Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
DETAILED ACTION
1. Claims 1-11 (filed 8/25/23) are pending. Claim 1 is an independent claim.
2. 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.
3. Claims 1-11 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a written description rejection.
An applicant shows possession of the claimed invention by describing the claimed invention with all of its limitations using such descriptive means as words, structures, figures, diagrams, and formulas that fully set forth the claimed invention. Lockwood v. Amer. Airlines, Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (Fed. Cir. 1997). Possession may be shown in a variety of ways including description of an actual reduction to practice, or by showing that the invention was "ready for patenting" such as by the 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. See, e.g., Pfaff v. Wells Elecs., Inc., 525 U.S. 55, 68, 119 S.Ct. 304, 312, 48 USPQ2d 1641, 1647 (1998); Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406; Amgen, Inc. v. Chugai Pharm., 927 F.2d 1200, 1206, 18 USPQ2d 1016, 1021 (Fed. Cir. 1991) (one must define a compound by "whatever characteristics sufficiently distinguish it"). "Compliance with the written description requirement is essentially a fact-based inquiry that will ‘necessarily vary depending on the nature of the invention claimed.’" Enzo Biochem, 323 F.3d at 963, 63 USPQ2d at 1612. An invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function. See MPEP 2163 I.A.
An applicant may also show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics. Enzo Biochem, 323 F.3d at 964, 63 USPQ2d at 1613 (quoting the Written Description Guidelines, 66 Fed. Reg. at 1106, n. 49, stating that "if the art has established a strong correlation between structure and function, one skilled in the art would be able to predict with a reasonable degree of confidence the structure of the claimed invention from a recitation of its function".). "Thus, the written description requirement may be satisfied through disclosure of function and minimal structure when there is a well-established correlation between structure and function." See MPEP 2163 II.3.
Claims 1-11 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. This is a written description rejection.
Applicant has broadly claimed a method for reducing an allergic response in an animal to an allergen in an environment, wherein the animal is predisposed to having an allergic response to the allergen, the method comprising: minimizing exposure to the allergen in the animal predisposed to having an allergic response to the allergen by contacting a source of the allergen in the environment with a composition containing a molecule that inhibits the ability of the allergen to bind to mast cells in the animal predisposed to having an allergic response to the allergen, thereby reducing the allergic response in the animal to the allergen in the environment (instant base claim 1), including wherein the molecule is an antibody (instant dependent claims 5 and 11), and including the other limitations of the dependent claims.
The specification does not disclose a representative number of species of the “molecule”, including an antibody, ingredient that must possess the functional property of inhibiting the ability of the allergen to bind to mast cells in the animal predisposed to having an allergic response to the allergen, nor sufficient relevant identifying characteristics in the form of structure or functional characteristics coupled with a known or disclosed correlation between structure and function.
An applicant shows possession of the claimed invention by describing the claimed invention with all of its limitations using such descriptive means as words, structures, figures, diagrams, and formulas that fully set forth the claimed invention. Lockwood v. Amer. Airlines, Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (Fed. Cir. 1997). Possession may be shown in a variety of ways including description of an actual reduction to practice, or by showing that the invention was "ready for patenting" such as by the 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. See, e.g., Pfaff v. Wells Elecs., Inc., 525 U.S. 55, 68, 119 S.Ct. 304, 312, 48 USPQ2d 1641, 1647 (1998); Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406; Amgen, Inc. v. Chugai Pharm., 927 F.2d 1200, 1206, 18 USPQ2d 1016, 1021 (Fed. Cir. 1991) (one must define a compound by "whatever characteristics sufficiently distinguish it"). "Compliance with the written description requirement is essentially a fact-based inquiry that will ‘necessarily vary depending on the nature of the invention claimed.' " Enzo Biochem, 323 F.3d at 963, 63 USPQ2d at 1612. An invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function. See MPEP 2163 I.A.
An applicant may also show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics. Enzo Biochem, 323 F.3d at 964, 63 USPQ2d at 1613 (quoting the Written Description Guidelines, 66 Fed. Reg. at 1106, n. 49, stating that "if the art has established a strong correlation between structure and function, one skilled in the art would be able to predict with a reasonable degree of confidence the structure of the claimed invention from a recitation of its function".). "Thus, the written description requirement may be satisfied through disclosure of function and minimal structure when there is a well-established correlation between structure and function." See MPEP 2163 II.3.
The specification discloses that any molecule or portion or fragment thereof that retains binding specificity for the allergen can be used as the molecule provided in the compositions or a part of the molecule where such molecule is a chimera of two or more portions linked together. The specification discloses non-limiting examples of such molecules such as antibodies, aptamers, and agonists/antagonists of the allergen ([0047].
