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 .
Notice of Pre-AIA or AIA Status
DETAILED ACTION
Status of the Claims
Claims 3-112, 117-132, 134-135, 137-147, 149-210, 212-230, 237-240, and 242-245 are cancelled. Claims 246-247 are new. Claims 1-2, 113-116, 133, 136, 148, 211, 231-236, 241 and 246-247 are pending. Claims 113 and 234-236 and 241 are withdrawn. Claims 1-2, 114-116, 133, 136, 148, 211, 231-233 and 246-247 are under examination.
Priority
This application is a national stage entry of PCT/EP2022/059940 filed on 4/13/2022, which claims priority from US provisional application 63/174,874 filed on 4/14/2021.
Information Disclosure Statement
The information disclosure statement filed on 04/13/2026 has been considered by the examiner.
Objections and Rejections Withdrawn
The specification objections are withdrawn as applicant has amended the specification accordingly for the trademarked items.
The objection over claims 1-2, 114, 120, 122, 148 and 211 are withdrawn per applicant’s amendments or cancellations to the claims.
The objection over claim 116 is withdrawn per applicant’s amendment to the claim.
The objection over claims 128, 133 and 148 is withdrawn per applicant’s cancellation or amendments to the claims.
The objection over claim 148 for SAM is withdrawn per applicant’s amendment to the claim.
The objection over claim 148 for JM and KD is withdrawn per applicant’s amendments to the claim.
The rejection under USC 101 is withdrawn per applicant’s amendments to claim 114 and all claims that include the limitation of claim 114, particularly to include a targeting domain with a synthetic binding protein.
The rejections under USC 112(b) over claim 116 for trademarks and for broad and narrow recitations are withdrawn per applicant’s amendments and arguments.
The former rejection under USC 112(b) over claim 211is withdrawn per applicant’s amendment, however, the amendment has brought up a new issue.
The rejection under USC 102 over Freywald is withdrawn per applicant’s amendments and arguments.
The rejection under USC 103 over Freywald and Pasquale is withdrawn per applicant’s amendments and arguments. Namely, applicant amended the claim to provide that the targeting domain comprises a synthetic binding protein. However, note below that there was a rejection further including Wiklander that taught the limitation of claim 116.
The rejection under USC 103 over Freywald, Pasquale and Sato is withdrawn per applicant’s amendments and arguments.
As these rejections have been withdrawn, applicant’s arguments toward these rejections are now moot.
Maintained Rejection – Modified As Necessitated by New Claims
Claim Rejections - 35 USC § 112(a)
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 1-2, 114-116, 133, 136, 148, 211, 231-233 and 246-247 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. Claims 1, 2, 114, 120, 122 and 148 as well as their dependent claims include a polypeptide comprising in the N-terminus to C-terminus direction, an ephrin receptor cysteine-rich (CR) domain, a first and a second ephrin receptor fibronectin type III domain and a transmembrane domain with claims also adding items like cargo protein or cargo binding domain at the C-terminal portion, and targeting domain at the N-terminal portion. In addition, other linker domains or SBD domains may be present. Targeting domains that only have to be N-terminal compared to the CR domain are provided broadly as various types of antibodies, antibody fragments or peptides/polypeptides capable of binding antigens, but does not provide sequences for such items where this would determine a binding functionality of the polypeptide. As the polypeptide comprises such domains with only order being dictated, it allows for variable amounts and types of other sequence to be present between domains or at the N-terminal and C-terminal ends of the polypeptide. Each of these new sequences allowed by the claims even if containing domains listed will represent a new polypeptide with new possible functionality, which allows the claims to encompass many varying polypeptides having numerous functionalities or even no functionality. It is noted that example 1 (section 7.1) of applicant’s specification provides for a polypeptide that is monobody-linker1-modified monomeric Fc-linker2-EphB2 scaffold-linker3-turboluc with EphB2 scaffold comprised residues 195-905 of EphB2, lacking a LBD, and containing the following amino acid substitutions L356A, I395A, S536E, A562S, Y822F relative to SEQID NO:222. Paragraph 483 provides for another polypeptide that is anti-EphA2 scFv-linker-EphB4 fragment as detailed in paragraph 483 with lacking LBD and amino acid substitutions which is then linked to the endodomain of EphA2 as provided therein. These versions of polypeptides have particular types of targeting domains at the N-terminus directly attached to a linker that is directly attached to an Ephrin receptor that has been modified in a particular way in the examples (these also start with a given domain and then end with a given domain, where applicant’s claims would allow the N-terminus and C-terminus to extend with other sequence). Thus, there are a limited amount of specialized domain sequences with linkers described in the polypeptides that are exemplified by applicants in their disclosure, which have the purpose of targeting exosomes or hybridosomes to a target area. However, the applicant does not have written description for all the possible polypeptides of various sequences and sizes the claims would allow due to “comprising” and with the domains, which although ordered from N-terminus to C-terminus, could be spaced apart with various sequences of different lengths including other functional sequences in between. That is, the polypeptide represents a vast genus of possible polypeptides of which applicant only describes and shows ownership for a limited few being made in examples with particular domains and structure. This creates the same issue for the polynucleotide that is supposed to encode the polypeptide. Applicant should consider amending the claims to be more in scope with described examples of polypeptides provided by applicant with limiting the polypeptide with “consisting of” or starting with what particular domain is at the N-terminal end of the polypeptide and laying out each domain directly connected to each next portion finishing with a definite domain or sequence at the C-terminal end.
