The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
This office action is in response to Applicants’ amendments/remarks received March 5, 2026.
Rejections and/or objections not reiterated from previous office actions are hereby withdrawn.
Claims 1-10, 32 are canceled. Claims 11-31, 33-40, 41, to SEQ ID NO: 2, are under consideration.
This application is a CIP of U.S. Application 18336915, filed June 16, 2023, which is a CON of U.S. Application 18050213, filed October 27, 2022, now U.S. Patent 11718644, which is a CON of PCT/US22/380774, filed July 22, 2022, which claims benefit of provisional applications 63/225388, filed July 23, 2021, and 63/225410, filed July 23, 2021. This application is also a CIP of U.S. Application 17508064, filed October 22, 2021, now abandoned, which is a CON of PCT/US20/47076, filed August 19, 2020, which claims benefit of provisional application 62/888674, filed August 19, 2019.
Objections and Rejections
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 29-30 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claims 29-30 are product claims dependent on claim 11. The claims do not recite any additional components to the product that further limit the claims. The recitation of an intended use (i.e. food product) in a product claim does not further limit the claims. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Reply: Applicants’ remarks have been considered but they are not persuasive. Applicants assert that claims 29-30 are directed to a food product that includes the rOVA composition of claim 11. Applicants assert that this is not just describing an intended use of the composition but is actually claiming the food product itself, made with the composition.
Applicants’ remarks are not persuasive. As noted above, claims 29-30 are product claims dependent on claim 11. The claims do not recite any additional components to the product that further limit the claims. The recitation of an intended use (i.e. food product) in a product claim does not further limit the claims. The claims are essentially the same composition claims as claim 11.
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.
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.
Claims 11-31, 33-35, 37-40, 41 are rejected under 35 U.S.C. 102(a)(1) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Anchel (WO 2016077457; IDS 07.25.25), and evidenced by Daly et al. (2005 J Mol Recognit 18: 119-138, published online November 26, 2004). Instant claim 11 and its dependent claims are product-by-process claims. See MPEP 2113. The instant specification discloses that a “host cell” for expression of recombinant ovalbumin is Pichia Pastoris (instant specification paragraphs 0568, 0953-0954, 0998-0999).
Anchel teaches recombinant expression of an ovalbumin (an egg white protein) in a host cell (at least example 1, paragraphs 0161-0164), where the host cell is Pichia pastoris (paragraphs 0165-0169), and purifying the recombinant protein, dialyzing with an aqueous buffer of appropriate pH to obtain the recombinant protein (paragraphs 0171-0174), where Anchel teaches the recombinant protein composition has an acidic pH 6 or neutral pH 7 (paragraph 0100). Therefore, Anchel can be deemed to teach a recombinant ovalbumin (rOVA) composition produced by the same process recited in instant claim 11, i.e. expressing a rOVA in a Pichia pastoris host cell, purifying the rOVA, etc. Since Anchel teaches a rOVA composition produced by the same expression system recited, the rOVA composition of Anchel can be deemed to comprise an rOVA comprising an N-glycan, wherein the N-glycan comprises 5-11 mannose units (instant claims 11-12, 31).
This is supported or evidenced by Daly et al., which teach Pichia pastoris glycosylation patterns where a core Man8GlcNAc2 is common to all the oligosaccharides (p. 129) and the number of mannose units range from 3-13, including 9-11 (p. 131).
Since the rOVA composition of Anchel is expressed and produced in the same host cell (i.e. a Pichia pastoris host cell) as the claimed rOVA composition, it would follow that the rOVA composition of Anchel necessarily comprises a rOVA comprising a N-glycan comprising 5-11 mannose units, including the recited mannose units, including 9-11, and glycosylation patterns (instant claims 11-14, 17, 28, 31, 33-35, 37).
Alternatively, it would be obvious to one of ordinary skill in the art before the effective filing date of the claimed invention that Anchel discloses a rOVA composition comprising a rOVA that reasonably appears to be identical to the claimed rOVA comprising a N-glycan comprising 5-11 mannose units, including the recited mannose units, including 9-11, and glycosylation patterns (instant claims 11-14, 17, 28, 31, 33-35, 37).