The specification discloses that the term “antibody” as used herein includes polyclonal and monoclonal antibodies of any type and from any species, as well as immunoglobulin antigen-binding fragments such as Fv, Fab, Fab’, F(ab’)2, or other antigen-binding fragments, sequences or subsequences that interact with molecular specificity (e.g., demonstrate specific binding) with an antigen ([0034]).
The recited genus of allergen binding molecule or antibody used in the claimed method encompasses any molecule having the binding specificity that can also block binding of the allergen to a mast cell (that is, that can block binding of the allergen to an IgE molecule that is bound to a mast cell through its Fc portion in an allergy presensitized individual), including wherein the molecule is an aptamer, agonist or antagonists of the allergen, or antibodies from any animal species that can produce them or from a synthetic antibody library.
The specification does not disclose any species of antibody that possesses the requisite said functional property except one that is present as a polyclonal antibody preparation having specificity for allergen Fel D1. In more detail, the specification discloses that the ability of two antibodies against Fel D1 peptides were tested for their ability to block binding of the allergen to human IgE, wherein one did possess this functional property, and whereas the other did not. One species of antibody is not representative of the genus of antibodies or the genus of molecules that possess the functional properties of binding specifically to Fel D1 and blocking binding of the said allergen to IgE on a mast cell (see Example 1).
There is no evidence of record for a representative number of species for the genus of such molecules or antibodies specific for Fel D1 or any other allergen or of non-antibody molecules specific for Fel D1 or any other allergen.
As applicant is undoubtedly aware, recent court decisions in the biotechnology arena have highlighted the issue with defining binding members strictly using functional terms as can be readily seen in both AbbVie Deutschland GmbH v. Janssen Biotech. Inc. 759 F.3d 1285 (Fed. Cir. 2014) and Amgen v. Sanofi. (Fed Cir, 2017-1480. 10/5/2017). Indeed, in Amgen the court indicates that that it is improper to allow patentees to claim a binding molecule by describing something that is not the invention, i.e., the structure to which it binds, as knowledge of the chemical structure of the thing being bound does not give the required kind of structure-identifying information about the thing being claimed. Notably, in the instant claims, the molecule as well as the antibody molecule are functionally described (even though antibodies have known structures, the cognate CDRs that provide the binding specificity are not known by a general structure /function relationship).
One of skill in the art was aware that the number and sequence of antibodies that bind to a single protein is a very large and structurally diverse genus, with no common structural relationship even for antibodies that bind to the same protein, epitope, or overlapping epitopes of a same protein [see for example, Edwards et al. (JMB, 2003, 334: 103-118, IDS reference), Lloyd et al. (Protein Eng. Design & Selection, 2009, 22(3): 159-168, IDs reference), Goel et al. (J. Immunol. 2004, 173: 7358-7367, IDS reference), Khan and Salunke (J. Immunol. 2014, 192: 5398-5405, IDS reference), Poosarla et al. (Biotech. Bioeng. 2017, 114(6): 1331-1342, IDS reference), Torres and Casadevall (Trend. Immunol. 2008, 29(2): 91-97, IDS reference)]. These evidentiary references underscore a large and structurally diverse genus of immune repertoire of antibodies that bind to a same antigen, a same epitope of an antigen, or overlapping epitopes of a same antigen.
As regards the two antibodies disclose in the specification in Example 1, it is unclear from the specification whether these are monoclonal antibodies or if the term antibodies is being used in Example 1 to describe two different polyclonal antisera or one of each said category.
Evidentiary reference Satyaraj and Wedner (EMJ Allergy Immunol. 2019 4(1): 40-46, IDS reference) teaches that “Indoor Poly” antibody is a rabbit polyclonal antiserum made against Fel D1 protein. This appears to be identical to the “antibody” disclosed in the instant specification that is designated as “indoor Ab” in Example 1. The evidentiary reference further teaches a rabbit anti-Fel D1 termed “FGI” which is a monoclonal antibody (mAb) that identifies the peptide sequence covering amino acid residues 23-40 in chain 1 of Fel D1, a known IgE-binding site. This antibody appears to be identical to the second antibody disclose in Example 1 of the instant specification. Satyaraj and Wedner teach that a dose-dependent inhibition of salivary Fel D1 and human IgE complex formation could be achieved using the polyclonal antiserum, but not using the mAb GFI, indicating that multiple epitopes on Fel D1 need to be blocked to prevent its interaction with IgE and the subsequent mast cell degranulation that occurs upon allergen binding (see entire reference, especially page 42 at column 1).
