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 .
2. Applicant’s response filed on 01/29/2026 is acknowledged.
3. Claims 1-17 and 20 are pending. Claim 1 is independent.
4. Applicant’s election without traverse of Group I in the reply filed on 01/29/2026 is acknowledged.
5. Claims 12-17 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected Group, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 01/29/2026.
6. Claims 1-11 and 20 are pending and under consideration for their full scope.
7. Applicant’s IDS documents filed on 03/24/2023 and 12/04/2024 have been considered.
Claim Objections
8. Claims 3 and 5 objected to because of the following informalities: Claim 3 recites “a amino acid sequence” in line 4 and claim 5 recites “a amino acid sequence” in line 3. This is not proper grammar.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
9. The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
10. Claims 6-7, 10 and 20 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
A. Claim 6 recites the limitation "the recombinant Ab" in line 8. There is insufficient antecedent basis for this limitation in the claim.
B. Claim 6 recites in lines 10-16 that the variable regions comprise a portion of the constant region. This recitation is indefinite because the variable region and constant regions are separate and the variable region does not comprise constant region.
C. Claim 7 recites the limitation "the recombinant Ab" in line 2. There is insufficient antecedent basis for this limitation in the claim.
D. Claim 7 recites that (c) the immunoglobulin light chain variable region further comprises at least a portion of a light chain constant region; (d) the immunoglobulin heavy chain variable region further comprises at least a portion of an immunoglobulin heavy chain constant region; (e) the immunoglobulin light chain variable region further comprises at least a portion of an immunoglobulin light chain constant region; and, the immunoglobulin heavy chain variable region further comprises at least a portion of an immunoglobulin heavy chain constant region. Antibody variable regions do not comprise constant regions.
E. Claim 10 recites “the recombinant antibody” in line 3. There is insufficient antecedent basis for this limitation in claim 7 which itself lacks antecedent basis for the term.
F. Claim 20 recites “a chimeric or recombinant antibody of claim 1” in line 1. There is insufficient antecedent basis for this limitation in claim 1.
Correction is required.
11. 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.
12. Claims 2-11 and 20 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.
Claim 1 requires an antibody or antigen binding fragment thereof that comprises 6 CDRs.
Claim 2 recites that the antibody is a single domain antibody or a single variable region of an Ab heavy or Ab light chain. This is not further limiting to claim 1.
Claim 4 recites that the heavy chain variable region comprises one of more substitutions. One or more additional substitutions to the antibody of claim 3 will not be further limiting to the antibody of claim 3 because it will neither be SEQ ID NO:1 nor 95% identical to SEQ ID NO:1.
Claim 6 recites that the antibody has 2-15 conservative amino acid substitutions. SEQ ID No:1 is 117 amino acids and SEQ ID NO:2 is 112 amino acids. 15 amino acid changes in a 122 or 117 amino acid polypeptide would not be 95% sequence identical to either or SEQ ID NOs 1 or 2. In addition, the claim language makes it possible to alter the sequence within the CDRs and that is not further limiting to claims 1, 3 and 5 upon which claim 6 depends.
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.
13. 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.
14. Claims 2-11 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for: an isolated or purified antibody (Ab), or antigen (Ag) binding fragment thereof, or monomeric or dimeric antigen binding protein (ABP), capable of specifically binding a human CD10 polypeptide, wherein the isolated or purified Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP comprises:(a) an immunoglobulin heavy chain variable region comprising CDR1 amino acid (aa) residues GYTFTDYF (residues 26-33 of SEQ ID NO: 1), CDR2 aa residues INPNNGDT (residues 51 to 58 of SEQ ID NO:1), and CDR3 aa residues AKGGFNPGDY (residues 97-106 of SEQ ID NO:1), and, (b) an immunoglobulin light chain variable region comprising CDR1 amino acid (aa) residues QSLVHRNGNTY (residues 27-37 of SEQ ID NO:2), CDR2 aa residues KVS (residues 55 to 57 of SEQ ID NO:2), and CDR3 aa residues SQSTHVPLT (residues 94-102 of SEQ ID NO:2); wherein the antibody comprises sequences which are 95% identical to SEQ ID NOs 1 and 2 including wherein the antibody comprises SEQ ID NOs 1 and 2 of CD10Mab 3124.
