “amino acid residues at positions 78 to 96 according to a reference position of a natural human ferritin H chain”. It is unclear which position 78-96 is? Without sequence identifier by a SEQ ID NO: to natural human ferritin H chain, the position NOs: 78-96 are indefinite. . Correction is required.
Claim 14 is rejected for reciting “ “internal cavity thereof”. It is unclear which tertiary structure/amino acids are considered as an internal cavity forms an internal cavity.
Claim Rejections, 35 U.S.C 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-14 are rejected under 35 U.S.C. 112(a), as containing 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(s), at the time the application was filed, had possession of the claimed invention.
It is noted that MPEP 2111.01 states that "[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow." modified ferritin comprising a human ferritin H chain, wherein the human ferritin H chain contains a modifying group covalently bonded specifically to a cysteine residue at position 91 and/or position 103 according to a reference position of a natural human ferritin H chain in claim 1 and a protein comprising an amino acid sequence comprising one or several mutations of amino acid residues selected from the group consisting of replacement, deletion, insertion, and addition of amino acid residues in the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 3 and having a 24-mer forming ability in claim 5“ can be genus of natural human ferritin H chain having any structure and modification at position 9/ and /or 103 or any number of modification including position 91 and 103 in claim 5 the sequence having any structure including any number of modifications within SEQ ID NO: 1 or 3..
The Court of Appeals for the Federal Circuit has recently held that a "written description of an invention involving a chemical genus, like a description of a chemical species, 'requires a precise definition, such as by structure, formula [or] chemical name,' of the claimed subject matter sufficient to distinguish it from other materials." University of California v. Eli Lilly and Co., 1997 U.S. App. LEXIS 18221, at *23, quoting Fiers v. Revel, 25 USPQ2d 1601, 1606 (Fed. Cir. 1993). To fully describe a genus of genetic material, which is a chemical compound, applicants must (1) fully describe at least one species of the claimed genus sufficient to represent said genus whereby a skilled artisan, in view of the prior art, could predict the structure of other species encompassed by the claimed genus and (2) identify the common characteristics of the claimed molecules, e.g., structure, physical and/or chemical characteristics, functional characteristics when coupled with a known or disclosed correlation between function and structure, or a combination of these (paraphrased from Enzo Biochemical).University of Rochester v. G.D. Searle & Co. (69 USPQ2d 1886 (2004)) specifically points to the applicability of both Lilly and Enzo Biochemical to methods of using products, wherein said products lack adequate written description. While in University of Rochester v. G.D. Searle & Co. the methods were held to lack written description because not a single example of the product used in the claimed methods was described, the same analysis applies wherein the product, used in the claimed methods, must have adequate written description (see Enzo paraphrased above).
There is no structure-function correlation with regard to the members of the genus of polypeptides having many structures genus of natural human ferritin H chain having any structure and modification at position 9/ and /or 103 or any number of modification including position 91 and 103 in claim 5 the sequence having any structure including any number of modifications within SEQ ID NO: 1 or 3. Therefore one of skill in the art would not recognize from the disclosure that applicants were in possession of the claimed invention.
The genus of polypeptides having required in the claimed invention is an extremely large structurally and functionally variable genus. An argument can be made that the recited genus of is adequately described by the disclosure of the structure of polypeptide of SEQ ID NO: 1 and SEQ ID NO: 3 . However, the art clearly teaches there is a practical limits to predict function of a polypeptide based structural homology:
A. Devos et al., (Proteins: Structure, Function and Genetics, 2000, Vol. 41: 98-107), teach that the results obtained by analyzing a significant number of true sequence similarities, derived directly from structural alignments, point to the complexity of function prediction. Different aspects of protein function, including (i) enzymatic function classification, (ii) functional annotations in the form of key words, (iii) classes of cellular function, and conservation of binding sites can only be reliably transferred between similar sequences to a modest degree. The reason for this difficulty is a combination of the unavoidable database inaccuracies and plasticity of proteins (Abstract, page 98) and the analysis poses interesting questions about the reliability of current function prediction exercises and the intrinsic limitation of protein function prediction (Column 1, paragraph 3, page 99) and conclude that "Despite widespread use of database searching techniques followed by function inference as standard procedures in Bioinformatics, the results presented here illustrate that transfer of function between similar sequences involves more difficulties than commonly believed. Our data show that even true pair-wise sequence relations, identified by their structural similarity, correspond in many cases to different functions (column 2, paragraph 2, and page 105).
