DETAILED ACTION
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Applicant’s Request for Continued Examination, Amendment and Arguments/Remarks received on 12 August 2026 have been entered.
Claims 1-4, 6, 8-9, 26, 29-32, 34, 45, 48, and 54-61 were previously pending in the application. Claims 29 and 34 have been cancelled, and no new claims have been added by Applicant. Claims 1-4, 6, 8-9, 26, 30-32, 45, 48, and 54-61 are currently pending in the application. Claims 1, 45, 54, 55, 56, 57, and 58 are independent claims.
The election of the following species remains in effect in the instant application:
Fusion partner to a cell surface marker specific VHH: b) an adeno-associated virus (AAV) capsid protein.
Claims 2-4, 6, 8, and 26 remain withdrawn from consideration as being directed to a nonelected species. Claims 1, 9, 30-32, 45, 48, and 54-61 are currently pending and under examination in the instant application. An action on the merits follows.
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA . The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Priority
The present application is a 35 U.S.C. 371 national stage filing of International Application No. PCT/EP2019/061295, filed 02 May 2019, which claims priority to EPO 18170659.9, filed 03 May 2018. Filing of a certified copy of the EPO 18170659.9, filed 03 May 2018 is acknowledged.
Thus, the earliest possible priority for the instant application is 03 May 2018.
Claim Objections
Previously presented claim 60 is newly objected to because of the following informalities: claim 60 is dependent on cancelled claim 34. Therefore, the actual structural elements which Applicant intends to claim as part of the invention cannot be determined. Appropriate correction is required. Further examination of this claim under 35 U.S.C. 101, 102, 103, 112(a), and double patenting is precluded.
Claim Rejections - 35 USC § 112(b)
The rejection of amended claim 57 under 35 U.S.C. 112(b) as failing to particularly point out and distinctly claim the subject matter which the inventor(s) regards as the invention for reciting “increasing transduction efficiency of a target cell”, is withdrawn.
Amended and previously presented claims 1, 9, 30-32, 45, 48, and 54-61 are newly rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claims 9, 30-32, 45, 48, 54-56, and 61 are included in this rejection due to their dependence on and/or encompassing of claims 1, 57, 58, and/or 60.
Amended independent claim 1 recites, “at an amnio acid position that is or corresponds to position 453-459 of viral protein 1 (VP1)” in lines 4-5. Amended and previously presented claims 57 and 58 each also each recite, “at an amnio acid position that is or corresponds to position 453-459 of viral protein 1 (VP1)” in lines 10-11 and 13-14, respectively. However, none of claims 1, 57, nor 58 recite a reference sequence for the position numbers to determine the sequence intended to be encompassed by the range of amino acids 453-459. Additionally, the claims do not recite a reference serotype for VP1 to which the recited position numbers correspond. As such, the metes and bounds of the claim cannot be determined.
Claim 60 recites, “The fusion protein according to claim 34” in line 1. However, claim 34 is cancelled, and, therefore, claim 60 is indefinite because the actual structural elements which Applicant intends to claim as part of the invention cannot be determined. Further examination of these claims under 35 U.S.C. 101, 102, 103, 112(a), and double patenting is precluded.
Claim Rejections - 35 USC § 112(a)- New Matter
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.
Amended and previously presented claims 1, 9, 30-32, 45, 48, and 54-61 are newly 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 new matter rejection.
The Applicant is reminded that an amendment to the claims or the addition of a new claim must be supported by the description of the invention in the application as filed. In re Wright, 866 F.2d 422, 9 USPQ2d 1649 (Fed. Cir. 1989). New or amended claims which introduce elements or limitations which are not supported by the as-filed disclosure violate the written description requirement. See, e.g., In re Lukach, 442 F.2d 967, 169 USPQ 795 (CCPA 1971); In re Smith, 458 F.2d 1389, 1395, 173 USPQ 679, 683 (CCPA 1972).
Amended independent claim 1 newly recites, “between any two amino acids at an amino acid position that is or corresponds to position 453-459 of viral protein 1(VP1)” in lines 4-5. Amended and previously presented claims 57 and 58 each also each recite, “between any two amino acids at an amnio acid position that is or corresponds to position 453-459 of viral protein 1 (VP1)” in lines 10-11 and 12-14, respectively, wherein “between any two amino acids” was added in a previous claims amendment filed 29 December 2025. However, the instant disclosure as filed does not provide any teachings of insertions between any two amino acids at a position that is or corresponds to position 453-459 of VP1.