the specification does not reasonably provide enablement for: an isolated or purified antibody (Ab), or antigen (Ag) binding fragment thereof, or monomeric or dimeric antigen binding protein (ABP), capable of specifically binding a human CD10 polypeptide, wherein the isolated or purified Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP comprises:(a) an immunoglobulin heavy chain variable region comprising CDR1 amino acid (aa) residues GYTFTDYF (residues 26-33 of SEQ ID NO: 1), CDR2 aa residues INPNNGDT (residues 51 to 58 of SEQ ID NO:1), and CDR3 aa residues AKGGFNPGDY (residues 97-106 of SEQ ID NO:1), and, (b) an immunoglobulin light chain variable region comprising CDR1 amino acid (aa) residues QSLVHRNGNTY (residues 27-37 of SEQ ID NO:2), CDR2 aa residues KVS (residues 55 to 57 of SEQ ID NO:2), and CDR3 aa residues SQSTHVPLT (residues 94-102 of SEQ ID NO:2) wherein the antibody is a single domain antibody or single variable region of the heavy and light chain of claim 2; wherein the heavy chain variable region comprises a amino acid sequence SEQ ID NO:1 of claim 3; wherein the immunoglobulin heavy chain variable region comprises one or more conservative amino acid substitutions of claim 4; wherein the light chain variable region comprises a amino acid sequence SEQ ID NO:2 of claim 5; wherein:(a) the immunoglobulin heavy chain variable region and/or immunoglobulin light chain variable region comprise one or more conservative amino acid substitutions; (b) SEQ ID NO:1 or SEQ ID NO:2 has two, three, four, five, six, seven, eight, nine, ten, eleven, twelve thirteen, fourteen or fifteen conservative amino acid substitutions, and the recombinant Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP retains its ability to specifically bind to a human CD10 protein or polypeptide (c) the immunoglobulin light chain variable region further comprises at least a portion of a light chain constant region; (d) the immunoglobulin heavy chain variable region further comprises at least a portion of an immunoglobulin heavy chain constant region; (e) the immunoglobulin light chain variable region further comprises at least a portion of an immunoglobulin light chain constant region; and, the immunoglobulin heavy chain variable region further comprises at least a portion of an immunoglobulin heavy chain constant region of claim 6 and wherein the recombinant Ab, the Ag binding fragment thereof, or monomeric or dimeric ABP, or the heavy chain constant region, or the light chain constant region, or the heavy chain constant region and the light chain constant region, further comprises or is bound to a heterologous protein, peptide, or a compound or a composition of claim 7; and claims dependent thereupon of claims 8-11. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and or use the invention commensurate in scope with the claims. The specification disclosure does not enable one skilled in the art to practice the invention without an undue amount of experimentation.
Factors to be considered in determining whether undue experimentation is required to practice the claimed invention are summarized In re Wands (858 F2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988)). The factors most relevant to this rejection are the scope of the claim, the amount of direction or guidance provided, the lack of sufficient working examples, the unpredictability in the art and the amount of experimentation required to enable one of skill in the art to practice the claimed invention.
The specification discloses the anti-CD10 antibodies comprising SEQ ID NOs 1 and 2; for use in the claimed invention.
The specification is not enabled for making and using the isolated or purified antibody wherein the antibody is a single domain antibody or single variable region of the heavy and light chain of claim 2; wherein the heavy chain variable region comprises a amino acid sequence SEQ ID NO:1 of claim 3; wherein the immunoglobulin heavy chain variable region comprises one or more conservative amino acid substitutions of claim 4; and wherein the light chain variable region comprises a amino acid sequence SEQ ID NO:2 of claim 5; wherein:(a) the immunoglobulin heavy chain variable region and/or immunoglobulin light chain variable region comprise one or more conservative amino acid substitutions; (b) SEQ ID NO:1 or SEQ ID NO:2 has two, three, four, five, six, seven, eight, nine, ten, eleven, twelve thirteen, fourteen or fifteen conservative amino acid substitutions, and the recombinant Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP retains its ability to specifically bind to a human CD10 protein or polypeptide or (c) the immunoglobulin light chain variable region further comprises at least a portion of a light chain constant region; (d) the immunoglobulin heavy chain variable region further comprises at least a portion of an immunoglobulin heavy chain constant region; (e) the immunoglobulin light chain variable region further comprises at least a portion of an immunoglobulin light chain constant region; and, the immunoglobulin heavy chain variable region further comprises at least a portion of an immunoglobulin heavy chain constant region of claim 6; and wherein the recombinant Ab, the Ag binding fragment thereof, or monomeric or dimeric ABP, or the heavy chain constant region, or the light chain constant region, or the heavy chain constant region and the light chain constant region, further comprises or is bound to a heterologous protein, peptide, or a compound or a composition.