However, conversely to the teaching of Santyaraj and Wedner, evidentiary reference Satyraj et al. (Immunity, Inflammation and Disease, 2019, 7: 68-73, IDS reference) teaches that a rabbit polyclonal anti-Gel D1 antiserum (presumably the same as that taught by Satyaraj and Wedner above and that is also disclosed in Example 1 of the instant specification ) blocked Fel D1 binding to IgE more than a monoclonal anti-Fel D1 IgG, so presumably there is a monoclonal antibody that blocks binding of Fel D1 to IgE and subsequence mast cell degranulation. The Examiner characterizes this as “presumably” because the said reference refers to citation “15” of the reference for the said teaching, while reference 15 does not pertain to the said teaching at all. The said reference 15 teaches that Fel D1 contains at least three IgE-specific binding sites, and multiple IgE binding epitopes are required for allergen cross-linking of mast cells and basophil bound IgEs and subsequent cellular degranulation (especially page 71 at the first paragraph and the paragraph spanning columns 1-2).
The specification further discloses “Binding of allergen [Fel D1] to human IgE present on pre-sensitized mast cells is the primary trigger for allergic reaction. Blocking the ability of allergen to bind IgE can thus avoid this trigger, and minimize, reduce , or even prevent an allergic response in an allergic individual” ([0082]). Thus, the structure of the antibodies that possess this functional property are not known until one applies a method to discover them, as is also enunciated above, i.e., the antibodies that possess this functional property will have extensively different structures.
Although one of skill in the art could potentially make such an antibody or a molecule and test it to determine if it possesses the requisite functional properties, note that:
“Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features.” See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895.
Therefore, it appears that the instant specification does not adequately disclose the breadth of the molecule, including an antibody, used in the method recited in the instant claims. In light of this, a skilled artisan would reasonably conclude that Applicant was not in possession of the genus of all such molecules or antibodies at the time the instant application was filed.
Applicant is also reminded that the written description provision of 35 U.S.C. 112 is severable from its enablement provision (Ariad Phar., Inc. v. Eli Lilly & Co., 598 F.3d 1336 (Fed. Cir. 2010); see also Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1876 (Fed. Cir. 2011).
4. 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.
5. The following is a quotation of the appropriate paragraphs of pre-AIA 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 –
(e) the invention was described in (1) an application for patent, published under section 122(b), by another filed in the United States before the invention by the applicant for patent or (2) a patent granted on an application for patent by another filed in the United States before the invention by the applicant for patent, except that an international application filed under the treaty defined in section 351(a) shall have the effects for purposes of this subsection of an application filed in the United States only if the international application designated the United States and was published under Article 21(2) of such treaty in the English language.
6. Claims 1-9 are rejected under pre-AIA 35 U.S.C. 102(e) as being anticipated by
US 2007/0231341 A1 (IDS reference).
Claim interpretation: The specification does not disclose a limiting definition for “contain” or “containing”. However, evidentiary reference Merriam Webster Dictionary (merriam-webster.com/dictionary/contain, 2026, 9 pages) teaches that “contain” is defined as “comprise”. Therefore the “composition containing a molecule” that is recited in instant base claim 1 is being interpreted as a composition comprising a molecule, opening the composition to comprise other non-recited elements. The specification discloses that the “term animal as used herein includes both humans and non-human animals of any kind”, with “animal” including any animal susceptible to or suffering from an allergic response to an environmental antigen or at least one symptom of such an allergic response upon exposure to the allergen, or can include any animal that is the source or a source of an environmental allergen ([0029]). The specification discloses that the term “antibody” as used herein includes polyclonal and monoclonal antibodies of any type and from any species, as well as immunoglobulin antigen-binding fragments such as Fv, Fab, Fab’, F(ab’)2, or other antigen-binding fragments, sequences or subsequences that interact with molecular specificity (e.g., demonstrate specific binding) with an antigen ([0034]). The specification discloses that the term “environment” as used herein refers to a local environment of an animal, any area exposed to a source of an allergen such as a pet, insect, or plant, or the environment can also comprise a part or all of an animal, plant, insect, or other source of an allergen. “For example, providing a composition for treatment for oral intake to an animal that is the source of an allergen constitutes treating the “environment” of another animal that is allergic or predisposed to having an allergic reaction to the allergen ([0031]). The specification discloses that any molecule or portion or fragment thereof that retains binding specificity for the allergen can be used as the molecule provided in the compositions or a part of the molecule where such molecule is a chimera of two or more portions linked together. The specification discloses non-limiting examples of such molecules such as antibodies, aptamers, and agonists/antagonists of the allergen ([0047]. The specification discloses at [0065] that in one embodiment, the “surface” is the surface of an animal that is a source of the allergen.