Response to Applicant’s Arguments to the Previous Rejection under USC 112(a)
Applicant argues they have written support for limitations as laid out in claim 114 (i.e. items like the listed domains/items in N-terminus to C-terminus order, the genus of cargo protein and cargo protein binding domain and the genus of targeting domains comprising a synthetic binding protein). The examiner thanks applicant for pointing out description of certain domains, but the rejection was not fully regarding the domains, but also that the use of “comprising” even with the domains being in a particular order does not exclude the presence of additional sequences of varying structures and functions from occurring between or on the outer portions of the polypeptide (and the related nucleic acid for claim 231. It was previously noted in the rejection that “However, the applicant does not have written description for all the possible polypeptides of various sequences and sizes the claims would allow due to “comprising” and with the domains, which although ordered from N-terminus to C-terminus, could be spaced apart with various sequences of different lengths including other functional sequences in between. That is, the polypeptide represents a vast genus of possible polypeptides of which applicant only describes and shows ownership for a limited few being made in examples with particular domains and structure. This creates the same issue for the polynucleotide that is supposed to encode the polypeptide.” This allows the claim to contain many more polypeptides or nucleic acids than are actually provided by applicant’s disclosure. Note a similar scenario in MPEP 2163 II 3(a) ii – “The claimed invention as a whole may not be adequately described if the claims require an essential or critical feature which is not adequately described in the specification and which is not conventional or known in the art. Consider the claim “A gene comprising SEQ ID NO:1.” The claim may be construed to include specific structures in addition to SEQ ID NO:1, such as a promoter, a coding region, or other elements. Although SEQ ID NO:1 is fully disclosed, there may be insufficient description of other structures embraced by the claim (e.g., promoters, enhancers, coding regions, and other regulatory elements).” In the case of a polypeptide, additional external and internal sequences could include other additional protein functional or non-functional groups of varying purpose (e.g. enzymatic, various binding domains, etc). Thus, the claim allows for many more unique proteins than applicant has support for. For this reason, the written description rejection is maintained.
In regards to correcting the issue, Applicant may consider language to notate that each domain (a), (b), (c), (d), and (e) is linked directly to one another in some manner as supported by applicant’s specification (whether direct bond or through a linking group/linker) while also indicating what the N-terminal and C-terminal domain/groups are. Note that in the N-terminus to C-terminus direction only provides directionality but does not indicate that “(a) the targeting domain…” has to be the N-terminal component and “(e) the cargo protein or cargo protein binding domain” has to be the C-terminal component. Applicant would amend any dependent claims as necessitated by any amendments to the independent claim.
New Matter – New Rejection As Necessitated by Amendments
Claim 115 is 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. Applicant includes “antibody mimetic” in the group where there is no “antibody mimetic” or language that suggests the genus of “antibody mimetics” in applicant’s specification. “Antibody mimetic” would provide a genus of molecules that have the ability to act like an antibody, but are not antibodies themselves. This could encompass a number of possible molecules of differing structures and binding abilities. There are not a sufficient number of species to provide possession of this genus. If applicant has species that are antibody mimetics, applicant may use these items in the group instead of the use of “antibody mimetics”.
Since claim 116 limits the targeting domain (the portion which includes the synthetic binding protein) to the Markush group listed and the items in that group have written support, claim 116 is corrective for this new matter issue.