B. Whisstock et al., (Quarterly Reviews of Biophysics 2003, Vol. 36 (3): 307-340,) also highlight the difficulties associated with "Prediction of protein function from protein sequence and structure": "To reason from sequence and structure to function is to step onto much shakier ground", closely related proteins can change function, either through divergence to a related function or by recruitment for a very different function, in such cases, assignment of function on the basis of homology, in the absence of direct experimental evidence, will give the wrong answer (page 309, paragraph 4), it is difficult to state criteria for successful prediction of function, since function is in principle a fuzzy concept. Given three sequences, it is possible to decide which of the three possible pairs is most closely related. Given three structures, methods are also available to measure and compare similarity of the pairs. However, in many cases, given three protein functions, it would be more difficult to choose the pair with most similar function, although it is possible to define metrics for quantitative comparisons of different protein sequences and structures, this is more difficult for proteins of different functions (page 312, paragraph 5), in families of closely related proteins, mutations usually conserve function but modulate specificity i.e., mutations tend to leave the backbone conformation of the pocket unchanged but to affect the shape and charge of its lining, altering specificity (page 313, paragraph 4), although the hope is that highly similar proteins will share similar functions, substitutions of a single, critically placed amino acid in an active-site residue may be sufficient to alter a protein's role fundamentally (page 323, paragraph 1).
C. This finding is reinforced in the following scientific teachings for specific proteins in the art that suggest, even highly structurally homologous polypeptides do not necessarily share the same function and many functionally similar proteins will have little or no structural homology to disclosed proteins. For example, proteins having similar structure have different activities (structure does not always correlate to function); Witkowski et al., (Biochemistry 38:11643-11650, 1999) teaches that one conservative amino acid substitution transforms a beta -ketoacyl synthase into a malonyl decarboxylase and completely eliminates beta-ketoacyl synthase activity. The art also teaches that functionally similar molecules have different structures; Kisselev L., (Structure, 2002, Vol. 10: 8-9) teach that polypeptide release factors in prokaryotes and eukaryotes have same function but different structures.
As stated above, no information beyond the characterization of a few species; such as the structure of disclosure of the structure of polypeptide of SEQ ID NO: 1 and SEQ ID NO: 3 respectively has been provided by the applicants’, which would indicate that they had the possession of the claimed genus of polypeptides. The claimed genera of polypeptides and the encoding polynucleotides have widely variable structures and associated functions. As it is discussed above, a minor changes in structure may result in changes affecting function, since, the specification provided no additional information (species/variant/mutant) correlating structure with function, one skilled in the art cannot reasonably conclude that applicant had possession of the claimed invention at the time the instant application was filed. Furthermore, "Possession may not be shown by merely describing how to obtain possession of members of the claimed ,genus or how to identify their common structural features" (See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895). A definition by function, as we have previously indicated, does not suffice to define the genus because it is only an indication of what the .gene does (function), rather what it is (structure), see University of California v. Eli Lilly & Co., 43 USPQ2d 1938, thus above claims lack adequate written description.
Applicants' are referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov.
Conclusion
Claims 1-14 are rejected. No claim is allowed.
Any inquiry concerning this communication or earlier communications from the
examiner should be directed to Mohammad Meah whose telephone number is 571-272-
1261. The examiner can normally be reached on 8:30-5PM.
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supervisor, Robert Mondesi can be reached on 4089187584. The fax phone number
for the organization where this application or proceeding is assigned is 571-273-8300.
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/MOHAMMAD Y MEAH/Examiner, Art Unit 1652