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
2. Claims 47-61 are pending and currently under prosecution.
Priority
3. Applicant’s claim under 35 U.S.C. §§ 121 and 365(c) for benefit of the earlier filing date of applications, is acknowledged.
4. Receipt is acknowledged of papers submitted under 35 U.S.C. 119(a)-(d), which papers have been placed of record in the file of 16/648,636.
Claim Interpretation
The following is a quotation of 35 U.S.C. 112(f):
(f) Element in Claim for a Combination. – An element in a claim for a combination may be expressed as a means or step for performing a specified function without the recital of structure, material, or acts in support thereof, and such claim shall be construed to cover the corresponding structure, material, or acts described in the specification and equivalents thereof.
The following is a quotation of pre-AIA 35 U.S.C. 112, sixth paragraph:
An element in a claim for a combination may be expressed as a means or step for performing a specified function without the recital of structure, material, or acts in support thereof, and such claim shall be construed to cover the corresponding structure, material, or acts described in the specification and equivalents thereof.
This application includes one or more claim limitations that do not use the word “means,” but are nonetheless being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, because the claim limitation(s) uses a generic placeholder that is coupled with functional language without reciting sufficient structure to perform the recited function and the generic placeholder is not preceded by a structural modifier. Such claim limitation(s) is/are: “generating an antibody-payload conjugate by means of a microbial transglutaminase (MTG)” in claim 47.
Because this/these claim limitation(s) is/are being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, it/they is/are being interpreted to cover the corresponding structure described in the specification as performing the claimed function, and equivalents thereof.
If applicant does not intend to have this/these limitation(s) interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, applicant may: (1) amend the claim limitation(s) to avoid it/them being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph (e.g., by reciting sufficient structure to perform the claimed function); or (2) present a sufficient showing that the claim limitation(s) recite(s) sufficient structure to perform the claimed function so as to avoid it/them being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph.
Claim Rejections - 35 USC § 112
7. The following is a quotation 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.
8. The following is a quotation of 35 U.S.C. 112 (pre-AIA ), first paragraph:
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.
9. Claims 47-61 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
This is a “written description” rejection.
The considerations that are made in determining whether a claimed invention is supported by an adequate written description are outlined by the published Guidelines for Examination of Patent Applications Under the 35 U.S.C. 112, para. 1, ``Written Description'' Requirement (Federal Register; Vol. 66, No. 4, January 5, 2001; The 2015 Written Description Workshop materials; hereinafter “Guidelines”).
These guidelines state that rejection of a claim for lack of written description, where the claim recites the language of an original claim should be rare. Nevertheless, these guidelines further state, “the issue of a lack of written description may arise even for an original claim when an aspect of the claimed invention has not been described with sufficient particularity such that one skilled in the art would recognize that the applicant has possession of the claimed invention” (Id. at 1105). The “Guidelines” continue:
The claimed invention as a whole may not be adequately described if the claims require an essential or critical feature which is not adequately described in the specification and which is not conventional in the art or known to one of ordinary skill in the art. This problem may arise where an invention is described solely in terms of a method of its making coupled with its function and there is no described or art-recognized correlation or relationship between the structure of the invention and its function. 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.
With further regard to the proposition that, as original claims, the claims themselves provide in haec verba support sufficient to satisfy the written description requirement, the Federal Circuit has explained that in ipsis verbis support for the claims in the specification does not per se establish compliance with the written description requirement:
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. The disclosure must allow one skilled in the art to visualize or recognize the identity of the subject matter purportedly described. Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
Regents of the University of California v. Eli Lilly & Co., 119 F.3d 1559, 43 USPQ2d 1398 (Fed. Cir. 1997). See also: University of Rochester v. G.D. Searle & Co., 69 USPQ2d 1886 1892 (CA FC 2004).
Thus, an original claim may provide written description for itself, but it must still be an adequate written description, which establishes that the inventor was in possession of the invention.
In this instance, claims 47-61 are drawn to a method comprises an antibody conjugate comprising a linker having the peptide structure (Aax)-(Aax)-(Aax)-B-(Aax), wherein Aax can be any naturally or non-naturally occurring amino acid.