Instant claim 1 recites: A method for reducing an allergic response in an animal to an allergen in an environment, wherein the animal is predisposed to having an allergic response to the allergen, the method comprising: minimizing exposure to the allergen in the animal predisposed to having an allergic response to the allergen by contacting a source of the allergen in the environment with a composition containing a molecule that inhibits the ability of the allergen to bind to mast cells in the animal predisposed to having an allergic response to the allergen, thereby reducing the allergic response in the animal to the allergen in the environment.
Note that the instant specification at [0082] discloses “Binding of allergen to human Ig# present on pre-sensitized mast cells is the primary trigger for allergic reaction. Blocking the ability of allergen to bind to IgE can thus avoid this trigger, and minimize, reduce, or even prevent an allergic response in an allergic individual.” (Thus, the anti-allergen-specific IgE is bound to a mast cell through its Fc portion in an allergic individual). When allergen is encountered, the allergen binds to the antigen-binding portions of IgE that is bound to mast cells in pre-sensitized individuals, triggering release of inflammatory mediators of allergic reactions such as histamine from the mast cell.)
Also note that a rejection based upon this reference was affirmed by the BPAI in the parent application serial no. 15/181,813.
US20070231341 A1 discloses that an allergen of particular concern for people who are allergic to cats (i.e., humans who are predisposed to having an allergic response to an allergen) is the feline skin and salivary gland allergen of the domestic cat Felis domesticus allergen 1 (Fel D1”). US20070231341 A1 discloses that exposure to this allergen elicits an IgE-mediated allergic response in sensitized individuals.
US20070231341 A1 discloses an immunogenic composition for oral administration to a cat, the composition comprising an antibody that specifically binds to Fel D1 allergen. US20070231341 A1 discloses that the monoclonal antibody can bind to the Fel D1 in such a manner so as to block epitopes recognized by human IgE, thus eliminating or diminishing the allergic response in humans (i.e., reducing an allergic response in an animal, a human in this instance, to an allergen in the environment, as is recited in instant base claim 1), the Fel D1 being primarily a salivary gland allergen that elicits an IgE-mediated allergic response in sensitized individuals. US20070231341 A1 discloses that the composition may comprise dextrose or lactose (note that the former is a flavoring agent, whereas the latter is a food substance when present in an effective amount for flavoring or nutrition, respectively, and that the art reference discloses that both are isotonic agents that can be included in the formulation as carriers), or any and all solvents, dispersion media, diluents, preservatives. US20070231341 A1 also discloses that the composition comprising the antibody can be made in various forms depending upon the route of administration, such as lyophilized powders, or liquids, or by delivery by spray, drops, wiping, dipping, rubbing or other topical administration of the antibody to a cat (i.e., wiping, rubbing or topical administration of the antibody to a cat meets the claim limitation recited in instant dependent claim 7 of “wherein the composition is applied to a surface in the environment as is detailed in the claim interpretation section above). (See entire reference, especially [0002], [0006]-[0008], [0079], [0084], [0086], [0088]-[0091], [0097], and claim 10).
7. The following is a quotation of pre-AIA 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action:
(a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter pertains. Patentability shall not be negated by the manner in which the invention was made.
8. Claims 1-11 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over
US 2007/0231341 A1 (IDS reference) in view of Jefferis and Lund (Immunol. Lett, 2002, 82: 57-65).
Instant claim 1 recites: A method for reducing an allergic response in an animal to an allergen in an environment, wherein the animal is predisposed to having an allergic response to the allergen, the method comprising: minimizing exposure to the allergen in the animal predisposed to having an allergic response to the allergen by contacting a source of the allergen in the environment with a composition containing a molecule that inhibits the ability of the allergen to bind to mast cells in the animal predisposed to having an allergic response to the allergen, thereby reducing the allergic response in the animal to the allergen in the environment.
Note that the instant specification at [0082] discloses “Binding of allergen to human Ig# present on pre-sensitized mast cells is the primary trigger for allergic reaction. Blocking the ability of allergen to bind to IgE can thus avoid this trigger, and minimize, reduce, or even prevent an allergic response in an allergic individual.” (Thus, the anti-allergen-specific IgE is bound to a mast cell through its Fc portion in an allergic individual). When allergen is encountered, the allergen binds to the antigen-binding portions of IgE that is bound to mast cells in pre-sensitized individuals, triggering release of inflammatory mediators of allergic reactions such as histamine from the mast cell.)
Also note that a rejection based upon this reference was affirmed by the BPAI in the parent application serial no. 15/181,813.
US20070231341 A1 discloses that an allergen of particular concern for people who are allergic to cats (i.e., humans who are predisposed to having an allergic response to an allergen) is the feline skin and salivary gland allergen of the domestic cat Felis domesticus allergen 1 (Fel D1”). US20070231341 A1 discloses that exposure to this allergen elicits an IgE-mediated allergic response in sensitized individuals.
