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
The amendment filed on 8-13-2025 is acknowledged. Claims 2 and 7 have been amended. Claim 23 has been added. Claims 2, 4-7 and 20-23 are pending. In light of the current claim construction and to facilitate compact prosecution, claims 20 and 21, previously withdrawn from consideration as a result of a restriction requirement, are hereby rejoined and fully examined for patentability under 37 CFR 1.104. Because a claimed invention previously withdrawn from consideration under 37 CFR 1.142 has been rejoined, the restriction requirement among groups I, IV and VI as set forth in the Office action mailed on 4-19-2023 is hereby withdrawn. In view of the withdrawal of the restriction requirement as to the rejoined inventions, applicant(s) are advised that if any claim presented in a divisional application is anticipated by, or includes all the limitations of, a claim that is allowable in the present application, such claim may be subject to provisional statutory and/or nonstatutory double patenting rejections over the claims of the instant application.
Once the restriction requirement is withdrawn, the provisions of 35 U.S.C. 121 are no longer applicable. See In re Ziegler, 443 F.2d 1211, 1215, 170 USPQ 129, 131-32 (CCPA 1971). See also MPEP § 804.01.
Consequently, claims 2, 4-7 and 20-23 are currently under examination
Information Disclosure Statement
The Information Disclosure Statement filed on 8-13-2025 has been considered. An initialed copy is attached hereto. It should be noted that the reference cited on said Information Disclosure Statement had been previously cited on the Information Disclosure Statement filed on 5-25-2025 and considered in the Office action filed on 9-13-2025.
It should be noted that the listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Priority
In light of the amendment to the specification, Applicant's claim for receiving the benefit of an earlier filing date under 35 U.S.C. 120 and 119 (e) is deemed perfected. It should be noted that the date used for the availability of art regarding the instant claims is as follows:
For claims drawn to the use of Dirofilaria immitis antigens the effective filing date of Application 16/790,277 (2-13-2020) will be used.
For claims drawn to the use of fusion proteins comprising four Brugia malayi antigens; fusion proteins comprising Abundant Larval Transcript, Tetraspanin, Small heat shock protein (HSP) 12.6, and Thioredoxin Peroxidase 2 generally; and fusion proteins comprising the sequences of SEQ ID NO:37, SEQ ID NO:49, SEQ ID NO:63 and SEQ ID NO:71, specifically, the effective filing date of Application 14/798,945 (7/14/2015) will be used.
Claim Rejections Maintained
35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 7 and 20-21 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 for essentially the reasons set forth in the previous Office action in the rejection of claim 7. 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.
Applicant argues:
1. Claim 7 is now limited to a group of antigens with specific sequences.
2. Examples clearly provide data showing the generation of an antigen-specific antibody response to a number of different antigens including Brugia malayi and Dirofilaria immitis Small heat shock protein (HSP) 12.6, B. malayi and D. immitis Abundant Larval Transcript (ALT2), B. malayi Vespid Venom Allergen homologue-Like protein (VAL-1), B. malayi and D. immitis Thioredoxin Peroxidase 2 (TPX2), B. malayi and O. volvulus Tetraspanin (TSP) (see, e.g., paragraphs [00142], [00145]-[00146], [00158], [00176]-[00179], [00198], [00199], [00208], [00238], [00239], [00257], [00258], [00280], [00281], [00289], and [00293]) and an antigen-specific memory T cell response (see, e.g., paragraphs [00148], [00180], [00202], [00231]-[00233], [00236], [00260]-[00262], [00282], and [00295]) in mice, macaques, jirds, and dogs, as well as methods and compositions for measuring/determining such responses (see, e.g., paragraphs [00122], [00125], [00131], [00154], [00167], [00171]-[00173], [00189], [00190], [00194], [00216], [00220], [00224], [00250], [00251], [00254], [00255], [00269], and [00272]-[00274]). Accordingly, the specification clearly describes the claimed invention in
sufficient detail that one skilled in the art would reasonably conclude that the inventor had possession of the claimed invention at the time of filing of the application.
Applicant’s arguments have been fully considered and deemed non-persuasive.
