DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Election/Restrictions
Applicant’s election without traverse of Group I (i.e., claims 1-13, 42, 58 and 66, drawn to a recombinant carbonic anhydrase polypeptide), and to Species A (i.e., Single and specific recombinant carbonic anhydrase polypeptide indicating ALL variables and including indication of: 1. Single and specific sequence identifier, Applicants’ Election: 65% identity with SEQ ID NO: 5, substitution at position 223, for L or I (i.e., 223L or 223I); 2. Single isoelectric point (pI), Applicants’ Election: lower than 8; 3. Single and specific increase in solubility and/or thermostability and if an increase in solubility then a single and specific time and temperature of exposure and solubility reference point; and if an increase in thermostability, single and specific time and temperature of exposure in an alkaline carbonate solution, Applicants’ Election: a recombinant carbonic anhydrase polypeptide having a solubility of greater than 6 after 24 hours at 80°C in an alkaline carbonate solution 1.45 M K2CO3 with alpha 0.7, and a recombinant carbonic anhydrase polypeptide having increased thermostability after a 72-hour exposure at 85°C, in an alkaline carbonate solution 1.45M K2CO3 with alpha 0.7; 4. Single and specific pH range, Applicants’ Election: pH range 8.5 to 11), in the reply filed on 12/17/2024 is acknowledged.
Claims 6 and 9 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species there being no allowable generic or linking claim. Similarly, claims 24, 29, 31-32, 35-41, 43-57, 59-65 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention there being no allowable generic or linking claim. Election was made without traverse in the reply filed on12/17/2024.
Please note that the Examiner has extended the Species to include substitutions at positions other than 223.
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 02/16/2026 has been entered.
Claim Status
Claims 1-42 were originally filed and amended on 09/24/2021. The amendment cancelled claims 25-28, 30 and 33-34; amended claims 5-14, 17-18, 22-24, 29, 31-32, 35-36 and 38-42; and added new claims 43-66.
The amendment filed on 08/20/2025, cancelled claims 5-7 and 16-18; and amended claims 1-2, 8, 10, 12, 14-15, 19, 22-23 and 45.
The amendment filed on 02/09/2026 amended claims 1, 14-15, 19, 23, 29 and 46.
Claims 1-4, 8-15, 19-24, 29, 31-32, 35-66 are currently pending, and claims 1-4, 8, 10-15, 19-23, 42, 58 and 66 are under consideration.
Priority
The present application claims status as a 371 (National Stage) of PCT/IB2020/052410 filed March 17th 2020, and claims the benefit under 35 U.S.C 119 (e) to U.S. Provisional Application No. 62/823,744 filed March 26th 2019. Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C 119 (e) or under 35 U.S.C 120, 121, or 365 (c ) is acknowledged.
Sequence Interpretation
The scope of “a recombinant carbonic anhydrase polypeptide” is interpreted as open-ended requiring 93% identity with SEQ ID NO: 5 with any N-/-C terminal additions. Per MPEP 2111.03(I), the transitional phrase “comprising”, which is synonymous with “including,” “containing,” or “characterized by,” is inclusive or open-ended and does not exclude additional, unrecited elements or method steps.
Since SEQ ID NO: 5 is 226 residues in length, a sequence that is at least 93% identical would encompass up to 15 modifications including any insertions, substitutions, deletions, etc., wherein one of the up to 15 modifications must be one amino acid difference (i.e., Leu or Ile) at position 223 as compared to SEQ ID NO: 1.
Response to Arguments
1. Applicants’ arguments, see Remarks, filed 02/09/2026, with respect to the 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; have been fully considered but are not persuasive. The 35 U.S.C. 112(a) rejection to claims 1-4, 8, 10-15, 19-23, 42, 58 and 66 has been maintained.
New Rejections
Claim Rejections - 35 USC § 112
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.
1. Claims 1-4, 8, 10-15, 19-23, 42, 58 and 66 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. This is a new matter rejection.