The specification is not enabled for making and using the isolated or purified antibody wherein the antibody is a single domain antibody or single variable region of the heavy and light chain of claim 2 is not enabled because the specification has not disclosed any single domain antibodies or single variable region antibodies which can bind to CD10.
The specification is not enabled for antibodies wherein the heavy chain variable region comprises “a” amino acid sequence SEQ ID NO:1 or “a” amino acid sequence SEQ ID NO:2. This claim recitation is not proper grammar and the language opens up the claims to read on any sub-fragment of either SEQ ID NOs 1 or 2. It is suggested that Applicant amend the claims to recite “the amino acid sequence of SEQ ID NO:1” “the amino acid sequence of SEQ ID NO:2” or the like.
The specification is not enabled for antibodies “wherein the immunoglobulin heavy chain variable region comprises one or more conservative amino acid substitutions” of claim 4; “wherein:(a) the immunoglobulin heavy chain variable region and/or immunoglobulin light chain variable region comprise one or more conservative amino acid substitutions; (b) SEQ ID NO:1 or SEQ ID NO:2 has two, three, four, five, six, seven, eight, nine, ten, eleven, twelve thirteen, fourteen or fifteen conservative amino acid substitutions” wherein the Ab retains its ability to specifically bind to a human CD10 protein or polypeptide of claim 6. Although the claims are dependent upon claim 1 which requires the 6 CDRs the claim language of claims 4 and 6 appear to open up the claims to allow for amino acid substitutions within one or more of the CDRs. The specification is not enabled for antibodies that bind to CD10 which do not specify all 6 CDRs.
The specification is not enabled for antibodies for use in the claimed invention with variable regions which comprise a portion of the constant region.
The specification is not enabled for antibodies which are bound to a composition.
The breadth of the instant claims encompasses antibodies with fewer than all six CDRs found in the heavy plus light chain binding region. The specification does not adequately disclose how the skilled artisan would make and use the various antibodies recited in the instant claims.
It is well established in the art that it is highly unpredictable which changes in amino acid sequence can be made in complementarity determining regions (CDRs) of a parental antibody such that the derived antibody retains the binding specificity and affinity of the parent antibody. The art of Mariuzza et al. (PTO-892; Reference U) reviews the structural basis of antigen-antibody recognition and teaches that a naturally occurring antibody comprises light and heavy chains. The antigen-combining site of an antibody is a three-dimensional structure, which fully comprises six "complementarity-determining regions" (CDRs), three each from the light and heavy chains. The amino acid sequences of the CDRs are hypervariable, as the amino acid residues contained within the CDRs determine much of antibody's antigen-binding specificity. Of the amino acid residues of the antibody contacting the antigen, six are within the light chain, nine are within the heavy chain, and two are within the constant or nearly constant "framework" regions (In particular, whole document). As such, one of skill in the art would not be able to make and use the genus of recited antibodies which would retain antigen binding function, because it is the 6 CDRs together which determine the antibody's antigen-binding specificity, but the specification sets forth that amino acids in CDRs can be varied from the parental antibody without identifying which CDR residues of the particularly disclosed antibodies that can be altered to retain antigen-binding function.
It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function.
Rudikoff et al. (PTO-892; Reference V) teaches that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function (In particular, page 1979, whole document). Rader et al. (PTO-892; Reference W) teaches in vitro selection and evolution of antibodies derived from phage display libraries by pairing either heavy or light chain of the rodent antibody with human polypeptide library for antibody humanization is unpredictable, and certain antibodies cannot be humanized using this approach; and in addition, antibodies consisting of the same heavy chain paired with light chains that differ in light chain CDR3 and elsewhere in VL can obtain undesired feature of binding different epitopes of the same antigen (In particular, discussion on pages 8914-8915, whole document). Accordingly, since it is known in the art that antibodies can comprise the same CDR3 amino acid sequences but not share antigen-binding specificity, it is apparent that one of skill in the art could not be able to make and use the genus of recited antibodies which would retain binding specificity and antagonist function. For these reasons, one of skill in the art would not recognize that the specification is not enabled for the use of the genus of the recited antibodies.
