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 .
DETAILED ACTION
Continued Examination Under 37 CFR 1.114
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. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 09/18/2025 has been entered.
Disposition of Claims
Claims 1-2, 5, 7, 12, 15, 21, 23-25, 46, 48, 50-52, 68-69, 88-95, 97, 99, and 101-105 were pending. Claims 3-4, 6, 8-11, 13-14, 16-20, 22, 26-45, 47, 49, 53-67, 69-87, 96, 98, and 100-105 are cancelled. Amendments to claims 1-2, 12, 50, 97, and 99 are acknowledged and entered. New claims 106-111 are acknowledged and entered. Claims 1-2, 5, 7, 12, 15, 21, 23-25, 46, 48, 50-52, 68, 88-95, 97, 99, and 106-111 will be examined on their merits.
Examiner’s Note
All paragraph numbers (¶) throughout this office action, unless otherwise noted, are from the US PGPub of this application US2020/0164008A1, Published 05/28/2020.
Applicant is encouraged to utilize the new web-based Automated Interview Request (AIR) tool for submitting interview requests; more information can be found at https://www.uspto.gov/patent/laws-and-regulations/interview-practice.
Response to Arguments
Applicant's arguments filed 09/18/2025 regarding the previous Office action dated 03/19/2025 have been fully considered. If they have been found to be persuasive, the objection/rejection has been withdrawn below. Likewise, if a rejection/objection has not been recited, said rejection/objection has been withdrawn. If the arguments have not been found to be persuasive, or if there are arguments presented over art that has been utilized in withdrawn rejections but utilized in new rejections, the arguments will be addressed fully with the objection/rejection below.
Claim Rejections - 35 USC § 112(b); Second Paragraph
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
(Rejection maintained.) Claims 97 and 99 remain 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 97 provides for the limitation of “wherein the AAV binding antibody affinity matrix comprises said empty capsid, and said empty capsid comprises the amino acid sequence of SEQ ID NO:1.” However, if the capsid is empty (one reasonable interpretation is that a “capsid” is a nanoparticle that does not comprise anything inside of it), it is unclear how said capsid comprises an amino acid sequence. It appears as though applicant is attempting to claim that the proteins which make up the capsid comprise a sequence of SEQ ID NO: 1, so the claim should be amended accordingly to clarify where exactly the sequence is found within the empty capsid. Claim 99 is rejected for similar reasoning.
One suggestion to clarify the metes and bounds of the claim is to amend the claims along the lines of the following:
“97. The method of claim 1, wherein the rAAV binding antibody affinity matrix comprises said empty capsid, and at least one structural protein of said empty capsid comprises the amino acid sequence of SEQ ID NO: 1.”
For at least these reasons, claims 97 and 99 remain rejected on the grounds of being indefinite.
Response to Arguments
No arguments/remarks were presented in the 09/18/2025 response with respect to this rejection. Applicant should submit an argument under the heading “Remarks” pointing out disagreements with the examiner’s contentions. Applicant must also discuss the references applied against the claims, explaining how the claims avoid the references or distinguish from them.
(Rejection withdrawn.) The rejection of Claims 103 and 105 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, is withdrawn in light of the cancellation of said claims.
(Rejection withdrawn.) The rejection of Claim 105 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, is withdrawn in light of the cancellation of said claim.
(New rejection.) Claims 1 and 2 and dependent claims 5, 7, 12, 15, 21, 23-25, 46, 48, 50-52, 68, 88-95, 97, 99, and 106-111 thereof 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.
Claims 1 and 2 have been amended to recite limitations wherein “said pre-apheresis blood product has an AAV antibody titer of up to 1:1000…” and further limitations regarding the “AAV antibody titer”. However, in the claims, the pre-apheresis blood product is subjected to an apheresis method wherein the affinity matrix comprises VP1, VP2, VP3, or empty capsids which correspond to the capsid proteins in the rAAV, and the claim recites that the post-apheresis blood therefore comprises “a reduced amount of antibodies binding said rAAV vector compared to said pre-apheresis blood product.” As the claim recites a specific type of anti-AAV antibody earlier in the claim, namely anti-rAAV antibodies, the antecedent basis of the “AAV antibody titer” recited later in the claims is unclear, because it is not clear if said “AAV antibody titer” is determining antibody titers against all known AAV subtypes (e.g. AAV-1, AAV-2, AAV-8, etc.), a subtype of anti-AAV antibodies that are known to bind to the capsid found in the rAAV (e.g. certain AAV serotypes have limited cross-reactivity with antibody binding), or only antibodies against the specific serotype(s) of capsid found in the rAAV. This also makes the antecedent basis for “AAV binding antibody affinity matrix” and “rAAV vector binding antibodies” recited throughout the dependent claims unclear (see e.g. claims 5, 7, etc.) because it is unclear if the “AAV binding antibody affinity matrix” is referring to a different AAV antibody matrix, or a matrix that only comprises rAAV binding antibodies.