With regard to Point 1, the amendment to claim 7 is insufficient to overcome the rejection as there is no limitation regarding the order of the component antigens. Moreover, the use of the phrase “selected from the group consisting of” indicates that you can have multiple instances of the same antigen in the claimed fusion protein (i.e. two or more ALT proteins etc.). Additionally, there is no limitation with regard to the specific antigens or their order in claims 20 and 21
With regard to Point 2, the cited portions of the specification either refer to the recited antigens in general and prophetic terms or refer to antigens with specific sequences. For example the portions of the specification dealing with rBmHAXT tetravalent fusion proteins are limited to the bmhsp12.6 antigen with the sequence set forth in GENBNAK Accession No. AY692227.1, the bmalt-2 antigen with the sequence set forth in GENBNAK Accession No. JF795950.1, the
bmtpx-2 antigen with the sequence set forth in GENBNAK Accession No. AF319997.1 and the bmtsp antigen with the sequence set forth in GENBNAK Accession No. JF795955.1. This disclosure cannot be extrapolated to the full breadth of the rejected claim as there is no limitation with regard to the sequence any additional antigens or the order in which the antigens are ordered within the claimed fusion protein.
As outlined previously, the instant claim is interpreted as being drawn (in part) to fusion proteins comprising four antigens isolated from Brugia malayi or Dirofilaria immitis wherein said fusion protein induces an antigen-specific antibody response or antigen-specific memory T cell response (claim 7); decreases Brugia malayi or Dirofilaria immitis larval viability in a subject (claim 20); or reduces establishment of adult Brugia malayi or Dirofilaria immitis in a subject (claim 21).
The claims are drawn to a vast genus of fusion proteins comprising one or more instances of the proteins with the amino acid sequences of SEQ ID NO:37, SEQ ID NO:49, SEQ ID NO:63 and SEQ ID NO:71 (in no particular order) or comprise unnamed antigens from either Brugia malayi or Dirofilaria immitis. To fulfill the written description requirements set forth under U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, the specification must describe at least a substantial number of the members of the claimed genus, or alternatively describe a representative member of the claimed genus, which shares a particularly defining feature common to at least a substantial number of the members of the claimed genus, which would enable the skilled artisan to immediately recognize and distinguish its members from others, so as to reasonably convey to the skilled artisan that Applicant has possession the claimed invention. To adequately describe the genus of fusion proteins with the claimed immunological characteristics, Applicant must adequately describe not only the specific antigens making up the fusion proteins but the order of the recited antigens within the fusion proteins which would induce a given immune response. The specification, however, does not disclose distinguishing and identifying features of a representative number of members of the genus of fusion proteins to which the claims are drawn, such as a correlation between the structure (sequence) and its recited function (inducing a given immune response), so that the skilled artisan could immediately envision, or recognize at least a substantial number of members of the claimed genus of fusion proteins. The specification is limited to the disclosure of rBmHAT, rBmHAX, rBmHAXT and rDiHAX fusion proteins which are made up of specific ALT2, Tetraspanin antigen, Small heat shock protein (HSP) and the Thioredoxin Peroxidase 2 protein but is silent with regard to fusion proteins comprising any other antigens or any other configuration of aforementioned antigens. The specification is equally silent with regard to what (if any) antigens (sequences) can be present between the recited antigen components or the particular order in which said antigens must be presented within the fusion protein. The art recognizes that defining epitopes is not easy and there is a confusing divergence between the textbook definition of epitope and the definition that is in use in published descriptions of experimental investigations and that epitopes must be empirically determined (Greenspan et al, Nature Biotechnology 17:936-937, 1999). Antibody epitopes are characterized by the art as either continuous or discontinuous (see pages 23-25, 27-33, Harlow et al, (Antibodies A Laboratory Manual, Cold Spring Harbor Laboratory Press Inc., 1988). T cell epitopes are continuous peptide fragments of a polypeptide or antigen that have been processed by an accessory cell. Colman et al. (Research in Immunology 145: 33-36, 1994, p.33 column 2, p. 35 column 1) disclose that a single amino acid change in an antigen can effectively abolish the interaction with an antibody entirely and that a very conservative amino acid substitution may abolish antibody binding and a non-conservative amino substitution may have little effect in antibody binding. This underlies the importance of the description of the immunoepitopes that are protective and which and where and how many changes can the immunoepitopes tolerate and still retain the ability to raise an immune response against any Staphylococcus bacterium. Houghten et al. (New Approaches to Immunization, Vaccines 86, Cold Spring Harbor Laboratory, p. 21-25, 1986) taught the criticality of individual amino acid residues and their positions in peptide antigen-antibody interactions. Houghten et al. state (see page 24): "One could expect point mutations in the protein antigen to cause varying degrees of loss of protection, depending on the relative importance of the binding interaction of the altered residue. A protein having multiple antigenic sites, multiple point mutations, or accumulated point mutations at key residues could create a new antigen that is precipitously or progressively unrecognizable by any of the antibodies in the polyclonal pool. Even though one could screen the encompassed fusion proteins for the ability to elicit a protective immune response against M. tuberculosis, the courts have held that possession of a genus may not be shown by merely describing how to obtain members of the claimed genus or how to identify their common structural features. The written description requirement is separate and distinct from the enablement requirement (See also Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920-23, 69 USPQ2d 1886, 1890-93 (Fed. Cir. 2004) and adequate written description requires more than a mere reference to a potential method for identifying candidate polypeptides. The purpose of the written description requirement is broader than to merely explain how to ‘make and use’ [the invention] Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1560, 19 USPQ2d 1111, 1114 (Fed. Cir. 1991). The disclosure of only one member of the genus to which the claims are drawn is insufficient to describe the large and variant genus of proteins the scope of which is set forth above. In such an unpredictable art, as set forth supra, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus. See Noelle v Lederman. 355 F. 3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) and In re Alonso (Fed. Cir. 2008-1079). Therefore, the specification fails to adequately describe at least a substantial number of members of the genus fusion proteins to which the claims refer; and accordingly, the specification fails to adequately describe at least a substantial number of members of the claimed genus of fusion proteins.