The specification teaches only a single insertion into an AAV capsid protein, wherein a VHH coding sequence is inserted into the pRC_RR_VP1_r1c3 plasmid by restriction digestion with NgoMIV and KasI and subsequent ligation and transformation [pg 25 ln 24- pg 26 ln 8, Figure 2]. The drawings depict a nanobody insertion between NgoMIV and KasI sites [Figure 2B].
Judd teaches that the VP1-mCherry vector, pRC_RR_VP1_r1c3, contains mCherry in place of the deleted amino acid sequence 453-GTTTQSR-459 according to VP1 numbering, wherein flanking NgoMIV and KasI restriction sites allow the mCherry to be easily replaced with sequences encoding other peptides of interest [Judd et al. 2012, Molecular Therapy- Nucleic Acids, 1, e54, 1-10, IDS, cited in a prior action, pg 2 col 1 ¶ 4- col 2 ¶ 1, pg 4 col 1 ¶ 1- col 2 ¶ 1, pg 8 col 1 ¶ 2]. Therefore, the instant disclosure teaches only replacing mCherry with the VHH domain, which amounts to a replacement of amino acids 453-459 within the VP1 capsid protein. The instant disclosure does not teach to insert the VHH domain between any two amino acids within the range of 453-459, but only to replace the full range of 453-459 with the inserted sequence.
Therefore, the disclosure does not provide support for the limitations newly added to amended independent claim 1 of “between any two amino acids at an amino acid position that is or corresponds to position 453-459 of viral protein 1(VP1)”, and which was previously added to amended and previously presented claims 57 and 58, and the limitation represents new matter.
Claim Rejections - 35 USC § 103
The rejection of amended, previously presented, and cancelled claims 1, 9, 29-32, 34, 45, 48, and 54-61 under 35 U.S.C. 103 as being unpatentable over Judd et al. 2012, Molecular Therapy- Nucleic Acids, 1, e54, 1-10, IDS; Muik et al. 2017, Biomaterials, 144, 84-94; Kaliberov et al. 2014, Lab Invest., Vol. 94(8), 893-905, cited in a prior action; Benchimol et al. 1989, Cell, Vol. 57(2), 327-334, cited in a prior action; and Hefta et al. 1988, Proceedings of the National Academy of Science, Vol. 85(13), 4648-4652, cited in a prior action, is withdrawn.
Amended and previously presented claims 1, 9, 30-32, 45, 48, and 54-61 are newly rejected under 35 U.S.C. 103 as being unpatentable over Judd et al. [2012, Molecular Therapy- Nucleic Acids, 1, e54, 1-10, IDS, cited in a prior action]; in view of Hallek [US20070238684A1, published 11 October 2007]; Kaliberov et al. [2014, Lab Invest., Vol. 94(8), 893-905, cited in a prior action]; Benchimol et al. [1989, Cell, Vol. 57(2), 327-334, cited in a prior action]; and Hefta et al. [1988, Proceedings of the National Academy of Science, Vol. 85(13), 4648-4652, cited in a prior action].
Regarding claims 1 and 30-32, Judd teaches a fusion protein (e.g., the r1c3 mutant) comprising an adeno-associated virus serotype 2 (AAV2) capsid protein VP1 and a second protein (e.g., mCherry), wherein the mCherry protein is inserted into an exposed loop of the AAV capsid protein at an amino acid position that is or corresponds to position 453-459 of VP1 (e.g., wherein the mCherry replaces amino acids 453-459) [column 7 ¶ 1- column 8 ¶ 1]. Judd also teaches that genetic insertion into the AAV capsid may be used to achieve vector retargeting, reduced immunogenicity, or to track vector transport [abstract]. Judd further teaches that the 453-459 site was identified within the VP3 shared region that can tolerate insertion of the large functional protein domain, mCherry, and maintain native infectivity while displaying robust fluorescence [abstract]. Judd teaches that alterations to the viral capsid protein have been made to retarget native tropism, and that genetic alterations have the advantages of relatively uniform end produces, ease of production, reduced cost, and avoidance of potentially toxic synthetic chemicals [column 1 ¶ 2- column 2 ¶ 1]. Judd teaches that encoding of large protein domains in general in the GH2/3 loop may offer improved vector performance [column 11 ¶ 2], and that the successful insertion of mCherry into the surface of the AAV2 capsid without affecting virus infectivity has important implications for future vector design with other protein domains once thought too large to incorporate into AAV [column 13 ¶ 2].