The specification teaches linkers shown in Table 5; see Table 5.
Thus, the claims are drawn to a genus of linkers having the peptide structure (Aax)-(Aax)-(Aax)-B-(Aax)， wherein Aax can be any naturally or non-naturally occurring amino acid.
Although the specification teaches linkers shown in Table 5; however, the specification does not teach that linkers having the peptide structure (Aax)-(Aax)-(Aax)-B-(Aax), wherein Aax can be any naturally or non-naturally occurring amino acid would have or retain the activity or function of the linkers shown in Table 5.
Given the fact that the claims are drawn to a genus of linkers having the peptide structure (Aax)-(Aax)-(Aax)-B-(Aax), wherein Aax can be any naturally or non-naturally occurring amino acid, which have no particular function or activity, there is no correlation between any one particularly identifying structural feature and any one particularly identifying functional feature. Consequently, it is submitted that the skilled artisan could not immediately envision, recognize or distinguish at least a substantial number of linkers having the peptide structure (Aax)-(Aax)-(Aax)-B-(Aax), wherein Aax can be any naturally or non-naturally occurring amino acid, to which the claims are directed.
Although the specification teaches linkers shown in Table 5, linkers shown in Table 5 are not reasonably representative of the plurality of linkers having the peptide structure (Aax)-(Aax)-(Aax)-B-(Aax), wherein Aax can be any naturally or non-naturally occurring amino acid. This is largely because each linker having the peptide structure (Aax)-(Aax)-(Aax)-B-(Aax), wherein Aax can be any naturally or non-naturally occurring amino acid, has substantially varying structure and need not have any particular function or activity.
Guidelines states, “[p]ossession may be shown in a variety of ways including description of an actual reduction to practice, or by showing the invention was ‘ready for patenting’ such as by disclosure of drawings or structural chemical formulas that show that the invention was complete, or by describing distinguishing identifying characteristics sufficient to show that the applicant was in possession of the claimed invention” (Id. at 1104). “Guidelines” further states, “[f]or inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus” (Id. at 1106); accordingly, it follows that an adequate written description of a genus cannot be achieved in the absence of a disclosure of at least one species within the genus. Moreover, because the claims encompass a genus of linkers having the peptide structure (Aax)-(Aax)-(Aax)-B-(Aax), wherein Aax can be any naturally or non-naturally occurring amino acid, which vary both structurally and functionally, an adequate written description of the claimed invention must include sufficient description of at least a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics sufficient to show that Applicant was in possession of the claimed genus. In this instance, factual evidence of an actual reduction to practice has not been disclosed by Applicant in the specification; Applicant has not shown the invention was “ready for patenting” by disclosure of drawings or structural chemical formulas that show that the invention was complete; and Applicant has not described distinguishing identifying characteristics sufficient to show that Applicant was in possession of the claimed invention at the time the application was filed.
Thus, it is submitted that the instant claims, and the disclosure describing the claimed subject matter, fails to satisfy the written description requirement set forth under 35 U.S.C. § 112, first paragraph.
10. 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 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.
Claim Rejections - 35 USC § 102
11. 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.
12. Claims 47-61 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Bregeon et al. (WO 2014202775, published on 24 December 2014, IDS).
Claims 47-61 are herein drawn to a method for generating an antibody-payload conjugate by a microbial transglutaminase (MTG), the method comprises a step of conjugating a linker having a primary amine residue, said linker having the peptide structure (shown in N->C direction):
NH2 (Aax)m-(Aax)-(Aax)n-B-(Aax)o, or NH2 (Aax)m-B-(Aax)n-(Aax)-(Aax)o,
wherein: m is an integer between ≥ 0 and ≤12, n is an integer between ≥ 0 and ≤12, o is an integer between ≥ 0 and ≥12, m+n+o≥0
Aax can be any naturally or non-naturally occurring L- or D-amino acid, and
B is a payload or a linking moiety, and
wherein NH2-Aax is an amino acid.