MPEP § 2163.02 states, “[a]n objective standard for determining compliance with the written description requirement is, 'does the description clearly allow persons of ordinary skill in the art to recognize that he or she invented what is claimed' ”. The courts have decided:
The purpose of the “written description” requirement is broader than to merely explain how to “make and use”; the applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the “written description” inquiry, whatever is now claimed.
See Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1563-64, 19 USPQ2d 1111, 1117 (Federal Circuit, 1991). Furthermore, the written description provision of 35 USC § 112 is severable from its enablement provision; and adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
MPEP 2163.02 further 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” See, e.g., Pfaff v. Wells Elecs., Inc., 525 U.S. 55, 68, 119 S.Ct. 304, 312, 48 USPQ2d 1641, 1647 (1998); Regents of the Univ. of Cal. v. Eli Lilly, 119 F.3d 1559, 1568, 43 USPQ2d 1398, 1406 (Fed. Cir. 1997); 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"). Moreover, because the claims encompass a genus of variant species, 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. However, factual evidence of an actual reduction to practice has not been disclosed by Applicant in the specification; nor has Applicant shown the invention was “ready for patenting” by disclosure of drawings or structural chemical formulas that show that the invention was complete; nor has Applicant described distinguishing identifying characteristics sufficient to show that Applicant were in possession of the claimed invention at the time the application was filed.
Additionally, MPEP 2163 states:
"A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed." In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004)”
And:
For 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. See, e.g., Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are "representative of the full variety or scope of the genus," or by the establishment of "a reasonable structure-function correlation." Such correlations may be established "by the inventor as described in the specification," or they may be "known in the art at the time of the filing date." See AbbVie, 759 F.3d at 1300-01, 111 USPQ2d 1780, 1790-91 (Fed. Cir. 2014) (Holding that claims to all human antibodies that bind IL-12 with a particular binding affinity rate constant (i.e., koff) were not adequately supported by a specification describing only a single type of human antibody having the claimed features because the disclosed antibody was not representative of other types of antibodies in the claimed genus, as demonstrated by the fact that other disclosed antibodies had different types of heavy and light chains, and shared only a 50% sequence similarity in their variable regions with the disclosed antibodies.).
As evidenced by the teachings of Skolnick et al., the art is unpredictable. Skolnick et al. (Trends in Biotechnology 18: 34-39, 2000) discloses the skilled artisan is well aware that assigning functional activities for any particular protein or protein family based upon sequence homology is inaccurate, in part because of the multifunctional nature of proteins (see, e.g., the abstract; and page 34, Sequence-based approaches to function prediction). Even in situations where there is some confidence of a similar overall structure between two proteins, only experimental research can confirm the artisan's best guess as to the function of the structurally related protein (see, in particular, the abstract and Box 2). Thus, one skilled in the art would not accept the assertion, which is based only upon an observed similarity in amino acid sequence that a variant of a given polypeptide would necessarily have a given immunological property. Consequently, there is no correlation between structure and function as required by the Written Description requirement.
Therefore, because the art is unpredictable, in accordance with the MPEP, the description of claimed fusion proteins is not deemed representative of the genus of vaccines to which the claim refers.
35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 22-23 are rejected under 35 U.S.C. 103 as being unpatentable over Grieve et al. (WO 94/15593 – IDS filed on 9-7-2022) and Dakshinamoorthy et al. (Vaccine Vol. 32, pages 19-25) for the reasons set forth in the previous Office action in the rejection of claims 4-7.
Applicant argues:
1. Grieve and Dakshinamoorthy do not teach or suggest the administration of a recombinant multivalent immunogenic composition comprising four antigens as claimed.