Further, Judd teaches that the VP1-mCherry vector, pRC_RR_VP1_r1c3, contains mCherry in place of the deleted amino acid sequence 453-459 according to VP1 numbering, wherein flanking NgoMIV and KasI restriction sites allow the mCherry to be easily replaced with sequences encoding other peptides of interest [pg 2 col 1 ¶ 4- col 2 ¶ 1, pg 4 col 1 ¶ 1- col 2 ¶ 1, pg 8 col 1 ¶ 2].
Judd does not teach that the second protein inserted into an exposed loop of the AAV capsid protein is a cell surface marker specific VHH.
However, Hallek teaches a fusion protein comprising an AAV VP1 capsid protein with an insertion of a cell membrane receptor ligand within a surface loop that is sufficiently flexible to withstand insertion without destabilizing the secondary structural elements of the AAV2 capsid protein, such as an insertion following amino acid 452 according to AAV2 VP1 numbering [0011-0012, 0015-0016, 0052-0060]. Hallek also teaches wherein the cell membrane receptor ligand inserted is a single chain antibody (scFv) which binds to cell surface receptors [0017]. Hallek additionally teaches wherein the inserted ligands allow targeting to specific cells and increased infectivity to facilitate more specific and more efficient gene transfer than with previously known AAV vectors [0008-0011]. Therefore, an ordinarily skilled artisan at the time of filing the instant application would have been motivated to insert an scFv into an AAV capsid protein in a flexible surface loop to target the AAV to a specific cell type for more specific and more efficient gene transfer.
Additionally, Kaliberov teaches that camelid heavy-chain-only antibodies (hcAbs) contain characteristics ideal for viral vector retargeting strategies: 1) cytosolic stability allowing functional incorporation into the viral capsid and 2) compatibility with phage biopanning selection to allow target cell specificity [column 3 ¶ 3]. Kaliberov also teaches that hcAbs contain a single variable domain (VHH) linked to two constant domains; that cloned and isolated single domain antibodies have shown a remarkable stability profile compared with conventional Igs and scFVs; and that engineered single domain antibody (sdAb) fusion proteins have demonstrated effective targeting in model systems [column 3 ¶ 3]. Kaliberov also teaches the validation of targeted gene delivery using adenovirus vector with capsid incorporated with VHH [column 4 ¶ 1]. Therefore, an ordinarily skilled artisan at the time of filing the instant application would have been motivated to use a single variable antibody-derived VHH domain for incorporation into a viral capsid protein for targeting the viral vector to a specific target cell type.
Regarding claims 45, 48, 56, and 61 Judd teaches a virus comprising the fusion protein [column 3 ¶ 3, column 8 ¶ 4, Figure 4-5].
Regarding claims 54-55, Judd teaches a nucleic acid comprising a nucleotide sequence encoding the fusion protein and a vector comprising the nucleic acid [column 3 ¶ 1, Figures 1, 2].
Regarding claims 57-58, Judd teaches a transduction method comprising contacting a target cell with a virus comprising the fusion protein and a nucleic acid comprising a nucleotide sequence encoding the fusion protein to introduce a nucleic acid into the target cell [Figure 2]. Judd also teaches that the r1c3 mutant comprising mCherry inserted at the position 453-459 of VP1 transduces HeLa cells with wild-type efficiency [Figure 6], which is an improvement in transduction efficiency of a target cell compared to virus produced without VP1.
Regarding claims 9, 34, and 59-60, Judd does not teach wherein the cell surface maker is a membrane protein nor wherein the membrane protein is selected from the group consisting of a multi-span homo trimer membrane protein, a type-II single span membrane protein, and a GPI-anchor membrane protein.
