DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s election with traverse of group I, claims 86-90 and 94, in the reply filed on 6/19/26, is acknowledged. Applicant has further elected D216E as the species of substitution. Upon reconsideration, L235A is also being included in the examination.
Applicant's traversal is on the grounds that the identified groups relate to common subject matter and that there would not be a serious search and/or examination burden to examine all the claims This is not found to be persuasive because burden is irrelevant to the restriction practice for cases filed under 35 U.S.C 371 (see MPEP Chapter 1800). Nonetheless, it is noted that IgG polypeptides and vectors (i.e. nucleic acids) are different products that are recognized divergent subject matter that is distinct because their structures are different and are therefore capable of separate manufacture, use and sale. Therefore these products are distinct, and searches for both would place an undue burden upon the examiner due to divergent subject matter of each Group. Further, a prior art search also requires a literature search. It is an undue burden for the examiner to search more than one invention. The claims encompass a genus of structurally distinct polypeptides or nucleic acids with different amino acid substitutions and different nucleic acid sequences. Furthermore, the groups and species are not linked by a single general inventive concept and unity of invention is lacking, since they lack a special technical feature over the prior art cited in the restriction requirement (and set forth below).
The requirement is still deemed proper and is therefore made FINAL.
Claims 91-93 are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
Claims 86-90 and 94 are being acted upon.
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 86-90 and 94 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
The scope of the claimed substitution relative to a wild-type bovine IgG constant domain at particular positions, i.e. 216, 234, 235, as recited in claim 86,. is unclear and indefinite. The claim recites EU index numbering, which is a numbering scheme for human IgG. For example, the claim recites a substitution at position 235 relative to a while type bovine IgG constant domain, using EU numbering, wherein said substitution is L235A. In EU numbering, position 235 of human IgG is “L” (see attached IMGT scientific chart). How is the position 235 of bovine IgG to be determined? Is it the residue that corresponds to position 235 in human IgG based on alignment or does it refer to the exemplary numbering in Fig. 23? The specification does not specifically define the numbering scheme, other than providing exemplary numbering in Fig. 23. However, residue 235 is not “L” in all of the exemplary numbering schemes in Fig. 23. For example, in Fig. 23, bovine IgG1a has P235, not L235. Would the claims encompass a bovine IgG1a constant region having an A at position 235? Figure 23 depicts bovine IgG3 as having 235L, but in the alignment of the residues, said residue 235 of bovine IgG3 corresponds to residue 257 in bovine IgG1a and human IgG1. It is noted that the claims are not limited to bovine IgG3 L235A, but broadly encompass any bovine IgG (and it appears that residue 235 is not the same in all types of bovine IgG). The scope of the claims positions cannot be establish.
Claim 86 is also unclear since it recites “at least one amino acid substitution” and wherein “said substitution” is at amino acid reissue 216, 234,…or 437. There is insufficient antecedent basis for “said substitution” since the claim does not recite a substitution, but rather the claim recites “at least one substitution”. This creates ambiguity as to the intended claim scope. For example, is the claim intending to be interpreted as comprising at least one amino acid substitutions, wherein at least one of the substitutions is at amino acid residue 216,234..or 237? Or is the claim intending that the one or more substitutions are from the recited positions? For the purposes of examination, the claim is being interpreted as a bovine IgG constant domain comprising at least one amino acid substitution relative to a wild-type bovine IgG constant domain, wherein at least one of the amino acid substitutions is at amino acid residue 216, 234…or 437. In other words, the constant domain is open to other amino acid substitutions, so long as one of the substitutions is from the recited positions.
The scope of claim 94 is unclear. Claim 94 is directed to a fusion molecule comprising “a bovine IgG constant domain” fused to an agent, said bovine IgG constant domain comprising “the modified IgG of claim 86”. Claim 86 is directed to a modified IgG comprising a bovine IgG constant domain. An IgG is an antibody structure comprising a variable region and an Fc region. Therefore, claim 86 is unclear, since it recites two different limitations of different scopes, i.e. a bovine IgG constant domain, and a “modified IgG of claim 86”. Would claim 94 encompass a fusion molecule comprising a bovine IgG constant domain fused to an agent, such as a heterologous protein fused to a bovine IgG constant domain. Or does the claim actually require an IgG antibody structure with a variable region and a constant region, i.e. a fusion molecule comprising “the modified IgG of claim 86”. If the former interpretation is intended, amending claim 94 to be an independent claim which recites the substitution limitations from claim 86 would be remedial, i.e. a fusion molecule comprising a bovine IgG constant domain fused to an agent, said bone IgG constant domain comprising at least one amino acid substitution relative to wild-type bovine IgG constant domain, wherein said substitution is at amino acid residue 216, 234, …”. Alternatively, if the latter interpretation is desired, reciting a fusion molecule comprising a modified IgG of claim 86 fused to an agent, would be remedial.
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 86-90 and 94 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural phenomenon (product of nature) without significantly more. The claim(s) recite(s) a modified IgG comprising a bovine IgG constant domain with certain substitutions. This judicial exception is not integrated into a practical application because IgG with the residues specified in the claims is a product of nature. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception for the reasons set forth below.