Applicant’s arguments have been fully considered and deemed non-persuasive.
With regard to Point 1, the rejected claims are not limited to “four antigens” but encompass all fusion proteins comprising “…three or four antigens isolated from Brugia malayi or Dirofilaria immitis.”.
As outlined previously, Grieve et al. disclose the administration of compositions comprising multiple parasitic nematode antigens generally and D. immitis proteins, specifically (see abstract, page 13, lines 7-18 and page 64, lines 1-18 for example). Grieve et al. further disclose that their compositions can comprise adjuvants and that said adjuvants can be an aluminum salt, a calcium salt, silica, a saponin, toxoids or a block polymer (see page 65, line 24 to page 66, line 16); that said compositions can be administered multiple time (see page 67, line 14 to page 68, line 9); and that said compositions induce antigen specific responses (see page 72, line 8-14).
Grieve et al. differs from the rejected claims in that they don’t explicitly disclose that their antigens are covalently linked to form a fusion protein or the use of multiple adjuvants.
Dakshinamoorthy et al. disclose the use of fusion proteins comprising Brugia malayi antigens Hsp12.6, ALT-2 and TSP LEL (see abstract). Dakshinamoorthy et al. further disclose the use of their fusion proteins in vaccine compositions comprising a combination of adjuvants (i.e. AL007 and TLR4 agonist AL019)[see section 2.3 on page 20) and that said vaccine compositions were greater than 95% effective (see abstract).
It would have been obvious for one of ordinary skill in the art to administer the antigens of Grieve et al. in the form of a fusion protein in order to take advantage of the increased immunogenicity of fusion proteins (as demonstrated by Dakshinamoorthy et al.).
One would have had a reasonable expectation of success as Dakshinamoorthy et al. disclose that their fusion methodologies can be applied to multiple antigens.
Claims 2, 4-6 and 20-23 are rejected under 35 U.S.C. 103 as being unpatentable over Samykutty et al. (Procedia in Vaccinology Vol. 3, pages 8-12 – IDS filed on 5-25-2022); Chandrashekar (WO 98/52971 – IDS filed on 9-7-2022) and Dakshinamoorthy et al. (Vaccine Vol. 32, pages 19-25) for the reasons set forth in the previous Office action in the rejection of claims 2 and 4-7.
Applicant argues:
1. Dakshinamoorthy published in December of 2013 and is therefore not a valid prior art reference as applied to the Brugia malayi antigens of at least Samykutty.
2. Samykutty describes the expression of individual recombinant antigens, rBmHSP and rBMAL-2, and vaccination of mice with the same. Samykutty, page 13, 3rd full paragraph. Chandrashekar describes the preparation of recombinant TPx-2 protein. Chandrashekar, page 42, Example 2. Dakshinamoorthy describes immunizing an animal with a multivalent vaccine protein referred to as rBmHATαc, which is composed of rBmHSP12.6, rBmALT-2 and rBmTSP LEL. Dakshinamoorthy, abstract. However, none of these references teach or suggest a recombinant multivalent immunogenic composition comprising four antigens isolated from Brugia malayi or Dirofilaria immitis, wherein the antigens are covalently attached to each other without a spacer between the antigens thereby forming a fusion protein.
Applicant’s arguments have been fully considered and deemed non-persuasive.
With regard to Point 1, the priority date for the instant invention (i.e. fusion proteins comprising four Brugia malayi antigens is the effective filing date of Application 14/798,945 (7/14/2015). Hence, the reference by Dakshinamoorthy et al. is valid prior art.
With regard to Point 2, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). Dakshinamoorthy et al. disclose the use of fusion proteins comprising Brugia malayi antigens Hsp12.6, ALT-2 and TSP LEL; Samykutty et al. disclose a multivalent vaccine form lymphatic filariasis comprising Brugia malayi BmALT-2 and BmHSP proteins; and Chandrashekar discloses vaccine compositions comprising the Brugia malayi Thioredoxin peroxidase 2 (TPx-2) protein. Their teachings make it obvious for the skilled artisan to use the Brugia malayi BmALT-2 and BmHSP proteins of Samykutty et al. and the Brugia malayi Thioredoxin peroxidase 2 of Chandrashekar in a single fusion protein for use in a nematode vaccine composition in order to take advantage of the increased immunogenicity of fusion proteins (as disclosed by demonstrated by Dakshinamoorthy et al.).
Samykutty et al. disclose a multivalent vaccine form lymphatic filariasis comprising Brugia malayi BmALT-2 and BmHSP proteins (see abstract).