Regarding instant claims 15, 38, as noted above, Anchel teaches the rOVA composition is produced in a Pichia pastoris host cell (examples 1-3), where there is no galactose unit in the N-linked oligosaccharide produced in Pichia pastoris (Daly et al. p. 129). Therefore, Anchel can be deemed to teach and/or disclose that the N-linked glycan does not comprise a galactose unit.
Regarding instant claim 16, Anchel teaches and/or discloses that the recombinant egg white protein has a glycosylation, acetylation, or phosphorylation pattern different from the egg white protein in egg white (paragraphs 0011, 0061, 0089, 0169).
Regarding instant claim 18, as noted above, Anchel teaches the rOVA composition is produced in a Pichia pastoris host cell (examples 1-3), where it is known that the amino-terminal methionine residue is cleaved in recombinant proteins produced and expressed in Pichia pastoris (Daly et al. p. 126). Therefore, Anchel can be deemed to teach and/or disclose that the amino acid sequence of the rOVA lacks an N-terminal methionine.
Regarding instant claims 19-20, 22, 39-40, Anchel teaches and/or discloses that the recombinant egg white protein has improved properties, including foam strength, height, gelation, etc. (at least paragraphs 0018, 0081, 0133-0136, examples 6-10). Additionally, since Anchel teaches and/or discloses a rOVA composition comprising a rOVA that appears to be identical to the claimed rOVA, it would follow that the rOVA composition of Anchel necessarily comprises the same improved characteristics recited in the instant claims. “Products of identical chemical composition can not have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). MPEP 2112.01.
Regarding instant claim 21, Anchel teaches and/or discloses the amino acid sequence of chicken ovalbumin (SEQ ID NO: 1) (paragraphs 0040, also Fig. 1), which has 98.9% sequence identity and 99.7% local similarity with instant SEQ ID NO: 2, where instant SEQ ID NO: 2 is the amino acid sequence of chicken ovalbumin secreted from Pichia (instant specification p. 79 Table 1). As noted above, Anchel discloses the rOVA composition is produced in a Pichia pastoris host cell (examples 1-3). Therefore, Anchel can be deemed to teach and/or disclose that the rOVA produced in the Pichia pastoris host cell comprises the amino acid sequence of instant SEQ ID NO: 2.
Regarding instant claims 23-24, Anchel teaches and/or discloses that the purified recombinant ovalbumin composition is in an aqueous buffer solution (instant claim 24) or in a powdered composition (instant claim 23) (example 3, also paragraph 0174).
Regarding instant claim 25, Anchel teaches and/or discloses that the recombinant egg white protein composition is acidic, neutral or basic, including having a pH of about 6 (paragraph 0100).
Regarding instant claims 26-27, Anchel teaches and/or discloses that the recombinant egg white protein composition has a water percentage up to 5%, at least 80% protein by weight, less than 0.5% fat by weight (at least paragraphs 0098-0099).
Regarding instant claims 29-30, Anchel teaches and/or discloses a food composition or a baked good comprising the recombinant egg white protein composition (paragraph 0075, example 10).
Regarding instant claim 41, Anchel teaches and/or discloses further processing the purified recombinant egg white protein composition to obtain a powdered egg white protein composition (at least example 3).
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive.
Applicants assert that the record fails to establish that the references disclose the claimed rOVA composition comprising an N-glycan, with specifically an N-linked glycan profile of “5-11 mannose units” as presently amended. Applicants assert that MPEP 2112.01 notes that inherency…may not be established by probabilities or possibilities; the mere fact that a certain thing may result from a given set of circumstances is not sufficient. Applicants assert that Daly et al. state that there can be variability in the length and type of oligosaccharides present on glycoproteins (Daly et al. p. 131). Applicants assert that this comports with the knowledge of the ordinarily skilled artisan that recombinant proteins can exhibit heterogenous glycoform profiles.