In the instant case, claim 1 was amended to include the limitation “with any N-/-C terminal additions”, which makes reference to the amino acid sequence of a recombinant carbonic anhydrase polypeptide having at least 93% identity with SEQ ID NO: 5 and one amino acid difference as compared to SEQ ID NO: 1. Applicants stated in their remarks that “[s]upport for these amendments can be found at least at pg. 11, lines 23-28, of the specification as filed” Further, Applicants stated that “no new matter is added” (See pg. 16 of the Remarks filed on 02/09/206). However, the support (i.e., pg. 11, lines 23-28,) provided by Applicants does not support that newly added limitation “with any N-/-C terminal additions” was previously presented, as the there is no mention a recombinant carbonic anhydrase polypeptide having carbonic anhydrase activity comprising an amino acid sequence having at least 93% identity with SEQ ID NO: 5 with any N-/-C terminal additions.
The specification is void of support that would clearly support the newly added limitation. The specification does not teach the specifically claimed recombinant carbonic anhydrase polypeptide with any N-/-C terminal additions. Examination of the instant support shows that the envisioned recombinant carbonic anhydrase polypeptide having carbonic anhydrase activity comprising an amino acid sequence having at least 93% identity with SEQ ID NO: 5 and one amino acid difference as compared to SEQ ID NO: 1 at residue position 223, wherein SEQ ID NO: 5 comprises 223L or 223I, and said recombinant carbonic anhydrase polypeptide has increased solubility and/or increased thermostability as compared to a corresponding carbonic anhydrase polypeptide lacking said one amino acid difference. Positive recitation of recombinant carbonic anhydrase polypeptide without any reference to whether any N-/-C terminal additions are included does not provide support in claiming that the that the recombinant anhydrase polypeptide includes any N-/-C terminal additions. Pursuant to MPEP 2163.03(V), [a]n original claim may lack written description support when . . . (2) a broad genus claim is presented but the disclosure only describes a narrow species with no evidence that the genus is contemplated. See Ariad Pharms., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1349-50 (Fed. Cir. 2010) (en banc). "Even if a claim is supported by the specification, the language of the specification, to the extent possible, must describe the claimed invention so that one skilled in the art can recognize what is claimed. The appearance of mere indistinct words in a specification or a claim, even an original claim, does not necessarily satisfy that requirement. "Enzo Biochem, Inc. v. Gen-Probe, Inc., 323 F.3d 956, 968, 63 USPQ2d 1609, 1616 (Fed. Cir. 2002). Therefore, the claimed the claimed recombinant carbonic anhydrase polypeptide with any N-/-C terminal additions is not expressly described.
The newly added claim limitations must be supported in the specification through express, implicit, or inherent disclosure.” MPEP 2105 states that “[a] lack of adequate written description issue also arises if the knowledge and level of skill in the art would not permit one skilled in the art to immediately envisage the product claimed from the disclosed process. See, e.g., Fujikawa v. Wattanasin, 93 F.3d 1559, 1571, 39 USPQ2d 1895, 1905 (Fed. Cir. 1996) (a "laundry list” disclosure of every possible moiety does not constitute a written description of every species in a genus because it would not “reasonable lead” those skilled in the art to any particular species); In re Ruschig, 379 F.2d 990, 995, 154 USPQ 118, 123 (CCPA 1967).
In the instant case, as set forth above, the disclosure describes recombinant carbonic anhydrase polypeptides having carbonic anhydrase activity comprising an amino acid sequence having at least 93% identity with SEQ ID NO: 5 and one amino acid difference as compared to SEQ ID NO: 1 at residue position 223, wherein SEQ ID NO:5 comprises 223L or 223I and said recombinant carbonic anhydrase polypeptide has increased solubility and/or increased thermostability as compared to a corresponding carbonic anhydrase polypeptide lacking said one amino acid difference (See Specification, Table 5). However, the instantly claimed genus encompassing any N-/-C terminal additions has not been adequately supported.