Bregeon et al. teach a method comprising lysine-based linkers for use in conjugation to glutamine amino acid residues present in native antibodies using a bacterial transglutaminase (TGase) (see entire document, e.g. pages 2, 5, 9, 33, 75, example 9 on pages 127-129), following conjugation, additional attachment of a toxic moiety is disclosed (see page 129, lines 12-20).
For claim 49, Bregeon et al. teach non-cleavable linker; see Table 2.
For claim 50, Bregeon et al. teach the linker is di- or tri-or oligo peptide (see Table 2) which meet the limitation of m + n + o ≤ 25.
For claim 51, Bregeon et al. teach the antibodies that are to be conjugated to the lysine-based linker at glutamine residue Q295; see page 75-lines 5-8.
For claims 52 and 54, Bregeon et al. teach N297-glycosylated antibodies; see page 46-line 7.
For claim 53, the lysine-based linkers of Bregeon et al. are positively charged amino acid residue.
For claims 55 and 57, Bregeon et al. teach the toxin is auristatins (e.g., MMAE, MMAF); see page 5.
For claim 56, Bregeon et al. teach the lysine-based linker comprising a reactive moiety R’, wherein the R’ comprising bioorthogonal-reaction compatible reactive group, e.g., azide (-N3), thiol (-SH); see page 76-lines 18-34.
For claim 58, Bregeon et al. teach the antibody's isotype as IgM, IgD, IgG, IgA, or IgE; see page 34-lines 32-35.
For claims 59-61, Bregeon et al. teach two or more linking moieties (e.g., V, Y) and two or more therapeutic moieties (e.g., (Z)z); see claim 9.
Double Patenting
13. 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 claims at issue 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); and 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 a nonstatutory double patenting ground provided the reference application or patent either is shown to be commonly owned with this application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO internet Web site contains terminal disclaimer forms which may be used. Please visit http://www.uspto.gov/forms/. The filing date of the application will determine what form 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 http://www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
14. Claims 47-61 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 9,764,038. Although the conflicting claims are not identical, they are not patentably distinct from each other because for the following reasons:
Claims 47-61 are herein drawn to a method for generating an antibody-payload conjugate by a microbial transglutaminase (MTG), the method comprises a step of conjugating a linker having a primary amine residue, said linker having the peptide structure (shown in N->C direction):
NH2 (Aax)m-(Aax)-(Aax)n-B-(Aax)o, or NH2 (Aax)m-B-(Aax)n-(Aax)-(Aax)o,
wherein: m is an integer between ≥ 0 and ≤12, n is an integer between ≥ 0 and ≤12, o is an integer between ≥ 0 and ≥12, m+n+o≥0
Aax can be any naturally or non-naturally occurring L- or D-amino acid, and
B is a payload or a linking moiety, and
wherein NH2-Aax is an amino acid.
Claims 1-13 of U.S. Patent No. 9,764,038 are drawn to a method for attaching a lysine-based linker to an antibody, comprising: a) providing a human or humanized antibody comprising one or more solvent exposed glutamine residues in a variable region and at least one acceptor glutamine residue in a constant region or in a sequence fused to a constant region or fused to a variable region, wherein said one or more solvent exposed glutamine residues are present in a light chain variable domain (VL) CDR at a Kabat position selected from the group consisting of 27, 55, and a combination thereof; and b) reacting said antibody with a lysine-based linker in the presence of a transglutaminase, under conditions permitting said lysine-based linker to be covalently linked to said at least one acceptor glutamine residue in a constant region or in a sequence fused to a constant region or fused to a variable region in said human or humanized antibody; the method further comprising reacting the antibody with a compound, wherein the compound is auristatins.