Kaliberov teaches a fusion protein comprising a cell surface protein specific VHH targeting human carcinoembryonic antigen (CEA), which is expressed on the membrane surface of tumor cells, fused to the C-terminus of an adenoviral capsid protein, fiber, to target adenoviral (Ad) vectors to target tumor cells (abstract, pages 893, 900, and 903, and Figure 3). Kaliberov further discloses a method for increasing transduction efficiency of a target cell to introduce a nucleic acid into the target cell comprising contacting the target cell with a virus comprising the CEA-fiber fusion protein [pages 895-901 and 903 and Figures 3-5]. Kaliberov also teaches that the genetic incorporation of targeting motifs, such as the CEA-specific VHH domain, alter tropism of vectors to achieve a cell-specific gene delivery for gene therapy applications [abstract], such as for imaging or therapeutic approaches against tumor cells [column 15 ¶ 4]. Additionally, Benchimol teaches that CEA is a cell surface glycoprotein that functions as a tumor marker [abstract and pages 327 and 330]. Hefta teaches that the human carcinoembryonic antigen (CEA), is anchored to membranes by covalent attachment to a glycosylphosphatidylinositol (GPI) moiety, and as such is a GPI-anchored membrane protein [title, abstract]. Therefore, an ordinarily skilled artisan would have been motivated to use an antibody-derived VHH domain targeting the GPI-anchored membrane protein CEA to target a viral vector to tumor cells for gene therapy applications.
Given the teachings of Judd that encoding of large protein domains in general in the GH2/3 loop may offer improved vector performance; the motivation taught by Hallek to insert an scFv into an AAV capsid protein in a flexible surface loop to target the AAV to a specific cell type for more specific and more efficient gene transfer; the motivation taught by Kaliberov to use a single variable antibody-derived VHH domain for incorporation into a viral capsid protein for targeting the viral vector to a specific target cell type; the teachings and motivation taught by Kaliberov, Benchimol, and Hefta that CEA is a GPI-anchored membrane protein and to use an antibody-derived VHH domain targeting the GPI-anchored membrane protein CEA to target a viral vector to tumor cells for gene therapy applications; it would have been prima facie obvious to an ordinarily skilled artisan at the time of filing the instant application to modify the fusion protein of Judd to replace the mCherry marker protein with a cell surface marker specific VHH, wherein the cell surface marker specific VHH is a membrane protein which is a multi-span homo trimer membrane protein (e.g., CD30) or a GPI- anchor membraned protein (e.g., hCEA) with a reasonable expectation of success.
Insofar as applicant’s arguments apply to this new grounds of rejection, Applicant argues that:
Kaliberov does not teach or suggest to genetically insert a VHH into a VP capsid protein of an AAV;
Judd informs that mCherry was selected specifically because of the proximity of its N- and C-termini; wherein success of functional insertions into AAV proteins was known to vary widely likely due to the unpredictable, context-dependent nature of protein subunit folding; such that use of a protein other than one with a compact structure with close proximity of the N- and C-termini could lead to completely different results and proteins characterized by a great distance of its N- and C-termini, such as VHH domains, would probably be unsuccessful as proper folding and supramolecular assembly are prevented due to steric hindrance;
Kaliberov teaches C-terminal fusion with an adenovirus fiber protein and does not remedy the teachings of Judd in that a skilled person would not have simply extrapolated the technical teaching of Kaliberov to arrive at the claimed subject matter;
it was unexpected that an insertion approach can be successfully applied with a VHH and an AAV capsid protein, and that it is self-evident from the teachings of the art itself that it could not have been foreseen that the VHH domain would correctly fold upon insertion into a loop of the VP protein allowing correct virus assembly and resulting in an AAV with increased cell specificity; and
Applicant intends to supplement the present response with a technical declaration to provide further evidence of unexpected results.
However, this is not agreed.
In response to Applicant’s arguments against the references individually, it is noted that the test for obviousness is not whether the features of a secondary reference may be bodily incorporated into the structure of the primary reference; nor is it that the claimed invention must be expressly suggested in any one or all of the references. Rather, the test is what the combined teachings of the references would have suggested to those of ordinary skill in the art. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981). 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). Further, the Examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007). In addition, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
Specifically, regarding Applicant’s arguments 1) and 3), note that Kaliberov was cited for teaching the motivation to use a single variable antibody-derived VHH domain for incorporation into a viral capsid protein for targeting the viral vector to a specific target cell type and not specifically for inserting the VHH into an AAV capsid protein. Note that Hallek was cited for teaching the motivation to insert an scFv (which comprises a variable heavy chain domain of a heavy chain antibody) into an AAV capsid protein within a flexible surface loop to target the AAV to a specific cell type for more specific and more efficient gene transfer.