Applicants’ remarks are not persuasive. MPEP 2112 notes that there is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the relevant time, but only that the subject matter is in fact inherent in the prior art reference. Schering Corp. v. Geneva Pharm. Inc., 339 F.3d 1373, 1377, 67 USPQ2d 1664, 1668 (Fed. Cir. 2003). In this instance, Anchel teaches obtaining a rOVA composition, which is the same recombinant protein composition recited in the instant claims, and teach that the rOVA is produced by a method or process comprising the same steps recited in the instant claims and disclosed in the specification (Anchel examples 1-3).
The instant specification discloses that a “host cell” for expression of recombinant ovalbumin is Pichia Pastoris (instant specification paragraphs 0568, 0953-0954, 0998-0999).
Anchel teaches recombinant expression of an ovalbumin (an egg white protein) in a host cell (at least example 1, paragraphs 0161-0164), where the host cell is Pichia pastoris (paragraphs 0165-0169), and purifying the recombinant protein, dialyzing with an aqueous buffer of appropriate pH to obtain the recombinant protein (paragraphs 0171-0174).
Since the prior art Anchel teaches the same protein claimed and that the rOVA composition is produced by the same expression system recited and same steps recited in instant claim 11, practicing the method of Anchel inherently results in producing a rOVA composition comprising a rOVA that is structurally the same as the claimed rOVA, where the rOVA inherently comprises an N-glycan comprising 5-11 mannose units.
While Daly et al. teach that there is considerable variability in the length and type of oligosaccharides present on glycoproteins (p. 131), Daly et al. teach that this structural heterogeneity is dependent on the characteristics of the target protein (p. 130-131). In this instance, the prior art Anchel teach producing the same target protein as the claimed protein, i.e. rOVA, in the same expression system Pichia pastoris of the claims and disclosed in the specification. Therefore, it would follow that the rOVA composition produced in Anchel comprises rOVA proteins having the same glycosylation features recited in the instant claims because the prior art teaches the same target protein is being produced in the same expression system and by the same conditions.
Regarding Applicants’ remarks that Daly et al. teach Pichia pastoris (P. pastoris) glycosylation patterns vary considerably (Daly et al. p. 131), the remarks are not persuasive. Daly et al. is teaching that the P. pastoris glycosylation patterns vary in regards to the target glycoprotein that is expressed in P. pastoris (p. 131). On page 131, Daly et al. report the number of mannose units and type of oligosaccharides for different target glycoproteins that have been expressed in P. pastoris. Daly et al. teach that the recombinant glycoproteins expressed in P. pastoris are heterogenous; however, Daly et al. teach that the number of mannose units of the expressed target proteins are within a noted range, including the recited 5-11 mannose units. Daly et al. teach that in alpha-amylase expressed in P. pastoris, the number of mannose units ranged from 3-11, with Man4-9GlcNAc2 being the most common form; recombinant aspartic protease expressed in P. pastoris was also found to contain mainly Man8-9GlcNAc2; alpha-lactalbumin had mostly Man9-12NAc2; mannose 6-phosphate receptor contained Man8-10GlcNAc2 and Man11-12GlcNAc2; type II membrane glycoprotein CD154 contained Man9-11 (p. 131).
It is known that the initial stage of glycosylation is similar in both yeast and mammalian cells, to give a core Man8GlcNAc2, before further processing (Daly et al. at least p. 129).
Therefore, Daly et al. teach Pichia pastoris glycosylation patterns where a core Man8GlcNAc2 is common to all the oligosaccharides (p. 129) and the number of mannose units range from 3-13, including 9-11, for expressed glycoproteins (p. 131).
Therefore, Daly et al. provide support and evidence that glycoproteins expressed and produced in Pichia pastoris comprise a N-glycan comprising mannose units that range from 3-13, including 9-11, which comprises the recited range of 5-11 mannose units and 9-11 mannose units.
This is further supported and evidenced by Ivey et al. (WO 2020041483; IDS 07.25.25), which teach and disclose that a recombinant egg white protein composition expressed in Pichia pastoris comprises Man7-9GlcNAc2, or 7-9 mannose units (p. 25-26 Table 1).