New Rejections – As Necessitated by Amendments to the Claims and New Claim 247
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 116, 211, 233 and 247 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 116 is indefinite as claims 114 and 115 after amendment to have the targeting domain comprising a synthetic binding protein where claim 116 provides CDR as one item to select for the entire targeting domain (i.e. the targeting domain). However, it takes multiple CDRs (usually 6) to bind an antigen. Similarly Fd fragments depend on being paired with light chain for binding. As IgGACH2 would refer to the CH2 domain of an IgG, then this one domain would also need other parts of the IgG to function for binding. Thus, it is unclear if the group in claim 116 provides for items that would be targeting domains that comprise synthetic binding domains (capable of being able to bind proteins/antigens) as some of these fragments like CDR or Fd fragments are incapable of doing this with only one or on their own. Applicant might amend the group to delete Fd fragments, CDR and IgGACH2 in favor of all the other items in the group that are capable of binding as provided. Applicant may further include IgG, IgM, IgA and IgE into the group as supported by the specification (paragraphs 597-603 of applicant specification) since these are capable of protein binding.
Claim 211 is indefinite for the recitation of “the polypeptide further comprises a synthetic binding protein” as claim 114, on which it depends, also has “a synthetic binding protein” in its polypeptide after amendment to the claims. Although it uses “further”, it is unclear whether this has to be an additional synthetic binding protein to that presented in claim 114 or if the limitation can be met by a prior art teaching of the synthetic binding protein needed for claim 114.
Claim 233 recites the limitation "the nucleic acid of claim 114" in the claim where claim 114 provides a polypeptide and not a nucleic acid. There is insufficient antecedent basis for this limitation in the claim. It is noted that applicant had changed the dependency by amendment and may consider changing it to the claim where “A nucleic acid” was introduced.
Claim 247 recites the limitation “the first linker comprises an amino acid sequence of GGGS”, where the use of “an amino acid sequence of GGGS” could allow for fragments of GGGS such as “GG” or GS” or others. Thus, it becomes unclear if applicant intends the full sequence of GGGS or would allow for the full sequence or a fragment thereof. If applicant intends the full sequence to be included then applicant may use the language “first linker comprises the amino acid sequence of GGGS”.
Claim Rejections - 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 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.
Maintained Rejection over Previously Cited Art – Modified As Necessitated by Applicant’s Amendments
Claims 1, 114-116, 133, 136, 148, 211, 231-233 and 246 is rejected under 35 U.S.C. 103 as being unpatentable over Freywald et al (JBC, 2002, volume 277, pages 3823-3828), Pasquale (JCB, 2016, volume 214, pages 5-7) and Wiklander US20200109183A1 as evidenced by Arora (cited previously) and as evidenced by Seiradake et al (Nat Struct Mol Biol, 2013, volume 20, pages 1-19).
In regards to “genetically engineered” this is a product by process limitation (MPEP 2113), if the prior art may arrive a such a genetically engineered polypeptide and it having a lack of ephrin binding and/or kinase activity in combined teachings of references, it will meet the limitation of the claims.
Applicant’s claimed invention depends mainly on polypeptide with a transmembrane domain and a portion of an N-terminal extracellular domain with ephrin receptor domains where a targeting domain can be attached to (made to be part of the polypeptide). Other claims of applicant also allow for intracellular domains to be present.
The limitation of “comprising in an N-terminus to C-terminus direction”, means that although the items following this will be present in this order, there can be sequence that can occur in before or after and in between these domains/sequences.
The limitation of a “cargo protein or cargo binding domain” as being a polypeptide domain that is either linked to the polypeptide structure that can be a protein/polypeptide itself or one that is capable of binding other proteins or “cargo”. The limitation does not present for a structure that the cargo must have besides being a protein or binding domain.
The limitation of “linker” is read as a sequence or other compound capable of linking one item to the next. Amino acid sequence or functional groups/bonds between domains can be construed as linking them together.
The limitation of “targeting domain” will be read as a domain capable of binding/targeting to an organ, cell or tissue in the body. This would include binding of a cell bound ligand such as an ephrin (ephrins are attached to cells). The specification does not limit targeting domain to only antibodies or antibody fragments. Paragraph 401 provides this regarding “targeting domain” – “a targeting domain that is capable of targeting the nanovesicle (e.g., EV or hybridosome) to a specific organ, tissue, or cell type).”
Claims 133 and 136 are toward characteristics between the cargo binding domain and the cargo protein. Where the prior art teaches a protein domain capable of binding other proteins or SBD (scaffold binding domain) of another protein, if the prior art teaches protein domains that act to bind other proteins, directly or indirectly, they will be seen as being capable of control by pH or ionic strength as they are protein/protein interactions. Note also that the claim is not toward a method of using for such protein binding and is read for the characteristics/structure of the claimed polypeptide itself.