US20070231341 A1 discloses an immunogenic composition for oral administration to a cat, the composition comprising an antibody that specifically binds to Fel D1 allergen. US20070231341 A1 discloses that the monoclonal antibody can bind to the Fel D1 is such a manner so as to block epitopes recognized by human IgE, thus eliminating or diminishing the allergic response in humans (i.e., reducing an allergic response in an animal, a human in this instance, to an allergen in the environment, as is recited in instant base claim 1), the Fel D1 being primarily a salivary gland allergen that elicits an IgE-mediated allergic response in sensitized individuals. US20070231341 A1 discloses that the composition may comprise dextrose or lactose (note that the former is a flavoring agent, whereas the latter is a food substance when present in an effective amount for flavoring or nutrition, respectively, and that the art reference discloses that both are isotonic agents that can be included in the formulation as carriers), or any and all solvents, dispersion media, diluents, preservatives. US20070231341 A1 discloses that the composition comprising the antibody can be made in various forms depending upon the route of administration, such as lyophilized powders, or liquids, or by delivery by spray, drops, wiping, dipping, rubbing or other topical administration of the antibody to a cat (i.e., wiping, rubbing or topical administration of the antibody to a cat meets the claim limitation recited in instant dependent claim 7 of “wherein the composition is applied to a surface in the environment as is detailed in the claim interpretation section above). US20070231341 A1 also discloses that besides blocking the interaction of the allergen with IgE, the antibody can facilitate removal of the allergen from the system upon binding the allergen (i.e., it can facilitate removal of immune complexes consisting of the allergen and the antibody through its Fc portion). (See entire reference, especially [0002], [0006]-[0008], [0079], [0084], [0086], [0088]-[0091], [0097], and claim 10).
US20070231341 A1 does not disclose that the antibody is a hybrid comprising the antigen binding portion of an antibody specific for the antibody along with at least a portion of human IgG.
Jefferis and Lund teach “The IgG molecule is a multifunctional glycoprotein that binds antigen…with the formation of immune complexes that activate effector mechanisms resulting in their clearance and destruction” (section 2 at the second sentence). Jefferis and Lund teach that the human Fc gamma Receptor I (FcgRI) is expressed on macrophages and has a high affinity for IgG and immune complexes (section 5) and that stimulation of cells such as macrophages through FcgRs may result in the activation of one or more of a variety of effector functions, including phagocytosis, ADCC and CDC (Introduction paragraph 2). See entire reference.
It would have been prima facie obvious to one of ordinary skill in the art before the time the instant invention was made to have constructed a hybrid antibody comprising the antigen binding portion of the blocking antibody that blocks binding of the Fel D1 allergen to a mast cell taught by the primary art reference and a human IgG Fc subclass portion that can bind to an FcR on macrophages and to have used it in the method disclosed by the primary art reference.
One of ordinary skill in the art would have been motivated to do this, and with a reasonable expectation of success in doing so, in order to create a composition comprising an antibody that not only blocks binding of the allergen to a mast cell, but actively facilitates removal of the allergen in the allergen-predisposed human through the human Fc portion of the antibody (that is also bound to the allergen through its antigen binding region), particularly in light of the disclosure of the primary art reference that such an antibody may do both.
9. 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.
10. Court rulings have been quite clear that ONLY DIVISIONAL applications are entitled to the shield from double patenting under 35 USC 121. Indeed, in AMGEN INC v. HOFFMANN LA ROCHE LTD GMBH LA (Nos. 2009-1020, 2009-1096) the court discusses this issue at length and states:
Turning to the legislative history, the court observed that a House Report also referred specifically to “divisional application[s].” Id. Notably absent from the legislative history, in the court's view, was a suggestion “that the safe-harbor provision was, or needed to be, directed at anything but divisional applications.” Id. at 1361. From there, the court “conclude^] that the protection afforded by section 121 to applications (or patents issued therefrom) filed as a result of a restriction requirement is limited to divisional applications.” Id. at 1362. Accordingly, the court decided that the § 121 safe harbor did not apply to the patent before it, which issued from a continuation-in-part application. Id.
We are persuaded by the reasoning in Pfizer that the § 121 safe harbor provision does not protect continuation applications or patents descending from only continuation applications. The statute on its face applies only to divisional applications, and a continuation application, like a continuation-in-part application, is not a divisional application.
Given that Applicant chose to file the 15/874,102 case that issued as US 10,774,137 as a separate unrelated application, not as a DIV of the instant application, the instant rejection has been set forth.
Claims 1-4, 8 and 9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 10,774,137 as evidenced by an admission in the specification of US 10,774,137 at column 4, lines 4-9.
Claims 1-7 of US 10,774,137 are drawn to a food grade powder providing sustained release of an anti-Fel D1 molecule comprising a hydrogel.