Therefore, Applicants’ remarks that Anchel does not anticipate the instant claims are not found persuasive. Since Anchel teaches producing the same target protein recited, i.e. rOVA, in the same expression system Pichia pastoris, and by the same steps recited, it would follow that the rOVA composition produced in Anchel inherently comprises rOVA proteins comprising N-glycans having the same mannose units as the claimed rOVA, including a rOVA comprising a N-glycan comprising 5, 6, 7, 8, 9, 10, and/or 11 mannose units.
Regarding the 103 rejection, Applicants assert that Daly et al. do not teach or suggest a specific N-linked glycan composition, let alone N-linked glycans of an rOVA protein. Applicants assert that instead Daly et al. state that Pichia pastoris (P. pastoris) glycosylation patterns vary considerably (Daly et al. p. 131).
Applicants’ remarks are not persuasive. Where applicant claims a composition in terms of a function, property or characteristic and the composition of the prior art is the same as that of the claim but the function is not explicitly disclosed by the reference, the examiner may make a rejection under both 35 U.S.C. 102 and 103. “There is nothing inconsistent in concurrent rejections for obviousness under 35 U.S.C. 103 and for anticipation under 35 U.S.C. 102.” In re Best, 562 F.2d 1252, 1255 n.4, 195 USPQ 430, 433 n.4 (CCPA 1977). MPEP 2112.
The reasons for maintaining Daly et al. as support and/or evidence are the same as noted above. Daly et al. teach Pichia pastoris glycosylation patterns where a core Man8GlcNAc2 is common to all the oligosaccharides (p. 129) and the number of mannose units range from 3-13, including 9-11, for expressed glycoproteins (p. 131). Daly et al. provide support and evidence that glycoproteins expressed and produced in Pichia pastoris comprise a N-glycan comprising mannose units that range from 3-13, including 9-11, which comprises the recited range of 5-11 mannose units and 9-11 mannose units. It would be obvious to one of ordinary skill in the art before the effective filing date of the claimed invention that Anchel discloses a rOVA composition comprising a rOVA that reasonably appears to be identical to the claimed rOVA comprising a N-glycan comprising 5-11 mannose units, including the recited mannose units, including 9-11, and glycosylation patterns (instant claims 11-14, 17, 28, 31, 33-35, 37).
Applicants assert that furthermore, additional references confirm that Pichia glycosylation may be heterogenous and unpredictable across proteins and even for a single protein. Applicants cite Schutter et al. and Dai et al. for support.
Applicants’ remarks are not persuasive. Schutter et al. and Dai et al., which teaching that Pichia glycosylation may be heterogenous and produce N-glycans having a range of mannose structures and isoforms, still do not teach away from the Pichia pastoris expression system having glycosylation patterns comprising a core Man8GlcNAc2 common to all the oligosaccharides (Daly et al. p. 129) and the number of mannose units ranging from 3-13, including 9-11, for expressed glycoproteins (Daly et al. p. 131).
As already noted, Daly et al. teach that structural heterogeneity is dependent on the characteristics of the target protein (p. 130-131). In this instance, the prior art Anchel teach producing the same target protein as the claimed protein, i.e. rOVA, in the same expression system Pichia pastoris of the claims and disclosed in the specification. Therefore, it would be obvious to one of ordinary skill in the art before the effective filing date of the claimed invention that Anchel discloses a rOVA composition comprising a rOVA that reasonably appears to be identical to the claimed rOVA comprising a N-glycan comprising 5-11 mannose units, including the recited mannose units, including 9-11, and glycosylation patterns.
This is further supported and evidenced by Ivey et al. (WO 2020041483; IDS 07.25.25), which teach and disclose that a recombinant egg white protein composition expressed in Pichia pastoris comprises Man7-9GlcNAc2, or 7-9 mannose units (p. 25-26 Table 1).
Regarding Applicants’ remarks that the claimed composition comprising rOVA exhibits a surprising ability to perform as well or better than native egg white, the remarks are not persuasive.