Regarding Applicant’s argument 2), Judd identifies the proximity of N- and C-termini as one factor in selecting mCherry for their high-throughput screen to identify sites in the VP3 domain of the AAV2 capsid protein that would tolerate insertion of a large protein domain but retain the ability to form infectious capsids [pg 2 col 2 ¶ 4]. Judd further teaches inclusion of a linker sequence connecting cap and heterologous sequences may improve tolerance of difficult insertions [pg 6 col 1 ¶ 2- col 2 ¶ 1]. Judd additionally presents a molecular model of AAV2-mCherry hybrid r1c3 wherein the flanking linker sequences comprising the NgoMIV and KasI restriction sites bridge the gaps between the N- and C-termini to minimize disruption of the capsid structure [Figure 7a]. Therefore, although Judd teaches that they chose a relatively amenable insert for their initial screen, Judd does not actually teach away from using more “difficult insertions” which do not meet the criteria they used for selecting mCherry.
Note also that amended independent claim 1 as written recites a fusion protein comprising a VHH domain and an AAV capsid protein, wherein the VHH is inserted into an exposed loop of said AAV capsid protein. Therefore, the instant invention as claimed does not preclude linker sequence or any other sequences (such as other antibody domains) from also being comprised within the claimed fusion protein. Accordingly, the instantly claimed fusion protein does not require an inserted sequence wherein N- and C-termini are distant from each other. In fact, the instant disclosure only teaches a fusion protein which additionally comprises a 25 amino acid linker sequence C-terminal to the NgoMIV restriction site-comprising linker and N-terminal to the VHH insert and a 5 amino acid linker sequence at the C-terminal end of the VHH insert which is N-terminal to the KasI restriction site-comprising linker, wherein the linker sequences are schematically depicted as bridging the gap between the N- and C-termini of the inserted VHH domain to allow proper folding of the capsid protein [Figure 2]. Therefore, the broadest reasonable interpretation of independent claim 1 encompasses an insertion comprising additional amino acid sequences, such as linker sequences. Such an interpretation is consistent with the recited scope of the claim as viewed in light of the specification. Accordingly, Applicant’s argument that insertion of a VHH domain is taught away by Judd due to the relative positions of the N- and C-termini is not supported by the teachings of Judd nor the scope of the claim.
Additionally, as discussed above, Hallek was cited for specifically teaching the insertion of single-chain antibodies (scFv) into exposed loops of an AAV capsid protein, including at a position corresponding to C-terminal of amino acid 452 according to AAV2 VP1 numbers. Given that scFv comprise heavy chain variable domains, the insertion of an scFv is encompassed by the scope of the claimed invention. Additionally, Kaliberov was cited for additional motivation to specifically include a VHH domain for retargeting viral vectors for cell type-specific gene therapy.
Regarding Applicant’s argument 4), as discussed above, Judd teaches that inclusion of linker sequences can allow the insertion of more difficult sequences which do not adhere to the original selection criteria taught for the selection of mCherry in their high throughput screen. Additionally, the scope of the claim as written allows for the inclusion of additional sequences, such as linker sequences or other antibody domains, in addition to the VHH domain, which would allow for the spatial bridging between the N- and C-termini of the inserted amino acid sequence to minimize disruption of the AAV capsid structure. Additionally, as also discussed above, Hallek teaches specifically to insert scFv into exposed loops of AAV capsid proteins. As such, Judd and Hallek provide the teachings for a reasonable expectation of success in generating a fusion protein as encompassed by the instant claims.
Regarding Applicant’s argument 5), no declaration has been provided by Applicant, and as such, Applicant’s argument that a declaration is forthcoming does not overcome a finding of obviousness.
Therefore, Applicant’s arguments do not overcome a finding of obviousness over Judd, Hallek, Kaliberov, Benchimol, and Hefta under 35 U.S.C. 103.
Conclusion
No claim is allowed.
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DR. KATIE L. PENNINGTON
Examiner
Art Unit 1634
/KATIE L PENNINGTON/Examiner, Art Unit 1634
Dr. A.M.S. Wehbé
/ANNE MARIE S WEHBE/Primary Examiner, Art Unit 1634
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