Samkutty et al. differs from the rejected claims in that they don’t explicitly disclose: the use of the Thioredoxin peroxidase 2 (TPx-2) protein; that their antigens are covalently linked to form a fusion protein; or the use of multiple adjuvants.
Chandrashekar discloses vaccine compositions comprising the Brugia malayi Thioredoxin peroxidase 2 (TPx-2) protein (see abstract and page 4, lines 21-22). Chandrashekar further discloses that their compositions can comprise an adjuvant (see page 5, lines 15-17); that said adjuvants can be an aluminum salt, a calcium salt, silica, a saponin, toxoids, cytokines, chemokines, viral coat proteins or a block polymer (see page 30, line 15 to page 31, line 4); that their compositions can be administered more than once (see page 32 lines 11-30); and that their compositions induce antigen specific responses (see page 35, line 6-9).
Dakshinamoorthy et al. disclose the use of fusion proteins comprising Brugia malayi antigens Hsp12.6, ALT-2 and TSP LEL (see abstract). Dakshinamoorthy et al. further disclose the use of their fusion proteins in vaccine compositions comprising a combination of adjuvants (i.e. AL007 and TLR4 agonist AL019)[see section 2.3 on page 20) and that said vaccine compositions were greater than 95% effective (see abstract).
Consequently, it would have been obvious for the skilled artisan to use the Brugia malayi BmALT-2 and BmHSP proteins of Samykutty et al. and the Brugia malayi Thioredoxin peroxidase 2 of Chandrashekar in a single fusion protein for use in a nematode vaccine composition in order to take advantage of the increased immunogenicity of fusion proteins (as disclosed by demonstrated by Dakshinamoorthy et al.).
With regard to the specific sequences recited in claim 2, it is deemed in absence of the contrary, that given the disclosed proteins and the claimed proteins are the same they would necessarily have the same sequences.
Claims 2, 4-6 and 20-23 are rejected under 35 U.S.C. 103 as being unpatentable over Dakshinamoorthy et al. (Vaccine Vol. 32, pages 2013) and Chandrashekar (WO 98/52971 – IDS filed on 9-72022) for the reasons set forth in the previous Office action in the rejection of claims 2 and 4-7. It should be noted that Applicant did not directly address this rejection in their response.
As outlined previously, Dakshinamoorthy et al. disclose the use of fusion proteins comprising Brugia malayi antigens Hsp12.6, ALT-2 and TSP LEL (see abstract). Dakshinamoorthy et al. further disclose the use of their fusion proteins in vaccine compositions comprising a combination of adjuvants (i.e. AL007 and TLR4 agonist AL019)[see section 2.3 on page 20) and that said vaccine compositions were greater than 95% effective (see abstract).
Chandrashekar discloses vaccine compositions comprising the Brugia malayi Thioredoxin peroxidase 2 (TPx-2) protein (see abstract and page 4, lines 21-22). Chandrashekar further discloses that their compositions can comprise an adjuvant (see page 5, lines 15-17); that said adjuvants can be an aluminum salt, a calcium salt, silica, a saponin, toxoids, cytokines, chemokines, viral coat proteins or a block polymer (see page 30, line 15 to page 31, line 4); that their compositions can be administered more than once (see page 32 lines 11-30); and that their compositions induce antigen specific responses (see page 35, line 6-9).
It would have been obvious for the skilled artisan to use the Brugia malayi Thioredoxin peroxidase 2 of Chandrashekar in the fusion protein of Dakshinamoorthy et al.) to form a single multimeric fusion protein for use in a nematode vaccine composition in order to take advantage of the increased immunogenicity of multimeric fusion proteins (as disclosed by demonstrated by Dakshinamoorthy et al.).
With regard to the specific sequences recited in claim 2, it is deemed in absence of the contrary, that given the disclosed proteins and the claimed proteins are the same they would necessarily have the same sequences.
New Grounds of Rejection
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 2, 4-6 and 20-23 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 7-12 of U.S. Patent No. 12,419,939. Although the claims at issue are not identical, they are not patentably distinct from each other because both claim sets are drawn to methods of inducing various immune response through the administration of compositions comprising an Abundant Larval Transcript antigen, a HSP 12.6 antigen and a Thioredoxin Peroxidase and two or more adjuvants. It should be noted that while the patented claims do not explicitly disclose that the various antigens are covalently attached it is an obvious option as evidenced by patented claim 4.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ROBERT A ZEMAN whose telephone number is (571)272-0866. The examiner can normally be reached on Monday thru Friday; 6:30 am - 3pm EST.
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/ROBERT A ZEMAN/Primary Examiner, Art Unit 1645 November 12, 2025
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