MPEP 716.01(c) notes that objective evidence which must be factually supported by an appropriate affidavit or declaration to be of probative value includes evidence of unexpected results, commercial success, solution of a long-felt need, inoperability of the prior art, invention before the date of the reference, and allegations that the author(s) of the prior art derived the disclosed subject matter from the inventor or at least one joint inventor. See, for example, In re De Blauwe, 736 F.2d 699, 705, 222 USPQ 191, 196 (Fed. Cir. 1984) ("It is well settled that unexpected results must be established by factual evidence." "[A]ppellants have not presented any experimental data showing that prior heat-shrinkable articles split. Due to the absence of tests comparing appellant's heat shrinkable articles with those of the closest prior art, we conclude that appellant's assertions of unexpected results constitute mere argument."). See also In re Lindner, 457 F.2d 506, 508, 173 USPQ 356, 358 (CCPA 1972); Ex parte George, 21 USPQ2d 1058 (Bd. Pat. App. & Inter. 1991).
Further, the arguments of counsel cannot take the place of evidence in the record. In re Schulze, 346 F.2d 600, 602, 145 USPQ 716, 718 (CCPA 1965). Examples of attorney statements which are not evidence and which must be supported by an appropriate affidavit or declaration include statements regarding unexpected results, commercial success, solution of a long-felt need, inoperability of the prior art, invention before the date of the reference, and allegations that the author(s) of the prior art derived the disclosed subject matter from the inventor or at least one joint inventor.
Further, MPEP 716.02(b) notes that Applicant has the burden to establish that the results are unexpected and significant. Evidence of unexpected properties may be in the form of a direct or indirect comparison of the claimed invention with the closest prior art which is commensurate in scope with the claims. See also MPEP 716.02(e) noting that the claimed subject matter has to be compared with the closest prior art to be effective to rebut a prima facie case of obviousness.
In this instance, Applicants have not provided a direct or indirect comparison of the claimed invention with the closest prior art which is commensurate in scope with the claims. The closest prior art is the rOVA composition produced by Pichia pastoris of Anchel (Anchel examples 1-3).
Regarding Applicants’ remarks on instant claims 12 and 33, the remarks are not persuasive for the reasons already noted. Since the rOVA composition of Anchel is expressed and produced in the same host cell (i.e. a Pichia pastoris host cell) as the claimed rOVA composition, it would follow that the rOVA composition of Anchel necessarily comprises a rOVA comprising a N-glycan comprising 5-11 mannose units, including the recited mannose units, including 9-11, and glycosylation patterns (instant claims 11-14, 17, 28, 31, 33-35, 37).
Regarding Applicants’ remarks on instant claims 15, 18, 19-20, 38, 39-40, the remarks are not persuasive for the reasons already noted. See also the 102/103 rejection above.
Claims 11, 17, 31, 33, 36 are rejected under 35 U.S.C. 103 as being unpatentable over Anchel (WO 2016077457; IDS 07.25.25, previously cited) in view of Kitabatake et al. (1993 Food Reviews International 9(4): 445-471; previously cited), and evidenced by Daly et al. (2005 J Mol Recognit 18: 119-138, published online November 26, 2004; previously cited). The teachings of Anchel over at least instant claims 11, 31, 33 are noted above.
Regarding instant claims 17, 36, Kitabatake et al. disclose that to improve the functional properties of food protein, physical and enzymatic treatments are effective and attractive (p. 445). Kitabatake et al. disclose dephosphorylated phosphoproteins is expected to improve the functionality of the protein (p. 469). Kitabatake et al. disclose treating ovalbumin by acid phosphatase (p. 469). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to dephosphorylate the rOVA produced by Pichia pastoris of Anchel noted above with a phosphatase as suggested in Kitabatake et al. The motivation to do so is given by Kitabatake et al., which disclose that the function of food proteins, such as ovalbumin, can be modified by enzymatic treatments, including dephosphorylation by phosphatase. One of ordinary skill would have a reasonable expectation of success because the prior art discloses that the function of food proteins can be modified by enzymes, including phosphatase.