Maintained/Modified Rejections in light of Amendment
Claim Rejections - 35 USC § 112
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.
1. Claims 1-4, 8, 10-15, 19-23, 42, 58 and 66 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.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the inventor was in possession of the claimed genus.
Independent claim 1 is drawn to “[a] recombinant carbonic anhydrase polypeptide having carbonic anhydrase activity comprising an amino acid sequence having at least 93% identity with SEQ ID NO: 5 with any N-/-C terminal additions and one amino acid difference as compared to SEQ ID NO: 1 at residue position 223; wherein SEQ ID NO: 5 comprises 223L or 223I, and said recombinant carbonic anhydrase polypeptide has increased solubility and/or increased thermostability as compared to a corresponding carbonic anhydrase polypeptide lacking said one amino acid difference”.
The Examiner interprets the scope of the claimed recombinant carbonic anhydrase polypeptide having carbonic anhydrase activity, as a sequence that would encompass up to 15 modifications including any insertions, substitutions, deletions, etc., where one of the 15 modifications must be a substitution at position 223 relative to the wild type (i.e., SEQ ID NO: 1).
As such, “a recombinant carbonic anhydrase polypeptide” encompasses any amino acid sequence of any carbonic anhydrase that comprises any 15 modifications where one of the modifications is an amino acid difference at position 223 (i.e., Applicant’s Election) compared to SEQ ID NO: 1 and still exhibit carbonic anhydrase activity as well as increased solubility and/or thermostability.
Therefore, the scope of claim 1 and dependent claims 2-4, 8, 10-15, 19-23, 42, 58 and 66 encompass a vast array of sequences where the necessary core structure and/or sequence that would be needed for the claimed recombinant carbonic anhydrase to exhibit the claimed functions is to be at least 93% identical to SEQ ID NO: 5 and comprise one amino acid difference relative to a corresponding carbonic anhydrase polypeptide lacking said one amino acid difference.
Applicants reduced to practice three different Thermovibrio ammonificans carbonic anhydrase (TACA) variants, i.e., SEQ ID NOs: 2-4, chosen as templates for random mutagenesis; with each variant having a different pI (i.e., pI of 8.3 for SEQ ID NO: 2, pI of 7.2 for SEQ ID NO: 3 and pI of 6.1 for SEQ ID NO: 4) in addition to exhibiting carbonic anhydrase activity (see specification, pg. 19, lines 1-5 and Table 1).
Figure 1, shows a sequence alignment between wild type TACA (i.e., SEQ ID NO: 1) and the three variants. It is noted that the only difference between SEQ ID NO: 1 and SEQ ID NO: 2 is one non-conservative substitution at R156E.
With respect to SEQ ID NO: 2, the number of positions with improved thermostability and/or solubility over wtTACA (i.e., SEQ ID NO: 1) was identified as 35, out of the 114 positions targeted (see specification, pg. 19, Table 2).
In other words, the results displayed in Table 3, reflect the effect of individual mutations at the 114 positions targeted and their effect on the solubility and stability as well as the overall performance relative to the parent template (i.e., SEQ ID NO: 2, R156E) (see pg. 20, Table 3). The results displayed in Table 3 fail to comply with the written description requirement because the recombinant carbonic anhydrase polypeptide does not encompass up to 15 modifications, for a sequence that is 226 amino acids in length and has at least 93% identity with SEQ ID NO: 5. Variants which comprise mutation: SEQ ID NO: 2+K223I or SEQ ID NO: 2+K223L (see pg. 23, Table 3, 1st and 2nd to last entries) had an increase in stability. However those variants comprise a total of 2 mutations (i.e., R156E from starting template SEQ ID NO: 2 and K223I or L).