Claims 8 and 9 of US 10,774,137 are drawn to a method of reducing symptoms of human allergy to a cat, the method comprising orally administering to the cat an effective amount of the food grade powder of claim 1.
As pertains to mechanism, note that the instant specification at [0082] discloses “Binding of allergen to human IgE present on pre-sensitized mast cells is the primary trigger for allergic reaction. Blocking the ability of allergen to bind to IgE can thus avoid this trigger, and minimize, reduce, or even prevent an allergic response in an allergic individual.” (Thus, the anti-allergen-specific IgE is bound to a mast cell through its Fc portion. When allergen is encountered, it binds to the antigen-binding portions of IgE that is bound to mast cells in pre-sensitized individuals, triggering release of inflammatory mediators of allergic reactions such as histamine from the mast cell.)
Although the claims at issue are not identical, they are not patentably distinct from each other because the admission in the specification of US 10,774,137 at column 4, lines 4-9 is that “Another advantage of one or more embodiments provided by the present disclosure is to expose a cat’s mouth to a molecule that binds FelD1 before it contacts a sensitive human: a bound allergen cannot interact with the mast cells in the human and thereby cannot cause an allergic reaction.” This is pertinent to the recitation in instant base claim 1 of “contacting a source of the allergen in the environment with a composition containing a molecule that inhibits the ability of the allergen to bind to mast cells in the animal predisposed to having an allergic response to the allergen”. In addition, Fel D1 allergen, a human having an allergic response to Fel D1, a hydrogel, and a food grade powder are species of allergens, susceptible animals, gels, and consumable for a feline recited in the instant claims.
11. Court rulings have been quite clear that ONLY DIVISIONAL applications are entitled to the shield from double patenting under 35 USC 121. Indeed, in AMGEN INC v. HOFFMANN LA ROCHE LTD GMBH LA (Nos. 2009-1020, 2009-1096) the court discusses this issue at length and states:
Turning to the legislative history, the court observed that a House Report also referred specifically to “divisional application[s].” Id. Notably absent from the legislative history, in the court's view, was a suggestion “that the safe-harbor provision was, or needed to be, directed at anything but divisional applications.” Id. at 1361. From there, the court “conclude^] that the protection afforded by section 121 to applications (or patents issued therefrom) filed as a result of a restriction requirement is limited to divisional applications.” Id. at 1362. Accordingly, the court decided that the § 121 safe harbor did not apply to the patent before it, which issued from a continuation-in-part application. Id.
We are persuaded by the reasoning in Pfizer that the § 121 safe harbor provision does not protect continuation applications or patents descending from only continuation applications. The statute on its face applies only to divisional applications, and a continuation application, like a continuation-in-part application, is not a divisional application.
Given that Applicant chose to file the 15/874,102 case that issued as US 10,774,137 as a separate unrelated application, not as a DIV of the instant application, the instant rejection has been set forth.
Claims 1-6 and 8-11 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 10,774,137 in view of US 2007/0231341 A1 (IDS reference) and Jefferis and Lund (Immunol. Lett, 2002, 82: 57-65), as evidenced by an admission in the specification of US 10,774,137 at column 4, lines 4-9.
Claims 1-7 of US 10,774,137 are drawn to a food grade powder providing sustained release of an anti-Fel D1 molecule comprising a hydrogel. (The specification of US 10,774,137 defines an anti-Fel D1 molecule as any molecule able to specifically bind to Fel D1 allergen (see column 1 at lines 43045)).
Claims 8 and 9 of US 10,774,137 are drawn to a method of reducing symptoms of human allergy to a cat, the method comprising orally administering to the cat an effective amount of the food grade powder of claim 1.
The admission in the specification of US 10,774,137 at column 4, lines 4-9 is that “Another advantage of one or more embodiments provided by the present disclosure is to expose a cat’s mouth to a molecule that binds Fel D1 before it contacts a sensitive human: a bound allergen cannot interact with the mast cells in the human and thereby cannot cause an allergic reaction.” This is pertinent to the recitation in instant base claim 1 of “contacting a source of the allergen in the environment with a composition containing a molecule that inhibits the ability of the allergen to bind to mast cells in the animal predisposed to having an allergic response to the allergen”. In addition, Fel D1 allergen, a human having an allergic response to Fel D1, a hydrogel, and a food grade powder are species of allergens, susceptible animals, gels, and consumable for a feline recited in the instant claims.
The claims of US 10,774,137 do not recite wherein the molecule is an antibody that binds to Fel D1.