Reply: Applicants’ amendments/remarks have been considered but they are not persuasive. The reasons for maintaining Anchel are the same as noted above. As already noted, since Anchel teaches producing the same target protein recited, i.e. rOVA, in the same expression system Pichia pastoris, and by the same steps recited, it would follow that the rOVA composition produced in Anchel inherently comprises rOVA proteins comprising N-glycans having the same mannose units as the claimed rOVA, including a rOVA comprising a N-glycan comprising 5, 6, 7, 8, 9, 10, and/or 11 mannose units.
Regarding Applicants’ remarks that Kitabatake et al. fail to address Pichia glycosylation or N-linked glycan profiles at all, the remarks are not persuasive. As already noted, since Anchel teaches producing the same target protein recited, i.e. rOVA, in the same expression system Pichia pastoris, and by the same steps recited, it would follow that the rOVA composition produced in Anchel inherently comprises rOVA proteins comprising N-glycans having the same mannose units as the claimed rOVA, including a rOVA comprising a N-glycan comprising 5, 6, 7, 8, 9, 10, and/or 11 mannose units.
Regarding Applicants’ remarks that Kitabatake et al. is directed to native ovalbumin and general food functionality, not to Pichia-expressed rOVA compositions having Applicants’ specific N-glycan profiles, the remarks are not persuasive. The deficiency of Kitabatake et al. to not teach a rOVA composition produced by Pichia pastoris and having the specific N-glycan profiles recited is remedied by Anchel. As already noted, Anchel teaches producing the same target protein recited, i.e. rOVA, in the same expression system Pichia pastoris, and by the same steps recited, it would follow that the rOVA composition produced in Anchel inherently comprises rOVA proteins comprising N-glycans having the same mannose units as the claimed rOVA, including a rOVA comprising a N-glycan comprising 5, 6, 7, 8, 9, 10, and/or 11 mannose units. Anchel teaches a rOVA protein having the same purpose as the OVA protein of Kitabatake et al., i.e. having function as a food protein. Therefore, it would have been obvious to dephosphorylate the rOVA produced by Pichia pastoris of Anchel noted above with a phosphatase as suggested in Kitabatake et al. because Kitabatake et al. disclose that the function of food proteins, such as ovalbumin, can be modified by enzymatic treatments, including dephosphorylation by phosphatase, to improve its functionality.
For at least these reasons, the 103 rejection is maintained.
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 11-31, 33-40, 41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 19 of U.S. Patent No. 11718644 (‘644) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘644 patent claim are drawn to a composition comprising a rOVA protein. The ‘644 patent claims recite the composition comprises a purified recombinant protein. The ‘644 specification discloses that the recombinant protein is a recombinant chicken OVA produced and expressed by a Pichia pastoris host cell. Since the recombinant protein composition of the ‘644 patent claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘644 patent claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘644 patent claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
Claims 11-31, 33-40, 41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 8-13 of U.S. Patent No. 11518797 (‘797) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘797 patent claims are drawn to a composition comprising a rOVA protein. The ‘797 patent claim 9 recites the composition comprises a recombinant ovalbumin protein. The ‘797 specification discloses that the recombinant protein is a recombinant chicken OVA produced and expressed by a Pichia pastoris host cell. Since the recombinant protein composition of the ‘797 patent claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘797 patent claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘797 patent claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
Claims 11-31, 33-40, 41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15, 17-18 of U.S. Patent No. 11279748 (‘748) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘748 patent claims are drawn to a composition comprising a rOVA protein. The ‘748 patent claims 1-2 recite the composition comprises a recombinant ovalbumin protein. The ‘748 patent claims 11-12 recite that the recombinant protein is a recombinant rOVA produced and expressed by a Pichia pastoris host cell. The ‘748 specification discloses the rOVA is chicken OVA. Since the recombinant protein composition of the ‘748 patent claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘748 patent claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘748 patent claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