Table 4 shows mutagenesis results using SEQ ID NO: 3 as a starting template. SEQ ID NO: 3 comprises a total of 15 mutations relative to wtTACA (SEQ ID NO: 1), i.e., two non-conservative substitutions at R156E and at V216T, and thirteen conservative substitutions at K27R, N38D, K88R, K116R, N119D, K128R, E160D, D168E, E192D, E199D, K203R, K206R, and L219I (see Fig. 1, and pg. 18, Table 1). As such, the results displayed in Table 4 fail to comply with the written description requirement because none of the variants displayed in Table 4 comprise an amino acid difference at position 223 relative to SEQ ID NO: 1 (see instant specification, pg. 25, Table 4), and the template sequence (i.e., SEQ ID NO: 3) encompasses the allowed number of modifications (i.e., 15) for a sequence that is 226 amino acids in length and is at least 93% identical to SEQ ID NO: 5.
Table 5, shows mutagenesis results of variants derived from SEQ ID NO: 4. SEQ ID NO: 4 comprises a total of 16 mutations relative to wtTACA (SEQ ID NO: 1), i.e., three non-conservative substitutions at V79E, R156E and V216T, and thirteen conservative substitutions at Y77F, K88E, Y105F, K116E, K128E, E137D, E145D, D168E, Y170F, E195D, E199D, L219I and I226R (see Figure 1, and pg. 18, Table 1). Therefore, the results displayed in Table 5 fail to comply with the written description requirement because the template sequence (i.e., SEQ ID NO: 4) encompasses more than the allowed number of modifications (i.e., 15) for a sequence that is 226 amino acids in length and is at least 93% identical to SEQ ID NO: 5.
Additionally, the variants displayed in Table 5 which comprise an amino acid difference at position 223 relative to SEQ ID NO: 1, comprise additional mutations thereby resulting in a variant with more than the allowed number of modifications (i.e., 15). For instance, variant comprising mutation: SEQ ID NO: 4 + S39I + E128K +T154D +K223I (SEQ ID NO: 8) (see instant specification, pg. 25, Table 5, last entry) fails to comply with the written description requirement because it comprises a total of 20 mutations, and the individual amino acid causing the increase in stability or solubility could not be identified. The same is true for the variant comprising mutation: SEQ ID NO: 4 + S39I + G130A + T154D + K223I (SEQ ID NO: 9) (see instant specification, pg. 26, Table 5, second entry); for the variant comprising mutation: SEQ ID NO: 4 + S39I + G130A + T154D +K223L (SEQ ID NO: 10) (see instant specification, pg. 26, Table 5, third entry); for the variant comprising mutation: SEQ ID NO: 4 + S39I + G130A + T154P + D195E + K223I (SEQ ID NO: 11) (see instant specification, pg. 26, Table 5, fourth entry); and for the variant comprising mutation: SEQ ID NO: 4 + S39I + G130A + T154P + D195E + K223L (SEQ ID NO: 7) (see instant specification, pg. 26, Table 5, fifth entry).
The results shown for SEQ ID NO: 6, which comprises mutation SEQ ID NO: 4 + S39I+K223L and the amino acid with positive effect on stability was identified to be Leu at position 223 (see instant specification, pg. 26, Table 5, seventh entry). However, SEQ ID NO: 6 fails to comply with the written description requirement because it encompasses a total of 18 mutations (16 from template SEQ ID NO: 4 and two additional) which is more than the allowed number of possible modifications for a sequence that is 226 amino acids in length and is at least 93% identical to SEQ ID NO: 5.
Likewise, the variant comprising mutation SEQ ID NO: 4 + D195E+K223I (see instant specification, pg. 27, Table 5), had increased thermostability, however the increase was attributed to the substitution at position 195. Therefore, the variant fails to comply with the written description requirement because it encompasses more than the allowed number of modifications (i.e., 15) for a sequence that is 226 amino acids in length and is at least 93% identical to SEQ ID NO: 5 and because the increment in thermostability is not attributed to Leu or Ile at position 223.