US20070231341 A1 does disclose orally administering an antibody that specifically binds to Fel D1 allergen and blocks epitopes recognized by human IgE, thus eliminating or diminishing the allergic response in humans:
US20070231341 A1 discloses that an allergen of particular concern for people who are allergic to cats (i.e., humans who are predisposed to having an allergic response to an allergen) is the feline skin and salivary gland allergen of the domestic cat Felis domesticus allergen 1 (Fel D1”). US20070231341 A1 discloses that exposure to this allergen elicits an IgE-mediated allergic response in sensitized individuals.
US20070231341 A1 discloses an immunogenic composition for oral administration to a cat, the composition comprising an antibody that specifically binds to Fel D1 allergen. US20070231341 A1 discloses that the monoclonal antibody can bind to the Fel D1 is such a manner so as to block epitopes recognized by human IgE, thus eliminating or diminishing the allergic response in humans (i.e., reducing an allergic response in an animal, a human in this instance, to an allergen in the environment, as is recited in instant base claim 1), the Fel D1 being primarily a salivary gland allergen that elicits an IgE-mediated allergic response in sensitized individuals. US20070231341 A1 discloses that the composition may comprise dextrose or lactose (note that the former is a flavoring agent, whereas the latter is a food substance when present in an effective amount for flavoring or nutrition, respectively, and that the art reference discloses that both are isotonic agents that can be included in the formulation as carriers), or any and all solvents, dispersion media, diluents, preservatives. US20070231341 A1 discloses that the composition comprising the antibody can be made in various forms depending upon the route of administration, such as lyophilized powders, or liquids, or by delivery by spray, drops, wiping, dipping, rubbing or other topical administration of the antibody to a cat (i.e., wiping, rubbing or topical administration of the antibody to a cat meets the claim limitation recited in instant dependent claim 7 of “wherein the composition is applied to a surface in the environment as is detailed in the claim interpretation section above). US20070231341 A1 also discloses that besides blocking the interaction of the allergen with IgE, the antibody can facilitate removal of the allergen from the system upon binding the allergen (i.e., it can facilitate removal of immune complexes comprising the allergen and the antibody through its Fc portion). (See entire reference, especially [0002], [0006]-[0008], [0079], [0084], [0086], [0088]-[0091], [0097], and claim 10).
As enunciated above in this office action, one of ordinary skill in the art was aware that the anti-allergen-specific IgE is bound to a mast cell through its Fc portion. When allergen is encountered, it binds to the antigen-binding portions of IgE that is bound to mast cells in pre-sensitized individuals, triggering release of inflammatory mediators of allergic reactions such as histamine from the mast cell.
Jefferis and Lund teach that the IgG molecule binds antigen but also comprises an Fc region that can bind to Fc receptors such as the FcgRI that residues on macrophages, and through FcR binding, can activate a variety of effector functions, including phagocytosis, ADCC and CDC that are useful for eliminating immune complexes (e.g., such as the Fel D1 allergen/anti-Fel D1 immune complexes. Jefferis and Lund teach human IgG subclasses that bind to FcRs on human macrophages:
Jefferis and Lund teach “The IgG molecule is a multifunctional glycoprotein that binds antigen…with the formation of immune complexes that activate effector mechanisms resulting in their clearance and destruction” (section 2 at the second sentence). Jefferis and Lund teach that the human Fc gamma Receptor I (FcgRI) is expressed on macrophages and has a high affinity for IgG and immune complexes (section 5) and that stimulation of cells such as macrophages through FcgRs may result in the activation of one or more of a variety of effector functions, including phagocytosis, ADCC and CDC (Introduction paragraph 2). See entire reference.
It would have been prima facie obvious to one of ordinary skill in the art before the time the instant invention was made to have constructed a hybrid antibody comprising the antigen binding portion of the blocking antibody that blocks binding of the Fel D1 allergen to a mast cell as disclosed by US20070231341 A1 and a human IgG Fc subclass portion that can bind to an FcR on macrophages as taught by Jefferis and Lund, and to have used it in the method recited in the claims of US 10,774,137.
One of ordinary skill in the art would have been motivated to do this, and with a reasonable expectation of success in doing so, in order to create and use a composition comprising an antibody that not only blocks binding of the allergen to a mast cell, but actively facilitates removal of the allergen in the allergen-predisposed human through the human Fc portion of the antibody (that is also bound to the allergen through its antigen binding region), particularly in light of the disclosure of US20070231341 A1u that such an antibody may do both.
12. Court rulings have been quite clear that ONLY DIVISIONAL applications are entitled to the shield from double patenting under 35 USC 121. Indeed, in AMGEN INC v. HOFFMANN LA ROCHE LTD GMBH LA (Nos. 2009-1020, 2009-1096) the court discusses this issue at length and states:
Turning to the legislative history, the court observed that a House Report also referred specifically to “divisional application[s].” Id. Notably absent from the legislative history, in the court's view, was a suggestion “that the safe-harbor provision was, or needed to be, directed at anything but divisional applications.” Id. at 1361. From there, the court “conclude^] that the protection afforded by section 121 to applications (or patents issued therefrom) filed as a result of a restriction requirement is limited to divisional applications.” Id. at 1362. Accordingly, the court decided that the § 121 safe harbor did not apply to the patent before it, which issued from a continuation-in-part application. Id.