15. Claims 47-61 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-23 of U.S. Patent No. 11,396,649. Although the conflicting claims are not identical, they are not patentably distinct from each other because for the following reasons:
Claims 47-61 are herein drawn to a method for generating an antibody-payload conjugate by a microbial transglutaminase (MTG), the method comprises a step of conjugating a linker having a primary amine residue, said linker having the peptide structure (shown in N->C direction):
NH2 (Aax)m-(Aax)-(Aax)n-B-(Aax)o, or NH2 (Aax)m-B-(Aax)n-(Aax)-(Aax)o,
wherein: m is an integer between ≥ 0 and ≤12, n is an integer between ≥ 0 and ≤12, o is an integer between ≥ 0 and ≥12, m+n+o≥0
Aax can be any naturally or non-naturally occurring L- or D-amino acid, and
B is a payload or a linking moiety, and
wherein NH2-Aax is an amino acid.
Claims 1-23 of U.S. Patent No. 11,396,649 are drawn to a method for the conjugation of a peptide linker comprising a lysine and/or a glutamine residue to an antibody, or an antigen-binding fragment thereof, using a microbial transglutaminase (MTG), the method comprising: a) mixing the antibody, or the antigen-binding fragment thereof, the peptide linker and the MTG within a fluid under determined conditions, thereby conjugating the peptide linker to the antibody, or the antigen-binding fragment thereof, under the catalyzing effect of the MTG, wherein the antibody is deglycosylated or non-glycosylated containing a mutation at residue N297; and b) extracting the conjugate obtained in step (a) from the fluid, wherein the peptide linker further comprises a toxin, wherein the toxin is MMAE.
16. Claims 47-61 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-22 of U.S. Patent No. 10,132,799. Although the conflicting claims are not identical, they are not patentably distinct from each other because for the following reasons:
Claims 47-61 are herein drawn to a method for generating an antibody-payload conjugate by a microbial transglutaminase (MTG), the method comprises a step of conjugating a linker having a primary amine residue, said linker having the peptide structure (shown in N->C direction):
NH2 (Aax)m-(Aax)-(Aax)n-B-(Aax)o, or NH2 (Aax)m-B-(Aax)n-(Aax)-(Aax)o,
wherein: m is an integer between ≥ 0 and ≤12, n is an integer between ≥ 0 and ≤12, o is an integer between ≥ 0 and ≥12, m+n+o≥0
Aax can be any naturally or non-naturally occurring L- or D-amino acid, and
B is a payload or a linking moiety, and
wherein NH2-Aax is an amino acid.
Claims 1-22 of U.S. Patent No. 10,132,799 are drawn to a method for evaluating antibodies, comprising: a) providing a first and second antibody sample each comprising a plurality of antibodies comprising at least one acceptor glutamine residue (Q) in a constant region, wherein the first and second antibody-containing samples differ from one another with respect to antibody variable region sequence, and wherein substantially all of the antibodies present in the first sample are of the same sequence and substantially all of the antibodies present in the second sample are of the same sequence; b) (i) reacting each of said first and second antibody sample with a lysine-based linker comprising a reactive group (R), in the presence of a transglutaminase (TGase), under conditions sufficient such that antibodies in said first and second antibody samples are conjugated to a lysine-based linker comprising the reactive group (R); and (ii) further reacting the resulting antibodies of process (i) with a compound comprising: (a) a reactive group (R′) that reacts with reactive group (R) on the lysine-based linker, and (b) a moiety-of-interest (Z), whereby a first and a second antibody sample each conjugated to a lysine-based linker comprising the moiety-of-interest (Z) is obtained; and c) evaluating antibodies of the first and second antibody sample each conjugated to the lysine-based linker comprising a moiety-of-interest (Z) obtained in process (b) for a characteristic of interest, wherein: (i) the first and second antibody samples are specific for the same antigen, (ii) at least 90% of the antibodies in each of the first and second antibody samples obtained in process (b) have the same number of functionalized acceptor glutamine residues (Q) per antibody, wherein each of the functionalized acceptor glutamines are conjugated to a lysine-based linker comprising a moiety of interest, and (iii) the moiety-of-interest (Z) is selected from the group consisting of a hydrophobic organic compound, an organic compound having an electrically negative charge, an organic compound having a molecular weight of at least 400 g/mol, and any combination thereof, wherein Z is auristatins, wherein at least one of the functionalized acceptor glutamine residues is a glutamine residue substituted into an antibody heavy chain at position 297 according to EU numbering convention.