Lastly, variant comprising mutation: SEQ ID NO: 4 + K223I had an increase in both solubility and on stability, and the increase was attributed to Ile at position 223 (see instant specification, pg. 27, Table 5, second to last entry); and variant comprising mutation: SEQ ID NO: 4 + K223L, had an increase in stability and the increase was attributed to Leu at position 223 (see instant specification, pg. 27, Table 5, last entry). However, these variants fail to comply with the written description requirement because they comprise a total of 17 modifications (i.e., 16 from template SEQ ID NO: 4 plus an additional mutation at position 223), which is more than the allowed number of modifications (i.e., 15) for a sequence that is 226 amino acids in length and is at least 93% identical to SEQ ID NO: 5.
In order to meet the written description requirement, Applicants must provide a representative number of species of recombinant carbonic anhydrase polypeptides having:
-carbonic anhydrase activity,
-an amino acid sequence having at least 93% identity with SEQ ID NO: 5,
-Leu or Ile at position 223 as compared to SEQ ID NO: 1; and
-increased solubility and/or thermostability as compared to a corresponding carbonic anhydrase polypeptide lacking said one amino acid difference.
An invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function. See MPEP 2163 (I)(A).
In the instant case, the sequences reduced to practice (i.e., SEQ ID NOs: 2-4) do not share a common core structure; without an indication of a core structure, sequence or residues that would be necessary in order for a recombinant carbonic anhydrase polypeptide to exhibit the claimed functions (i.e., increased solubility and/or increased thermostability), it would be difficult for a skilled artisan to envision the correlation between structure and function for the whole genus and/or to predict what would be covered by the functionally claimed genus because Applicants have failed to provide a representative number of species to support the scope of the whole genus.
As such, claims 1-4, 8, 10-15, 19-23, 42, 58 and 66 do not meet the written description requirement, because “[t]he ‘essential goal’ of the description of the invention requirement is to clearly convey the information that an applicant [inventor] has invented the subject matter which is claimed.” In re Barker, 559 F.2d 588, 592 n.4, 194 USPQ 470, 473 n.4 (CCPA 1977). See MPEP 2163.I.
Accordingly, claims 1-4, 8, 10-15, 19-23, 42, 58 and 66 remain rejected.
Examiner’s note: a telephone call was made to Applicants’ representative (Christopher M. Goff) on 06/01/2026, however the party could not be reached. A detailed message was left and a tentative interview was proposed for 06/11/2026 at 3:30 ET with the intend of discussing the 35 U.S.C 112(a) rejection to claims 1-4, 8, 10-15, 19-23, 42, 58 and 66, clarify the “93% identity to SEQ ID NO: 5” statement made in the action mailed on 10/17/2025 (see Final Rejection dated 10/17/2028 at pg. 11) and possibly move towards allowance. However, no response to this message has been received.
Response to Arguments
Applicants' arguments filed 02/09/2026 have been fully considered but they are not persuasive for the following reasons:
MPEP §2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus.
The importance of structure/function correlations was highlighted by the courts (Abbvie Deutschland v. Janssen Biotech and Centorcor Biologics, App. No. 2013-1338, -1346 (Fed. Cir., July 1, 2014)). The Abbvie case involved antibodies and written description. The court stated: “We have held that “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.” Id. at 1350 (quoting Eli Lilly, 119 F.3d at 1568– 69).”. The courts then further stated: “With the written description of a genus, however, merely drawing a fence around a perceived genus is not a description of the genus. One needs to show that one has truly invented the genus, i.e., that one has conceived and described sufficient representative species encompassing the breadth of the genus. Otherwise, one has only a research plan, leaving it to others to explore the unknown contours of the claimed genus.” (emphasis added) and then state: " Functionally defined genus claims can be inherently vulnerable to invalidity challenge for lack of written description support, especially in technology fields that are highly unpredictable, where it is difficult to establish a correlation between structure and function for the whole genus or to predict what would be covered by the functionally claimed genus. Ariad, 598 F.3d at 1351 (“[T]he level of detail required to satisfy the written description requirement varies depending on the nature and scope of the claims and on the complexity and predictability of the relevant technology.”); see also Centocor Ortho Biotech, Inc. v. Abbott Labs., 636 F.3d 1341, 1352 (Fed. Cir. 2011) (noting the technical challenges in developing fully human antibodies of a known human protein). It is true that functionally defined claims can meet the written description requirement if a reasonable structure-function correlation is established, whether by the inventor as described in the specification or known in the art at the time of the filing date. Enzo Biochem, Inc. v. Gen-Probe Inc., 323 F.3d 956, 964 (Fed. Cir. 2002). However, the record here does not indicate such an established correlation. Instead, Abbvie used a trial and error approach to modify individual amino acids in order to improve the IL-12 binding affinity. Moreover, the ’128 and ’485 patents do not describe any common structural features of the claimed antibodies. The asserted claims attempt to claim every fully human IL-12 antibody that would achieve a desired result, i.e., high binding affinity and neutralizing activity, and cover an antibody as different as Stelara, whereas the patents do not describe representative examples to support the full scope of the claims.”