Claims 11-31, 33-40, 41 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 15-18, 22-23, 25-30, 32-53 of copending Application No. 18455552 (‘552) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘552 application claim are drawn to a composition comprising a rOVA protein. The ‘552 application claim 15 recite the composition comprises a recombinant ovalbumin protein and the ‘552 application claims 26, 36 recite that the recombinant protein is a recombinant rOVA produced and expressed by a Pichia pastoris host cell. The ‘552 specification discloses the rOVA is chicken OVA. Since the recombinant protein composition of the ‘552 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘552 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘552 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 11-31, 33-40, 41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 8-30 of U.S. Patent No. 12096784 (‘784) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘784 patent claims are drawn to a composition comprising a rOVA protein. The ‘784 patent claim 8 recites the composition comprises a recombinant ovalbumin protein. The ‘784 patent claim 16 recites that the recombinant protein is a recombinant rOVA produced and expressed by a Pichia pastoris host cell. The ‘784 specification discloses the rOVA is chicken OVA. Since the recombinant protein composition of the ‘784 patent claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘784 patent claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘784 patent claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
Claims 11-31, 33-40, 41 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 33-72 of copending Application No. 18766643 (‘643) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘643 application claim are drawn to a composition comprising a rOVA protein comprising a N-glycan comprising 11 or fewer mannose units and having the same mannose units and glycosylation patterns. The ‘643 specification also discloses the rOVA is chicken OVA. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘643 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 11-31, 33-40, 41 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 48-49, 51, 54 of copending Application No. 18907140 (‘140) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘140 application claim are drawn to a composition comprising a rOVA protein. The ‘140 application claims recite the composition comprises a recombinant protein. The ‘140 specification discloses that the recombinant protein is a recombinant chicken OVA produced and expressed by a Pichia pastoris host cell. Since the recombinant protein composition of the ‘140 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘140 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘140 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 11-31, 33-40, 41 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 51-52 of copending Application No. 18903982 (‘982) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘982 application claim are drawn to a composition comprising a rOVA protein. The ‘982 application claims recite the composition comprises a recombinant protein. The ‘982 specification discloses that the recombinant protein is a recombinant chicken OVA produced and expressed by a Pichia pastoris host cell. Since the recombinant protein composition of the ‘982 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘982 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘982 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 11-31, 33-40, 41 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-27, 30 of copending Application No. 19399116 (‘116) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘116 application claim are drawn to a composition comprising a rOVA protein. The ‘116 application claim 1 recites the composition comprises a recombinant ovalbumin protein and the ‘116 application claims 26-27 recite that the recombinant ovalbumin is produced and/or expressed by a Pichia host cell. The ‘116 specification discloses the rOVA is chicken OVA. Since the recombinant protein composition of the ‘116 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘116 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘116 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 11-31, 33-40, 41 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of copending Application No. 18761860 (‘860) (reference application) in view of Anchel (supra) and Daly et al. (supra). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘860 application claim are drawn to a composition comprising a rOVA protein. The ‘860 application claim 1 recites the composition comprises a recombinant ovalbumin protein, claim 7 recites the recombinant ovalbumin is a chicken ovalbumin, and claims 15-16 recite that the recombinant ovalbumin is produced and/or expressed by a Pichia host cell. The ‘860 specification discloses the rOVA is chicken OVA. Since the recombinant protein composition of the ‘860 application claims reasonably comprises the same protein expressed and produced in the same host cell as the instant claims, it would follow that the recombinant protein composition of the ‘860 application claims comprising rOVA necessarily comprises a N-glycan comprising 11 or fewer mannose units, including the recited mannose units and glycosylation patterns. Additionally, any features and/or components of the instant rOVA composition not expressly recited in the ‘860 application claims are reasonably remedied by the teachings of Anchel and/or Daly et al. noted above.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reply: Applicants’ remarks regarding the nonstatutory double patenting have been considered but they are not persuasive. The reasons for maintaining Anchel and Daly et al. are the same as noted above.
No claim is allowed.
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/Marsha Tsay/Primary Examiner, Art Unit 1656