The specification provides insufficient direction or guidance regarding how to produce antibodies as broadly defined by the claims other than the CD10Mab 3124 antibodies of SEQ ID NOs 1 and 2. One of ordinary skill in the art would be required to practice undue experimentation to practice the invention commensurate in scope with the claimed.
In view of the quantity of experimentation necessary, the limited working examples, the unpredictability of the art, the lack of sufficient guidance in the specification, and the breadth of the claims, it would take undue trials and errors to make and use the claimed antibodies with less than six CDRs.
Reasonable correlation must exist between the scope of the claims and scope of the enablement set forth. In view on the quantity of experimentation necessary the limited working examples, the nature of the invention, the state of the prior art, the unpredictability of the art and the breadth of the claims, it would take undue trials and errors to practice the claimed invention.
15. Claims 2-11 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.
Applicant is in possession of: an isolated or purified antibody (Ab), or antigen (Ag) binding fragment thereof, or monomeric or dimeric antigen binding protein (ABP), capable of specifically binding a human CD10 polypeptide, wherein the isolated or purified Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP comprises:(a) an immunoglobulin heavy chain variable region comprising CDR1 amino acid (aa) residues GYTFTDYF (residues 26-33 of SEQ ID NO: 1), CDR2 aa residues INPNNGDT (residues 51 to 58 of SEQ ID NO:1), and CDR3 aa residues AKGGFNPGDY (residues 97-106 of SEQ ID NO:1), and, (b) an immunoglobulin light chain variable region comprising CDR1 amino acid (aa) residues QSLVHRNGNTY (residues 27-37 of SEQ ID NO:2), CDR2 aa residues KVS (residues 55 to 57 of SEQ ID NO:2), and CDR3 aa residues SQSTHVPLT (residues 94-102 of SEQ ID NO:2); wherein the antibody comprises sequences which are 95% identical to SEQ ID NOs 1 and 2 including wherein the antibody comprises SEQ ID NOs 1 and 2 of CD10Mab 3124.
Applicant is not in possession of: an isolated or purified antibody (Ab), or antigen (Ag) binding fragment thereof, or monomeric or dimeric antigen binding protein (ABP), capable of specifically binding a human CD10 polypeptide, wherein the isolated or purified Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP comprises:(a) an immunoglobulin heavy chain variable region comprising CDR1 amino acid (aa) residues GYTFTDYF (residues 26-33 of SEQ ID NO: 1), CDR2 aa residues INPNNGDT (residues 51 to 58 of SEQ ID NO:1), and CDR3 aa residues AKGGFNPGDY (residues 97-106 of SEQ ID NO:1), and, (b) an immunoglobulin light chain variable region comprising CDR1 amino acid (aa) residues QSLVHRNGNTY (residues 27-37 of SEQ ID NO:2), CDR2 aa residues KVS (residues 55 to 57 of SEQ ID NO:2), and CDR3 aa residues SQSTHVPLT (residues 94-102 of SEQ ID NO:2) wherein the antibody is a single domain antibody or single variable region of the heavy and light chain of claim 2; wherein the heavy chain variable region comprises a amino acid sequence SEQ ID NO:1 of claim 3; wherein the immunoglobulin heavy chain variable region comprises one or more conservative amino acid substitutions of claim 4; wherein the light chain variable region comprises a amino acid sequence SEQ ID NO:2 of claim 5; wherein:(a) the immunoglobulin heavy chain variable region and/or immunoglobulin light chain variable region comprise one or more conservative amino acid substitutions; (b) SEQ ID NO:1 or SEQ ID NO:2 has two, three, four, five, six, seven, eight, nine, ten, eleven, twelve thirteen, fourteen or fifteen conservative amino acid substitutions, and the recombinant Ab, or Ag binding fragment thereof, or monomeric or dimeric ABP retains its ability to specifically bind to a human CD10 protein or polypeptide (c) the immunoglobulin light chain variable region further comprises at least a portion of a light chain constant region; (d) the immunoglobulin heavy chain variable region further comprises at least a portion of an immunoglobulin heavy chain constant region; (e) the immunoglobulin light chain variable region further comprises at least a portion of an immunoglobulin light chain constant region; and, the immunoglobulin heavy chain variable region further comprises at least a portion of an immunoglobulin heavy chain constant region of claim 6 and wherein the recombinant Ab, the Ag binding fragment thereof, or monomeric or dimeric ABP, or the heavy chain constant region, or the light chain constant region, or the heavy chain constant region and the light chain constant region, further comprises or is bound to a heterologous protein, peptide, or a compound or a composition of claim 7; and claims dependent thereupon of claims 8-11.
