DETAILED ACTION
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 .
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. The present application is drawn from PCT/CA2021/051690, filed 11/25/2021; and claims benefit under 35 U.S.C. 119(e) to U.S. Provisional application 63/118306, filed 11/25/2020.
Election/Restrictions
Applicant’s election without traverse of Group I, encompassing claims 1-2, 4-5, 10, 15, 26-30, 33-35, 37, 40-41, 47-48, 54 and 61, in the reply filed on 2/11/2026 is acknowledged. Claims 62-66 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected Groups II and III, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 2/11/2026.
Similarly, applicant’s election of single species of fusion protein formulation in the reply of 2/11/2026 is acknowledged. The species of fusion protein is the “scFab-N-human light chain apoferritin”, wherein the Fab is conatumumab linked to the N-terminal half of the human light chain apoferritin; and the formulation is “Conatumumab MB” comprising the fusion protein and an additional scFv bioactive moiety in a nanocage.
Status of Claims
Claims 1-2, 4-5, 10, 15, 26-30, 33-35, 37, 40-41, 47-48, 54 and 61-66 are pending, claims 62-66 are withdrawn, and claims 1-2, 4-5, 10, 15, 26-30, 33-35, 37, 40-41, 47-48, 54 and 61 are being examined on the merits.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-2, 26-27, 33-35, 37, 40 and 61 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Yoo et al., (from IDS of 11/1/2023; Scientific Reports, published 11/17/2020).
Yoo et al. teaches ferritin nanocages displaying tumor necrosis factor-related apoptosis-inducing ligand (TRAIL); Yoo teaches TRAIL is a natural ligand for its functional receptors, DR4 or DR5. Thus, Yoo develops TRAIL-active trimer nanocages that presents the TRAIL ligand on a ferritin nanocage (abstract). Yoo teaches the ferritin nanocage is a well-studied biological nanoparticle that has been employed in various medical related applications, including targeted drug delivery and vaccine development. The ferritin nanocage is assembled from 24 monomer subunits through 2-, 3- and fourfold symmetry, thus allowing for the loading of ligands into the designated interfaces with the expected arrangement. For example, hemagglutinin has been inserted at the threefold interface of adjacent subunits such that it assembles to generate eight trimeric viral spikes on the ferritin surface, yielding a potent influenza vaccine (pg. 2, para. 3).
Specifically Yoo teaches an embodiment with a Trail ligand linked to a ferritin monomer, comprising a linker (Fig. 1A). Yoo teaches the fusion protein may also further comprise an IL4rP peptide (pg. 3, para. 1). Yoo teaches the nanocages expose N- and C- terminal fusion payloads on the surface; and that upon assembly of the 24 monomeric ferritin subunits into the cage structure, 8 TRAIL homotrimers are displayed on the surface of the ferritin nanocages. Yoo also teaches that short or long versions of ferritin subunits may be used, with flexible or rigid linkers (pg. 2, last paragraph). Yoo teaches that in embodiments in which the IL4rP peptide was added, it was added to the C-terminus of the TRAIL-ferritin monomer fusion protein, with a linker and a MMP2 cleavage site (pg. 3, para. 1).
Regarding claims 1-2 and 40, the TRAIL-ferritin monomer fusion protein of Yoo et al. anticipates a fusion protein comprising a nanocage monomer linked to a DR4/DR5 antigen binding moiety wherein the fusion proteins self-assemble to form a nanocage. As TRAIL is the natural ligand for DR4 and DR5 and binds the ectodomain of DR4 and DR5, the fusion protein of Yoo anticipates that of instant claims 1-2. As Yoo teaches the TRAIL-ferritin monomer self-assembled to generate a 24 monomeric nanocage with 8 TRAIL homotrimers displayed on the surface of the nanocage, Yoo anticipates the nanocage of instant claim 40.
Regarding claim 26-27; the fusion protein of Yoo comprises ferritin. The instant specifications define the terms “ferritin” and “apoferritin” are used interchangeably and generally refer to a ferritin chain (specs., pg. 11, para. 2). Thus, the ferritin monomer of the fusion protein of Yoo anticipates instant claims 26-27.