Freywald teaches kinase null EphB6 receptor (title and abstract). Freywald teaches subcloning EphB6 into an expression vector that is transfected into cells (Experimental Procedures and Results). Freywald provides that EphB6 binds c-Cbl (figure 6). Freywald provides that the structure of EphB6 is typical of other Ephrin receptors (Discussion). Arora evidences that Eph receptors have ligand binding domain, cysteine abundant region, two FN III domains, a transmembrane domain, a juxtamembrane region, a SAM domain and a PDZ binding motif (figure 1 of Arora, Arora indicates EphB6 in section 5.2 and table 1 and section 6). Arora evidences that “EphB6 and EphA10 share the same general architecture as the rest of the Eph RTK family members but are catalytically dysfunctional because of alterations in key residues
that are essential for their tyrosine kinase activities” (section 6 of Arora). Thus, Arora evidences the protein structure that EphB6 had at the time of Freywald. Sequences found between domains in the protein would be construed as amino acid sequences linking the domains together, and thus, be linkers.
Freywald and Pasquale teach the claims as discussed above. Pasquale teaches “Exosomes show promise as cell-derived vehicles for delivery of therapeutic agents (György et al., 2015) and Gong et al. (2016) demonstrate preferential binding of EphB2-positive exosomes to cells expressing ephrinB1, followed by exosome internalization. Thus, it may be possible to take advantage of the Eph system for targeted delivery of therapeutic exosomes to cancer cells or other diseased cells overexpressing Eph receptors/ephrins as well as for promoting exosome uptake by recipient cells” (page 7 of Pasquale).
Freywald and Pasquale does not teach attaching an antibody, antibody fragment or targeting peptide/polypeptide to the Eph receptors on exosomes.
Pasquale teaches exosomes expand the sphere of influence of Eph receptors and ephrins (title and abstract). Pasquale teaches that Ephrin receptors can be deployed by cells on exosomes to activate ephrinB signaling (abstract). Pasquale teaches “Exosomes show promise as cell-derived vehicles for delivery of therapeutic agents (György et al., 2015) and Gong et al. (2016) demonstrate preferential binding of EphB2-positive exosomes to cells expressing ephrinB1, followed by exosome internalization. Thus, it may be possible to take advantage of the Eph system for targeted delivery of therapeutic exosomes to cancer cells or other diseased cells overexpressing Eph receptors/ephrins as well as for promoting exosome uptake by recipient cells” (page 7 of Pasquale). Thus, it was recognized by Pasquale as possible to use ephrin receptors on exosomes for the purpose of drug delivery.
Wiklander teaches extracellular vesicle (EV) therapeutics, wherein the EVs are coated with proteins containing Fc domains (such as antibodies) for i.e. targeting and therapeutic applications (abstract and figure 1). Figure 1 of Wiklander provides an Fc binder domain attached/linked to an exosomal transmembrane protein in the lipid bilayer of an exosome (also paragraphs 10-11 and 14). Wiklander teaches “Such therapeutic protein and/or peptide agents may be selected from a group of non-limiting examples including: antibodies, intrabodies, single chain variable fragments (scFv), affibodies, bi- and multispecific antibodies or binders, affibodies, darpins, receptors…” (paragraph 28). Wiklander teaches Fc domain containing receptors or ligands (paragraph 31). Items within these groups can be synthetic. Wiklander’s figure 1 shows the Fc binder domain attached to the extraexosomal end of the protein, which for ephrin receptors will be the N-terminal portion placed before the cysteine rich domain. Wiklander mentions any C and/or N terminal direction with the fusion proteins (paragraphs 39-42). Wiklander provides for linkers in its teachings (paragraph 34).
One of ordinary skill in the art before the time of filing would have produced ephrin receptor exosomes as motivated by Freywald and Pasquale and further modified the Ephrin receptors as being an available transmembrane receptor with Fc domains for improved targeting of therapeutic exosomes in the body by teachings of Wiklander. Thus, there was a reasonable expectation of success in combining the teachings of the references to produce ephrin receptors conjugated/attached to Fc domains for better targeting of exosomes they are bound to in order to reach new targets in the body, where exosomes are recognized for use to carry drugs for targeted delivery.
It was obvious to one of ordinary skill in the art before the time of filing that ephrin receptors like EphB6 would be able to be carried in exosomes for signaling by the combined teachings of the references with Freywald teaching an Eph receptor that meets the limitation of the claims and Pasquale teaching the presence of expressed Eph receptors in exosomes from cells. Pasquale also recognizes a use of exosomes with Ephrin receptors for targeted delivery of therapeutic exosomes to cancer or other diseased cells making Ephrin receptors a reasonable choice for such targeted exosomes. Thus, there was a reasonable expectation of success in combining the teachings of the references and obtaining exosomes with Eprhin receptors including those like EphB6 (a recognized Ephrin receptor).