The specification has not adequately described the isolated or purified antibody wherein the antibody is a single domain antibody or single variable region of the heavy and light chain of claim 2 is not enabled because the specification has not disclosed any single domain antibodies or single variable region antibodies which can bind to CD10.
The specification has not adequately described antibodies wherein the heavy chain variable region comprises “a” amino acid sequence SEQ ID NO:1 or “a” amino acid sequence SEQ ID NO:2. This claim recitation is not proper grammar and the language opens up the claims to read on any sub-fragment of either SEQ ID NOs 1 or 2. It is suggested that Applicant amend the claims to recite “the amino acid sequence of SEQ ID NO:1” “the amino acid sequence of SEQ ID NO:2” or the like.
The specification has not adequately described antibodies “wherein the immunoglobulin heavy chain variable region comprises one or more conservative amino acid substitutions” of claim 4; “wherein:(a) the immunoglobulin heavy chain variable region and/or immunoglobulin light chain variable region comprise one or more conservative amino acid substitutions; (b) SEQ ID NO:1 or SEQ ID NO:2 has two, three, four, five, six, seven, eight, nine, ten, eleven, twelve thirteen, fourteen or fifteen conservative amino acid substitutions” wherein the Ab retains its ability to specifically bind to a human CD10 protein or polypeptide of claim 6. Although the claims are dependent upon claim 1 which requires the 6 CDRs the claim language of claims 4 and 6 appear to open up the claims to allow for amino acid substitutions within one or more of the CDRs. The specification is not enabled for antibodies that bind to CD10 which do not specify all 6 CDRs.
The specification has not adequately described antibodies for use in the claimed invention with variable regions which comprise a portion of the constant region.
The specification has not adequately described antibodies which are bound to a composition.
The breadth of the instant claims encompasses antibodies with fewer than all six CDRs found in the heavy plus light chain binding region. The specification has not adequately described the various antibodies recited in the instant claims.
Consequently, conception cannot be achieved until a representative description of the structural and functional properties of the claimed invention has occurred, regardless of the complexity or simplicity of the method.
As evidenced by the art of Goel et al. (PTO-892; Reference X), Khan et al. (PTO-892; Page 2; Reference U) and Poosarla et al. (PTO-892; Page 2; Reference V), antibody specificity for a particular antigen does not correlate with any particular structure for the antibodies themselves. It was well known to those skilled in the art at the time the invention was made that minor structural differences among structurally related antibodies or compositions thereof could result in substantially different binding activities. Given the lack of guidance in the specification, it is unpredictable which antibodies with which structures would bind to the recited sequences. The specification does not disclose a correlation between the structure of the antibodies themselves and their function of binding to the recited sequences such that a skilled artisan would have known what antibody structures possess the claimed functions.
U.S. Court of Appeals for the Federal Circuit recently decided Amgen v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017) which concerned adequate written description for claims drawn to antibodies. The Federal Circuit explained in Amgen that when an antibody is claimed,
35 U.S.C. § 112(a) requires adequate written description of the antibody itself. Amgen, 872 F.3d at 1378-79. The Amgen court expressly stated that the so-called "newly characterized antigen" test, which had been based on an example in USPTO-issued training materials and was noted in dicta in several earlier Federal Circuit decisions, should not be used in determining whether there is adequate written description under 35 U.S.C. § 112(a) for a claim drawn to an antibody. Citing its decision in Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co. , the court also stressed that the "newly characterized antigen" test could not stand because it contradicted the quid pro quo of the patent system whereby one must describe an invention in order to obtain a patent. Amgen, 872
F.3d at 1378-79, quoting Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1345
(Fed. Cir. 2010). In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional. Id.