Regarding claims 33-35 and 37; Yoo teaches the fusion protein comprises a (G4S)n linker between the TRAIL domain and the ferritin domain (Fig. 1), and may further comprise a bioactive moiety, specifically an IL4rP peptide, which is linked to the C-terminus of the fusion protein, comprising a flexible linker (G4S)n and an MMP2 cleavage site inserted in the middle of the flexible linker (pg. 3, para. 1). Thus, the fusion protein of Yoo anticipates instant claims 33-35 and 37.
Regarding claim 61; Yoo teaches injection formulations and compositions comprising the TRAIL fusion protein nanocages for the purposes of treating breast cancer tumors and pancreatic cancer tumor bearing mice (Figs. 5-7). Thus, Yoo anticipates the compositions of instant claim 61.
Claim Rejections - 35 USC § 103
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 1-2, 4-5, 10, 26-30, 33-35, 37, 40, 47-48, 54 and 61 are rejected under 35 U.S.C. 103 as being obvious over Yoo et al., (from IDS, Cite No. C17; Scientific Reports, published 11/17/2020) and Julien et al., (from IDS, Cite No. B3; WO 2019023811; published 2/7/2019) and Dubbuisson et al., (from IDS; Cite No. C3; Antibodies, 2017).
The applied reference has a common inventor with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(1) and 102(a)(2).
The reasons why the fusion proteins and nanocages of Yoo anticipate instant claims 1-2, 26-27, 33-35, 37, 40 and 61 are described above. Specifically, Yoo teaches a TRAIL-ferritin monomer fusion protein and the resulting nanocage whereby the TRAIL is expressed on the surface of the nanocage, whereby TRAIL is a binding moiety (i.e. ligand) specific for DR4 and DR5.
However, Yoo does not teach wherein the DR4/DR5 binding moiety is an antibody, or Fab fragment; nor does Yoo teach wherein the nanocage also comprises an Fc fragment on its exterior surface.
Julien et al. teaches a nanoparticle platform for antibody and vaccine delivery (title), whereby a fusion protein comprises a nanocage monomer and an antibody or fragment thereof linked to the nanocage monomer, wherein a plurality of fusion proteins self-assemble to form a nanocage (abstract). Julien teaches wherein the antibody or fragment comprises a Fab fragment or scFv, or comprise an Fc fragment (pg. 67, claims 30-32). In example 10 (pg. 42), Julien teaches a single-chain Fc (scFv) nanoparticle design. The sequence of the scFv nanoparticle of Julien is equivalent to the scFv of instant SEQ ID NO: 60 (pg. 54) linked to a human ferritin light chain (hFTL) of instant SEQ ID NO: 56 (pg. 53), with a G4S linker. Regarding fusion proteins, Julien teaches a plurality of fusion proteins self-assemble to form a nanocage in which a plurality of the antibodies or fragments thereof decorate the exterior surface of the nanocage, whereby the antigen binding epitope is exposed for interacting with an antigen (pg. 26, lines 32-35). Julien teaches antibodies may be for example, anti-CD22 or anti-CD19 antibodies, such as Epratuzumab or Denintuzumab (pg. 29, lines 16-17), and that the fusion protein is associated with a Fab light and heavy chain which may be produced contiguously with the fusion protein (pg. 29; lines 30-33). Julien teaches the amino acid sequence for human ferritin L chain was obtained and a 12 amino acid GS linker was added to the N- and C-terminus (pg. 37, lines 30-31). Julien then teaches Fab HC-nanoparticle constructs, Fab LC and unconjugated nanoparticles, wherein the nanoparticles are ferritin, were transiently co-transfected into HEK293F cells for construction design (pg. 38, lines 12-14; see Fig. 2). Julien also teaches generating single-chain Fab-ferritin nanoparticles that only require transfection of one plasmid (pg. 7, lines 11-14; see Fig. 1C). Thus, Julien teaches the art of antibody scFab-ferritin fusion proteins, as well as scFv-ferritin fusion proteins, and the co-expression of Fab and Fc domains on the surface of nanocages comprised of self-assembled ferritin monomers.