New Rejection – As Necessitated by Applicant’s Amendments, Only Previously Cited Art
Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over Freywald et al (JBC, 2002, volume 277, pages 3823-3828), Pasquale (JCB, 2016, volume 214, pages 5-7), Wiklander US20200109183A1 and Sato et al (Scientific Reports, 2016, DOI: 10.1038/srep21933, pages 1-11) as evidenced by Arora (cited previously) and as evidenced by Seiradake et al (Nat Struct Mol Biol, 2013, volume 20, pages 1-19).
Freywald, Pasquale and Wiklander teach the claims as discussed above. Pasquale teaches “Exosomes show promise as cell-derived vehicles for delivery of therapeutic agents (György et al., 2015) and Gong et al. (2016) demonstrate preferential binding of EphB2-positive exosomes to cells expressing ephrinB1, followed by exosome internalization. Thus, it may be possible to take advantage of the Eph system for targeted delivery of therapeutic exosomes to cancer cells or other diseased cells overexpressing Eph receptors/ephrins as well as for promoting exosome uptake by recipient cells” (page 7 of Pasquale).
Freywald, Pasquale, and Wiklander do not teach hybridosomes (a modified form of exosome).
Sato also recognizes the use of exosomes as biomaterials for use as nanocarriers for drug delivery systems (abstract and figure 1). Sato teaches hybrid exosomes made by fusing them with liposomes (abstract). Sato recognizes these methods of producing hybrid exosomes (hybridosomes) is strategy for rationally designing exosomes as nanocarriers for drug delivery systems (abstract and Discussion).
One of ordinary skill in the art before the time of filing would be able to form hybrid exosomes from exosomes including those with Ephrin receptors, which also are recognized as useful for delivery of therapeutic agents, in order to be used for drug delivery systems by the combined teachings of the references. Thus, there was a reasonable expectation of success in combining the teachings of the references to obtain hybrid exosomes (membrane engineered exosomes) that have Eprhin receptors for drug (therapeutic) delivery systems.
Response to Applicant’s Arguments over the Rejections Under USC 103
It is noted that both the rejections under US 103 over Freywald and Pasquale and over Freywald, Pasquale and Sato have been withdrawn as they do not provide for the targeting domain comprising a synthetic binding protein.
Applicant argues in regards to claim 116, Wiklander is silent to making the polypeptide as claimed. The rejection is over Freywald, Pasquale and Wiklander and the combination of these references is what teaches the claimed invention. Applicant does not argue the rejection in terms of this combination. In regards to Wiklander it was pointed out that “Figure 1 of Wiklander provides an Fc binder domain attached/linked to an exosomal transmembrane protein in the lipid bilayer of an exosome (also paragraphs 10-11 and 14). Wiklander teaches “Such therapeutic protein and/or peptide agents may be selected from a group of non-limiting examples including: antibodies, intrabodies, single chain variable fragments (scFv), affibodies, bi- and multispecific antibodies or binders, affibodies, darpins, receptors…” (paragraph 28).” Freywald provides for an ephrin receptor which is a transmembrane protein and Pasquale provides for the advantage of the Eph system for targeted delivery of therapeutic exosomes to cancer cells or other diseased cells overexpressing Eph receptors/ephrins as well as for promoting exosome uptake by recipient cells” (page 7 of Pasquale).” Thus, there are motivations to engineer transmembrane proteins including ephrin receptors which exist as transmembrane proteins on exosomes linked to polypeptide agents such as antibodies, scFv and others on their extra-exosomal region. This would be seen as useful for targeting for therapeutic delivery from teachings of the prior art. Therefore, recombination of the previously cited prior art as necessitated by applicant’s amendment still provides for applicant’s claimed invention with a reasonable expectation of success.
In regards to claim 247, the limitation of “the second linker comprises the amino acid sequence of GGGS” where the second linker is between the TM domain and the cargo protein binding domain (via dependence on claim 246) is not motivated by the prior art as a GGGS sequence, which is more typical of synthetic linkers, does not exist in this portion between domains in the ephrin receptor of Freywald and is not motivated in such a position. However, the applicant would have to overcome the rejections under USC 112(a) and USC 112(b) in addition to inserting this limitation found in claims 247 and 246 into independent claim 114.
Conclusion
No claims are currently 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.
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/MARK V STEVENS/Primary Examiner, Art Unit 1613
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