17. Claims 47-61 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 10,434,180. Although the conflicting claims are not identical, they are not patentably distinct from each other because for the following reasons:
Claims 47-61 are herein drawn to a method for generating an antibody-payload conjugate by a microbial transglutaminase (MTG), the method comprises a step of conjugating a linker having a primary amine residue, said linker having the peptide structure (shown in N->C direction):
NH2 (Aax)m-(Aax)-(Aax)n-B-(Aax)o, or NH2 (Aax)m-B-(Aax)n-(Aax)-(Aax)o,
wherein: m is an integer between ≥ 0 and ≤12, n is an integer between ≥ 0 and ≤12, o is an integer between ≥ 0 and ≥12, m+n+o≥0
Aax can be any naturally or non-naturally occurring L- or D-amino acid, and
B is a payload or a linking moiety, and
wherein NH2-Aax is an amino acid.
Claims 1-13 of U.S. Patent No. 10,434,180 are drawn to a method for conjugating a hydrophobic compound to an antibody, comprising: a) providing an antibody having at least one acceptor glutamine residue, wherein the residue at position 297 of the antibody according to Kabat numbering is not glycosylated; b) reacting said antibody with a linker comprising a primary amine and a reactive group (R), in the presence of a transglutaminase (TGase), under conditions sufficient to obtain an antibody comprising an acceptor glutamine linked to a reactive group (R) via said linker, wherein the reaction mixture is free of organic solvent or contains less than 10% (v/v) organic solvent; and (c) reacting, in the presence of at least 5% (v/v) organic solvent: (i) an antibody of process (b) comprising an acceptor glutamine linked to a reactive group (R) via said linker, with (c) (ii) a compound comprising a moiety of interest (Z), wherein (Z) is a hydrophobic compound selected from the group consisting of auristatins, dolastatins, duocarmycins, maytansanoids, and pyrrolobenzodiazepine, and a reactive group (R′) capable of reacting with reactive group R, under conditions sufficient to obtain an antibody comprising an acceptor glutamine linked to moiety of interest (Z) via said linker, wherein R and R′ is each a moiety comprising a bioorthogonal-reaction compatible reactive group selected from an azide and a strained alkene.
18. Claims 47-61 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-27 of copending Application No. 18/426675. Although the conflicting claims are not identical, they are not patentably distinct from each other for the following reasons:
Claims 47-61 are herein drawn to a method for generating an antibody-payload conjugate by a microbial transglutaminase (MTG), the method comprises a step of conjugating a linker having a primary amine residue, said linker having the peptide structure (shown in N->C direction):
NH2 (Aax)m-(Aax)-(Aax)n-B-(Aax)o, or NH2 (Aax)m-B-(Aax)n-(Aax)-(Aax)o,
wherein: m is an integer between ≥ 0 and ≤12, n is an integer between ≥ 0 and ≤12, o is an integer between ≥ 0 and ≥12, m+n+o≥0
Aax can be any naturally or non-naturally occurring L- or D-amino acid, and
B is a payload or a linking moiety, and
wherein NH2-Aax is an amino acid.
Claims 1-27 of copending Application No. 18/426675 are drawn to a method for conjugating a peptide linker comprising a lysine and/or a glutamine residue to an antibody, or an antigen-binding fragment thereof, by a microbial transglutaminase (MTG) the method comprising: a) mixing the antibody, or the antigen-binding fragment thereof, the peptide linker and the MTG within a fluid under determined conditions, thereby conjugating the peptide linker to the antibody, or the antigen-binding fragment thereof, under the catalyzing effect of the MTG, wherein the peptide linker is mixed with the antibody, or the antigen-binding fragment thereof, at a 0.5x to 50x molar ratio; and b) extracting the conjugate obtained in step (a) from the fluid, wherein the peptide linker further comprises a toxin, wherein the toxin is MMAE.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
Conclusion
19. No claim is allowed.
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/YAN XIAO/Primary Examiner, Art Unit 1642
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