However, Julien does not teach wherein the antibody, or Fab fragment thereof, is an antibody that binds DR4 and/or DR5, or specifically DR5.
Dubuisson et al. teaches antibodies and derivatives targeting DR4 and DR5 for cancer therapy (title). Specifically, Dubuisson teaches Conatumumab (i.e. AMG 655), is a monoclonal antibody against DR5, which has been assess in clinical trials (pg. 8, para. 3; Fig. 5). Note that Conatumumab is the anti-DR5 antibody of instant Example 1 (specs., pg. 51) and the Conatumumab LC, HC and scFab sequences are depicted in instant SEQ ID NOs: 61-62, respectively (specs., pg. 55). Further, Dubuisson teaches TRAIL proteins fused to Fc, scFv, single chains or monoclonal antibodies targeting TRAIL receptors (i.e. DR4 and/or DR5) functionalized to nanoparticles or linkers are a strategy to increase valency with the aim to increase both bioavailability and efficacy (pg. 17, para. 3).
It would have been obvious to one of skill in the art to modify the TRAIL-ferritin monomer fusion proteins of Yoo et al. to instead comprise Conatumuab Fab-ferritin monomer fusion proteins. One would have been motivated to do so in order to generate alternative nanocages expressing DR5 antigen-binding moieties for therapeutic purposes as taught by Dubuisson et al. There would have been a reasonable expectation for success given that antibody Fab fragments may be linked to ferritin monomers such that they form a nanocage expressing the Fab binding domains on the surface of the nanocage, as taught by Julien et al.; and that Conatumuab is an anti-DR5 antibody, as taught by Dubuisson et al. Thus, the invention was prima facie obvious to one of skill in the art at the time the invention was made.
Regarding claims 4-5 and 10; the combination fusion protein of Yoo, Julien and Dubuisson is described above, whereby the fusion protein comprises an anti-DR5 Conatumuab antibody Fab linked to a ferritin monomer. Thus the combination fusion protein of Yoo, Julien and Dubuisson make obvious instant claims 4-5 and 10.
Regarding claims 28-30; Julien teaches the fusion protein may comprise the ferritin light chain (pg. 37, line 30) and also teaches a scFv attached to the ferritin light chain (pg. 42, Example 10). Thus, Julien makes obvious instant claims 28-30, whereby the nanocage monomer is an apoferritin light chain, which assembles with a second monomer subunit to form the nanocage, and whereby the light chain monomer subunits comprise N and C regions of apoferritin.
Regarding claims 47-48 and 54; Julien teaches the nanocages may self-assemble from multiple identical, or multiple different, fusion proteins, and therefore be multivalent (pg. 33, lines 8-10; pg. 68, claim 39). Julien teaches fusion proteins comprising Fc fragments (pg. 68, claim 30), or scFv (pg. 42, Example 10), as well as fusion proteins comprising Fab fragments (pg. 67, claim 29). Thus, the combination nanocage comprising the fusion proteins of Yoo, Julien and Dubuisson, wherein the nanocages comprise Fab-ferritin fusion proteins and scFv-ferritin fusion proteins, such that the nanocage is decorated on the exterior surface with both a Conatumuab Fab and a scFv, makes obvious instant claim 47. Further, Julien teaches that a plurality of fusion proteins self-assemble to form a nanocage in which a plurality of the antibodies or fragments decorate the exterior surface of the nanocage (abstract). Thus, the combination of Yoo, Julien and Dubuisson make obvious instant claim 48. Julien also teaches the nanocage may also carry a diagnostic agent cargo molecule (pg. 68, claim 40); and thus makes obvious instant claim 54.
Claims 15 and 41 are rejected under 35 U.S.C. 103 as being unpatentable over Yoo et al., (from IDS, Cite No. C17; Scientific Reports, published 11/17/2020) and Julien et al., (from IDS, Cite No. B3; WO 2019023811; published 2/7/2019) and Dubbuisson et al., (from IDS; Cite No. C3; Antibodies, 2017) as applied to claims 1-2, 4-5, 10, 26-30, 33-35, 37, 40, 47-48, 54 and 61 above, and further in view of Georgiev et al., (ACS Infectious Diseases, 2018).