In the instant case, the details provided in the instant specification pertaining to claimed recombinant carbonic anhydrase polypeptide fail to convey with reasonable clarity that the inventor had possession of the claimed invention. The evidence provided in the specification is not sufficient to satisfy the written description of a genus because the “identifying characteristics” described in the instant specification, in particular requiring at least 93% identity to SEQ IDNO: 5 in addition to one amino acid difference at position 223 as compared to SEQ ID NO: 1, refer to a recombinant carbonic anhydrase with at least 15 modifications including any insertions, substitutions, deletions, etc.; in addition to one amino acid difference at position 223 as compared to SEQ ID NO: 1. However, Applicants have reduced to practice three sequences (i.e., SEQ ID NOs: 2-5) and their respective variants, and none of the sequences reduced to practice meet the claim limitations as recited in instant claim 1. Therefore, there is no core structure/sequence associated with the increased solubility and/or increased thermostability as compared to a corresponding carbonic anhydrase polypeptide lacking said one amino acid difference.
Additionally, a "representative number of species" means that the species which are adequately described are representative of the entire 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. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014).
Thus, the limited recombinant carbonic anhydrase polypeptide having carbonic anhydrase activity, in addition to at least 93% identity with SEQ ID NO: 5, one amino acid difference as compared to SEQ ID NO: 1, and having increased solubility and/or increased thermostability as compared to a corresponding carbonic anhydrase polypeptide lacking said one amino acid difference do not constitute a representative number of recombinant carbonic anhydrase polypeptides that an ordinary skilled artisan can reasonably extrapolate and still exhibit the claimed function.
Furthermore, the evidence provided the instant specification in particular Tables 3-5, is also not sufficient to satisfy the written description requirement because the variants do not encompass up to 15 modifications (i.e., 93% identity to SEQ ID NO: 5) and still exhibit the function increased solubility and/or increased thermostability. Therefore, the “identifying characteristics” recited in the instant specification are not sufficient to distinguish the claimed recombinant carbonic anhydrase polypeptide from other known carbonic anhydrase polypeptides lacking said one amino acid difference. As such, the details disclosed in the instant specification pertaining to the 93% identity with SEQ ID NO: 5 are not sufficient to show that Applicants were in possession of the claimed genus (i.e., recombinant carbonic anhydrase polypeptide), and are also not sufficient to claim that the Applicants’ were in possession of the claimed species (i.e., recombinant anhydrase polypeptide having at least 93% identity with SEQ ID NO: 5 and one amino acid difference at position 223 as compared to SEQ ID NO: 1).
Accordingly, the 35 U.S.C. 112(a) rejection of claims 1-4, 8, 10-15, 19-23, 42, 58 and 66 is maintained.
Conclusion
No claims are allowed.
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/CLAUDIA ESPINOSA/Patent Examiner, Art Unit 1654
/LIANKO G GARYU/Supervisory Patent Examiner, Art Unit 1654
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