Laws of nature and natural phenomena, as identified by the courts, include naturally occurring principles/relations and nature-based products that are naturally occurring or that do not have markedly different characteristics compared to what occurs in nature. The courts have often described these exceptions using other terms, including “physical phenomena,” “scientific principles”, “natural laws,” and “products of nature.” Product of nature exceptions include both naturally occurring products and non-naturally occurring products that lack markedly different characteristics from any naturally occurring counterpart. See, e.g., Ambry Genetics, 774 F.3d at 760, 113 USPQ2d at 1244 (“Contrary to Myriad's argument, it makes no difference that the identified gene sequences are synthetically replicated. As the Supreme Court made clear, neither naturally occurring compositions of matter, nor synthetically created compositions that are structurally identical to the naturally occurring compositions, are patent eligible.”). Thus, a synthetic, artificial, or non-naturally occurring product such as a cloned organism or a human-made hybrid plant is not automatically eligible because it was created by human ingenuity or intervention. See, e.g.,In re Roslin Institute (Edinburgh), 750 F.3d 1333, 1337, 110 USPQ2d 1668, 1671-72 (Fed. Cir. 2014) (cloned sheep); cf. J.E.M. Ag Supply, Inc. v. Pioneer Hi-Bred Int’l, Inc., 534 U.S. 130-132, 60 USPQ2d 1868-69 (2001) (hybrid plant). Instead, the key to the eligibility of all non-naturally occurring products is whether they possess markedly different characteristics from any naturally occurring counterpart. See MPEP 2106.04(b).
In the instant case, the claims are directed to compositions of matter as set forth in Step 1 of the subject matter eligibility test (see MPEP 2106). Regarding step2A, prong 1, the claims recite a modified IgG comprising a bovine IgG constant domain comprising at least one amino acid substitution relative to a wild-type bovine IgG, wherein said substitution (i.e. at least one substitution) is D216E. The claims broadly recite “at least one amino acid substitution” relative to a wild-type bovine IgG. This would encompass numerous amino acid substitutions to any bovine IgG constant domain (comprising CH1, CH2, and/or CH3), so long as one of the specified substitutions was present. Bovine and human IgG are homologous polypeptides and human IgG1 comprises residues 216E (see Fig. 23 of the instant specification). Thus, naturally occurring human IgG1 can be considered a “modified” version of bovine IgG having more than one substitution relative to a wild-type bovine IgG, including D216E. The manner in which the IgG is made, for example modified by using a wild-type bovine IgG having a D residues and introducing and E substitution, would represent product by process limitations. However, during examination, a product-by-process claim is only limited to the structure implied by the process. In the instant case, the claims broadly read on naturally occurring human IgG1, which would represent a variant or “modified” IgG constant region relative to wild type bovine IgG having more than one substitution including residue 216E. Regarding claim 94, naturally occurring human IgG1 can be considered a “fusion” polypeptide comprising a variable region (i.e. an agent) fused to a “modified” bovine IgG constant domain. Alternatively, naturally occurring human IgG1 is also glycosylated, which would also be within the scope of a fusion molecule “fused” to a carbohydrate (i.e. an agent).
Regarding step 2A prong two and step 2B, the claims do not recite additional elements that integrate the judicial exception into a practical application, nor do the claims recite any additional elements that amount to significantly more than the judicial exception. Claim 89-90 recite a kit or a pharmaceutically acceptable carrier. However, these limitations, recited at a high level of generality amount to nothing more than field of use or insignificant extra-solution activity. Thus the claimed “modified” IgG is not markedly different in structure or function from naturally occurring IgG.
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) 86-90 and 94 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by WO 2017062253 (of record).
WO 2017062253 teaches a chimeric (i.e. modified) IgG comprising a non-bovine variable region and a bovine IgG constant region, wherein the bovine IgG constant region comprises a CH1 domain, a CH2 domain and a CH3 domain (see page 3, in particular). WO 2017062253 teaches pharmaceutical compositions comprising said modified IgG and a pharmaceutically acceptable carrier and kits comprising said IgG. (See page 5 and 57, in particular). Said chimeric IgG can be considered a fusion between a variable region and a bovine IgG constant region. Alternatively, WO 201706225 also teaches said antibodies conjugating IgG to a therapeutic agent (i.e. a “fusion” to an agent, see page 39, in particular).
Regarding the one or more amino acid substitutions relative to a wild type bovine IgG constant domain, WO 201706225 teaches that the bovine IgG1 constant region can comprises a substitution 235A according to the EU index (see page 29, in particular). Regarding the limitation that the substitution is “L235A” to the extent that this refers to a particular numbering scheme/and or starting material (i.e. using bovine IgG3, etc.), it is noted that the manner in which the substitution is made would be a product by process limitation and the patentability of a product does not depend on its method of production in the absence of a structural difference. The claim requires “A” at position 235, which is taught by the cited reference. Whether the “A” is introduced by substitution from a type of bovine IgG with L at position 235, or a different isotype of bovine IgG having a different residue at position 235 does not change the resulting structure which has A at position 235. Thus, the prior art modified bovine IgG with a substitution of an A residue at position 235 is within the scope of the present claims. WO 2017062253 also teaches another embodiment wherein the chimeric bovine antibodies have substitutions shown in SEQ ID NO: 86. Said SEQ ID NO: 86 has a sequence EPRCKP, which is modified relative to the wild type bovine IgG1 sequence, which has an amino acid sequence DPRCP. The specification in Fig. 23 indicates that EU position 216 of bovine IgG1 corresponds to the first position D above in DPRCKP. Therefore, said modified bovine IgG of SEQ ID NO: 86 in the prior art with EPRCKP comprises one or more substitutions, including a D216E substitution compared to a wild-type bovine IgG1.
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to AMY E JUEDES whose telephone number is (571)272-4471. The examiner can normally be reached on M-F from 7am to 3pm.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Misook Yu can be reached on 571-272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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Amy E. Juedes
Patent Examiner
Technology Center 1600
/AMY E JUEDES/Primary Examiner, Art Unit 1644
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