The combination fusion proteins and nanocages comprising an anti-CD5 antibody Fab and/or an antibody scFv, linked to a ferritin monomer, such that the fusion proteins self-assemble into a ferritin nanocage expressing the antibody fragments on the exterior surface, is described above. However, the applied references do not teach wherein the ferritin monomers are subunits of ferritin monomers.
Georgiev et al. teaches two-component ferritin nanoparticle for multimerization of diverse trimeric antigens (title). Georgiev teaches the the ferritin molecule is derived from insect Trichoplusia ni, and self-assembles with 12 copies each of heavy (HC) and light chain (LC; pg. 789, col. 1, para. 2). Georgiev teaches deleting the N-term residues for both iFerr HC and iFerr LC, to provide alternative antigen attachment points on the ferritin (pg. 789, col. 1, para. 2). Antigens were added to the subunit (iFerr) HC or the iFerr LC or both, and resulting nanocages were generated (pg. 790, Fig. 2C). Thus, Georgiev teaches ferritin monomer subunits (N-term deleted), whereby the antigen is attached to one subunit and the monomer subunits self-assemble (HC/LC) to form the nanocage.
It would have been obvious to one of skill in the art to configure the ferritin nanocage monomers with an attached antibody Fab, of the combination of Yoo, Julien and Dubuisson, to be ferritin monomer subunits. One would have been motivated to do so given that deletion the the N-terminal residues may present alternative and multiple attachment locations for adding the Fab antibody fragments to the monomers. There would have been a reasonable expectation for success given that Georgiev demonstrates both HC and LC ferritin subunits with antigen attached, whereby the subunits self-assemble. Thus, the invention was prima facie obvious to one of skill in the art at the time the invention was made.
Regarding claims 15 and 41, Georgiev demonstrates an antigen-ferritin subunit fusion protein which self-assembles with a second ferritin subunit, as part of a two component ferritin nanoparticle system. Thus the combination of Yoo, Julien and Dubuisson, using the ferritin subunits of Georgiev, make obvious the fusion proteins of instant claim 15 and the resulting nanocages of instant claim 41.
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 1-2, 4-5, 10, 26-30, 33-35, 37, 40, 47-48, 54 and 61 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 12,214,052 in view of Yoo et al., (from IDS, Cite No. C17; Scientific Reports, published 11/17/2020) and Julien et al., (from IDS, Cite No. B3; WO 2019023811; published 2/7/2019) and Dubbuisson et al., (from IDS; Cite No. C3; Antibodies, 2017).
US Patent ‘052 claims a fusion protein comprising an antibody fragment consisting of a scFv, wherein the antibody fragment is fused to a nanocage monomer via a linker (claim 1), wherein the nanocage monomer is ferritin (claim 2), with a linker (claims 3-4); as well as the resulting nanocage (claim 5), whereby the nanocage is multivalent (claim 6), and comprises 3 to 100 nanocage monomers (claim 7).
Yoo teaches a TRAIL (i.e. DR4/5 ligand) molecule attached to a ferritin monomer as a fusion protein, and the resulting ferritin nanocages expressing TRAIL on the surface. Julien teaches that antibodies, or fragments thereof, including scFv or Fab fragments, may be attached to a ferritin monomer, and results in a ferritin nanocage expressing the antibody fragments on the surface. Julien also teaches that an antibody Fc, or a scFv, can be attached to a ferritin monomer. Dubuisson teaches Conatumuab, which is an anti-DR5 antibody, from which the antigen-binding fragment, the scFv or Fab portion, may be derived. As discussed above, the combination of Yoo, Julien and Dubuisson make obvious a fusion protein comprising the Fab portion of Conatumuab and a ferritin monomer, and the resulting ferritin nanocage, expressing the Conatumuab Fab, and an antibody scFv portion, or a plurality of each, on the surface of the nanocage.