The specification does not provide adequate written description of the claimed invention.
The legal standard for sufficiency of a patent's (or a specification's) written description is
whether that description "reasonably conveys to the artisan that the inventor had possession at
that time of the. . .claimed subject matter", Vas-Cath, Inc. V. Mahurkar, 19 U.S.P.Q.2d 1111
(Fed. Cir. 1991). In the instant case, the specification does not convey to the artisan that the
applicant had possession at the time of invention of the claimed inventions.
The claims encompass antibodies with variants of the recited amino acid sequences. The claims recite variable region sequences containing amino acids not found in the antibodies that were actually produced in the examples in the specification which actually bind to CD10.
It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in
order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites.
MacCallum, et al. (PTO-892; Page 2; Reference W) analyzed many different antibodies for interactions with antigen and state that although CDR3 of the heavy and light chain dominate, a number of residues outside the standard CDR definitions make antigen contacts (see page 733, right column) and non-contacting residues within the CDRs coincide with residues as important in defining canonical backbone conformations (see page 735, left column). De Pascalis, et al. (PTO-892; Page 2; Reference X) demonstrates that grafting of the CDRs into a human framework was performed by grafting CDR residues and maintaining framework residues that were deemed essential for preserving the structural integrity of the antigen binding site (see page 3079, right column). Although abbreviated CDR residues were used in the constructs, some residues in all 6 CDRs were used for the constructs (see page 3080, left column). Thus it is unpredictable as to what amino acids can be changed in the original intact antibodies disclosed in the specification wherein the antibodies would still function. Thus, the skilled artisan cannot envision the detailed structure of the encompassed invention and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation.
Adequate written description requires more than a mere statement that it is part of the invention and a reference to a potential method of isolating it. In the instant application, the amino acid sequence itself or isolated protein is required. See Fiers v. Revel, 25 USPQ 2d 1601 at 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Lts., 18 USPQ2d 1016. In view of the aforementioned problems regarding description of the claimed invention, the specification does not provide an adequate written description of the invention claimed herein.
See The Regents of the University of California v. Eli Lilly and Company, 43 USPQ2d 1398,
1404-7 (Fed. Cir. 1997). In University of California v. Eli Lilly and Co., 39 U.S.P.Q.2d 1225
(Fed. Cir. 1995) the inventors claimed a genus of DNA species encoding insulin in different vertebrates or mammals, but had only described a single species of cDNA which encoded rat insulin. The court held that only the nucleic acids species described in the specification (i.e. nucleic acids encoding rat insulin) met the description requirement and that the inventors were not entitled to a claim encompassing a genus of nucleic acids encoding insulin from other vertebrates, mammals or humans, id. at 1240. The Federal Circuit has held that if an inventor is "unable to envision the detailed constitution of a gene so as to distinguish it from other materials.
. .conception has not been achieved until reduction to practice has occurred", Amgen, Inc. v.
Chugai Pharmaceutical Co, Ltd., 18 U.S.P.Q.2d 016 (Fed. Cir. 1991). Attention is also directed
to the decision of The Regents of the University of California v. Eli Lilly and Company (CAFC,
July 1997) wherein is stated: "The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 222 USPQ 369, 372-373 (Fed. Cir. 1984) (affirming rejection because the specification does "little more than outlin[e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate.").
Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material. Thus, as we have previously held, a cDNA is not defined or described by the mere name "cDNA," even if accompanied by the name of the protein that it encodes, but requires a kind of specificity usually achieved by means of the recitation of the sequence of nucleotides that make up the cDNA." See Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606.
As such, there is insufficient written description of the required kind of structure identifying information about the corresponding makeup of the claimed antagonists and antibodies to demonstrate possession.
16. Claim 1 appears to be in condition for allowance.
17. Any inquiry concerning this communication or earlier communications from the examiner should be directed to NORA MAUREEN ROONEY whose telephone number is (571)272-9937. The examiner can normally be reached on M-F from 8:00am to 4:30pm.
If attempts to reach the examiner by telephone are unsuccessful, the examiner' s supervisor, Misook Yu, can be reached at telephone number (571) 272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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March 21, 2026
/Nora M Rooney/
Primary Examiner, Art Unit 1641