We are persuaded by the reasoning in Pfizer that the § 121 safe harbor provision does not protect continuation applications or patents descending from only continuation applications. The statute on its face applies only to divisional applications, and a continuation application, like a continuation-in-part application, is not a divisional application.
Given that Applicant chose to file the 17/731,403 case that issued as US 12,012,447 as a separate unrelated application, not as a DIV of the instant application, the instant rejection has been set forth.
Claims 1-6, 8 and 9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-8 of U.S. Patent No. 12,012,447.
Claims 1-6 of US 12,012,447 are drawn to a supplement of system for reducing allergic response to Fel D1, comprising dried (avian) egg yolk powder comprising an anti-Fel D1 molecule that is anti-Fel-D1 specific polyclonal immunoglobulin Y, including a food composition that is a cat food.
Claims 7 and 8 of US 12,012,447 are drawn to a method for reducing allergic response to Fel D1 comprising, administering the food composition to a cat.
Although the claims at issue are not identical, they are not patentably distinct from each other because cat, powder, and Fel D1 are species recited in the method of the instant claims.
13. Claims 1-6 and 8-11 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2 of U.S. Patent No. 8,454,953.
Claims 1-2 of US 8,424,953 are drawn to a method for reducing an allergic response in a human to Fel D1 in an environment comprising minimizing exposure to Fel D1 in the human predisposed to having response to Fel D1 by contacting the source of the allergen in the environment with a composition containing an anti-Fel D1 antibody that inhibits the ability of Fel D1 to bind to mast cells in the human predisposed to having an allergic response to Fel D1; thereby reducing the allergic response in the human to Fel D1 in the environment, wherein Fel D1 is from a feline and the composition is consumed by that feline, including wherein the antibody is a hybrid molecule comprising at least a portion of human IgG.
Instant dependent claim 6 is included in this rejection because a liquid, a solid, a gel or a powder are obvious species of composition comprising the antibody that is consumed by the feline, as is evidenced for example by US20070231341 A1 of record above in this office action.
Although the claims at issue are not identical, they are not patentably distinct from each other because the human, feline and Fel D1 are species recited in the method of the instant claims.
14. Claims 1-7 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2 of U.S. Patent No. 9,388,236 as evidenced by an admission in the instant specification at [0034].
The claims of US 9,388,236 are drawn to a method for reducing an allergic response in a human to Fel D1 in an environment comprising minimizing exposure to Fel D1 in the human predisposed to having an allergic response to Fel D1 by contacting the Fel D1 in the environment with a composition containing an anti-Fel D1 polyclonal antibody that inhibits the ability of Fel D1 to bind to mast cells in the human predisposed to having an allergic response to Fel D1; thereby reducing the allergic response in the human to the Fel D1 in the environment, wherein the Fel D1 in the environment is on a surface of an object that has been contacted by the cat and the composition is applied directly to the surface, wherein the composition is a liquid, aerosol or gel, and wherein the anti-Fel D1 polyclonal antibody is present at a concentration greater than 1:200,000 dilution, including wherein the composition is applied directly to the surface by a method selected from pouring, spraying, misting, wiping, shaking, dusting or depositing the composition onto the surface, including wherein the surface is a solid surface.
The admission in the instant specification at ([0034]) is that the term “antibody” as used herein includes polyclonal and monoclonal antibodies of any type and from any species, as well as immunoglobulin antigen-binding fragments such as Fv, Fab, Fab’, F(ab’)2, or other antigen-binding fragments, sequences or subsequences that interact with molecular specificity (e.g., demonstrate specific binding) with an antigen. This is relevant to the recitation in instant dependent claim 5 of “wherein the molecule is an antibody”.
Although the claims at issue are not identical, they are not patentably distinct from each other because the human, feline and Fel D1 are species recited in the method of the instant claims.
15. Claim 10 is objected to because of the following informality: ‘a” should be recited between “portion of” and “human” at the second to last line. Appropriate correction is required.
16. No claim is allowed.
17. Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARIANNE DIBRINO whose telephone number is (571)272-0842. The examiner can normally be reached on M, T, Th, F.
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/Marianne DiBrino/
Marianne DiBrino, Ph.D.
Patent Examiner
Group 1640
Technology Center 1600
/MISOOK YU/Supervisory Patent Examiner, Art Unit 1641