It would have been obvious to one of skill in the art to include the Conatumuab Fab/ferritin fusion protein with the scFv-ferritin fusion protein to generate multivalent ferritin nanocages expressing Conatumuab Fab and scFv on the surface of the nanocage. One would have been motivated to do so given that Conatumuab targets activation of DR5, for use of the nanocage in tumor cell therapy, as taught by Yoo and Dubuisson. There would have been a reasonable expectation for success given that antibodies and Fab fragments may be attached to ferritin monomers as fusion proteins, and that ferritin nanocages may be multivalent with multiple antibody fragments expressed on the surface, as taught by Julien et al. Thus, the invention was prima facie obvious at the time the invention was made.
The multivalent Conatumuab Fab/scFv ferritin nanocage combination of Yoo, Julien, Dubuisson, and US ‘052 claims 1-7, make obvious instant claims 1-2, 4-5, 10, 26-30, 33-35, 37, 40, 47-48, 54 and 61. The references to each limitation of the claims made obvious over the combination of Yoo, Julien, Dubuisson are described above.
Claims 1-2, 4-5, 10, 15, 26-30, 33-35, 37, 40-41, 47-48 and 61 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 6-8, 11, 14-18, 20-21, 23, 37-40, 42 and 50 of copending Application No. 18/691,258 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the scope of the claims of application ‘258 anticipate that of the instant claims.
Application ‘258 claims a self-assembled polypeptide complex comprising a plurality of first and second fusion polypeptides, wherein the first fusion is an Fc polypeptide and a nanocage monomer, and the second fusion is an antibody fragment capable of binding to DR5 and a nanocage monomer (claim 1). App ‘258 also claims wherein the nanocage monomer is ferritin (claims 2-4 and 6). App ‘258 claims wherein the self-assembled polypeptide complex comprises a C-half-ferritin and second N-half-ferritin (claims 7 and 23), whereby the Fc polypeptide is linked to the C-half ferritin’s N terminus via a linker (claim 8), wherein the Fc polypeptide is a scFv (claim 11), or comprises an IgG1 Fc chain (claim 14), which may have various mutations (claims 15-16); whereby each second fusion has the antibody fragment linked to the N-terminus (claim 17), wherein each fragment is an Fab (claim 18), whereby the polypeptide complex has a third fusion polypeptide (claims 20 and 42), which may be an Fab (claim 21), and whereby the fusion protein assembly is across various N- and C-terminal formats (claims 37-40). App ‘258 also claims a method of administering a composition comprising the polypeptide complex (i.e. nanocage; claim 50).
App ‘258 claims 1-4, 6, 11, 14-18 and 20-21 anticipate the anti-DR5 antibody fragment-ferritin monomer fusion protein of instant claims 1-2, 4-5, 10, 26-30; as well as wherein the fusion protein further comprise a bioactive moiety of instant claims 33-35 and 37; as well as wherein the nanocage further comprises one or more Fc domains (scFv) on the exterior surface of instant claims 40 and 47-48. App ‘258 claims 7-8, 23, 37-40 and 42 anticipate the split monomer format of instant claims 15 and 41. The methods of administering a composition comprising the nanocage of app ‘258 claim 50 anticipates the composition of instant claim 61.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
As described above, Yoo teaches motivation for attaching a DR4/DR5 ligand to a ferritin monomer in order to generate ferritin nanocages which express the ligand on the outer surface, for the purposes of treating cancer. Dubuisson teaches the anti-DR5 antibody Conatumuab was known in the art for treating cancer. Julien teaches that antibody fragments, including scFv, Fab and/or Fc, may be attached to ferritin monomers to generate fusion proteins which self-assemble to form ferritin nanocages expressing the antibody fragments on the outer surface of the nanocage. Julien teaches scFv constructs comprising two Fc domains linked with a G4S linker, which may be attached to a ferritin monomer. Julien teaches the nanocages may be multivariant and express a plurality of antibody fragments, i.e. dual Fab and dual scFv, on the surface of the nanocage; whereby two different fusion proteins are generated, each comprising an antibody fragment attached to an alternative ferritin monomer or subunit thereof. Julien teaches the resulting nanocages, expressing the plurality of two different antibody fragments (i.e. Fab and scFv) on the outer surface. Julien also teaches wherein the nanocage carries a cargo molecule, and compositions comprising the nanocages. Thus, the combination of Yoo, Julien and Dubuisson make obvious an “anti-DR5 Conatumuab Fab-ferritin monomer” fusion protein and ferritin nanocages expressing the anti-DR5 Fab on the surface; as well as each of the instant claims as described in the prior art 103 rejections above.
Therefore, any co-pending application or issued patent that claims an antibody fragment/ferritin monomer fusion protein, and the resulting ferritin nanocage, makes obvious the instant claims in view of the triple combination DR5 antibody/ferritin fusion proteins and nanocages of Yoo, Julien and Dubuisson.
Claims 1-2, 4-5, 10, 26-30, 33-35, 37, 40, 47-48, 54 and 61 are provisionally rejected over the listed claims of the following pending applications, in view of Yoo et al., (from IDS, Cite No. C17; Scientific Reports, published 11/17/2020) and Julien et al., (from IDS, Cite No. B3; WO 2019023811; published 2/7/2019) and Dubbuisson et al., (from IDS; Cite No. C3; Antibodies, 2017). In applications which claim “split ferritin monomer subunits”, instant claims 15 and 41 are also rejected.
Below is a Table listing patents and/or co-pending applications, which name a common inventor, and which claim a fusion protein comprising an antibody fragment linked to a ferritin monomer, whereby the fusion proteins self-assemble into a ferritin nanocage expressing the antibody fragment on the outer surface. In some cases there are two fusion proteins in a polypeptide complex, whereby the resulting nanocage expresses two or more antibody fragments on the outer surface. In each case the co-pending claims would make obvious, over Yoo, Julien and Dubuisson, instant claim 1, and all dependent claims, for the same reasons why Yoo, Julien and Dubuisson make obvious the instant claims as described above.
U.S. Patent or co-pending U.S. application
Claims
Comment
18/578239
1-5, 7, 9, 14-23, 54, 64-69, 71-77
Plurality of (non-CD19) antibody-ferritin and Fc-ferritin fusion proteins; with mutated Fc domains
18/701187
1, 3-15, 17-21, 24, 29-31, 33-39, 51
Plurality of (SARS-CoV-2) antibody-ferritin and Fc-ferritin fusion proteins; with mutated Fc domains. Split ferritin monomer subunits.
18/701020
1-79
IgG4 Fc-ferritin and (generic) antibody-ferritin fusion proteins; with mutated Fc domains. Split ferritin monomer subunits. Compositions and methods.
18/691267
1-8, 11, 14-20, 22, 25-26, 28-29, 31, 44-47, 49, 55
IgG1 Fc-ferritin and (generic) antibody-ferritin fusion proteins; with mutated Fc domains. Split ferritin monomer subunits.
18/263217
1-7, 9-10, 14-16, 19-20, 35-39, 50, 77, 110-112, 125, 152
Fc-ferritin and (HIV-1) antibody-ferritin fusion proteins; with mutated Fc domains. Split ferritin monomer subunits.
17/631588
1, 4, 6-7, 35-36, 61, 97-98, 115-116
Fc-ferritin and (HIV-1) antibody-ferritin fusion proteins; with mutated Fc domains. Split ferritin monomer subunits.
18/030944
1-2, 4-12, 21-23, 26-28, 30, 32-33, 35-41, 45-46, 50, 53, 57, 67-70, 83, 100, 103
(SARS-CoV-2) antibody-ferritin and Fc-ferritin fusion proteins; with mutated Fc domains.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JAMES R. MELCHIOR whose telephone number is (703)756-4761. The examiner can normally be reached M-F 8:00-5:00 CST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Samira Jean-Louis can be reached at (571) 270-3503. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/JAMES RYLAND MELCHIOR/Examiner, Art Unit 1644
/NELSON B MOSELEY II/Primary Examiner, Art Unit 1642
Prosecution Insights