Since a skilled artisan would not be reasonably apprised as to the metes and bounds of the claimed invention, instant claims 1-2 are rejected on the grounds of being indefinite. Claims 5, 7, 12, 15, 21, 23-25, 46, 48, 50-52, 68, 88-95, 97, 99, and 106-111 are also rejected since they depend from claim 1 and/or 2, but do not remedy these deficiencies of claim 1 and/or 2.
Claim Interpretation
The claims in this application are given their broadest reasonable interpretation using the plain meaning of the claim language in light of the specification as it would be understood by one of ordinary skill in the art.
Claim 1 is drawn to a method of administering a recombinant adeno-associated viral (rAAV) vector to a human, wherein said rAAV vector comprises:
(A) a capsid, and
(B) a rAAV recombinant nucleic acid comprising a heterologous polynucleotide that either (i) encodes for a first protein: or (ii) transcribes a nucleic acid that inhibits, decreases or reduces expression of a second protein,
said method comprising:
(a) removing a pre-apheresis blood product from said human,
(b) passing said pre-apheresis blood product through a sterile AAV binding antibody affinity matrix comprising a VP1 of said capsid, a VP2 of said capsid, a VP3 of said capsid, or an empty capsid comprising said capsid in the absence of said heterologous polynucleotide, to produce a post-apheresis blood product comprising a reduced amount of antibodies binding said rAAV vector compared to said pre-apheresis blood product;
(c) infusing said post-apheresis blood product to said human; and
(d) administering said rAAV vector to said human, wherein either:
(i) said pre-apheresis blood product has an AAV antibody titer of up to 1:1000 and said step (d) administering is up to 1 hour after said step (c):
(ii) said pre-apheresis blood product has an AAV antibody titer of up to 1:300 and said step (d) administering is up to 3 hour after said step (c); or
(iii) said pre-apheresis blood product has an AAV antibody titer of up to 1:100 and said step (d) administering is up to 12 hours after said step (c); and
(iv) said pre-apheresis blood product has an AAV antibody titer of up to 1:30 and said step (d) administering is up to 24 hours after said step (c).
Claim 2 is drawn to a method of administering a recombinant adeno-associated viral (rAAV) vector to a human, wherein said rAAV vector comprises:
(A) a capsid, and
(B) a rAAV recombinant nucleic acid comprising a heterologous polynucleotide that either
(i) encodes for a first protein; or
(ii) transcribes a nucleic acid that inhibits, decreases or reduces expression of a second protein,
said method comprising:
(a) removing a pre-apheresis blood product from said human,
(b) passing said pre-apheresis blood product through a sterile AAV binding antibody affinity matrix comprising a VP1 of said capsid, a VP2 of said capsid, a VP3 of said capsid, or an empty capsid comprising said capsid in the absence of said heterologous polynucleotide, to produce a post-apheresis blood product comprising a reduced amount of antibodies binding said rAAV vector compared to said pre-apheresis blood product
(c) infusing said post-apheresis blood product to said human and
(d) administering said rAAV vector to said human,
wherein either:(i) said pre-apheresis blood product has an AAV antibody titer of about 1:1000 and said step (d) administering is about 1 hour after said step (c):(ii) said pre-apheresis blood product has an AAV antibody titer of about 1:300 and said step (d) administering is about 3 hour after said step (c);(iii) said pre-apheresis blood product has an AAV antibody titer of about 1:100 and said step (d) administering is about 12 hours after said step (c); or (iv) said pre-apheresis blood product has an AAV antibody titer of about 1:30 and said step (d) administering is about 24 hours after said step (c).
Further limitations on the method of claim 1 and/or 2 are wherein the AAV binding antibody affinity matrix is disposed within a column, apparatus, chamber, device, filter, cartridge, tube having an inlet and an outlet for extracorporeal or intracorporeal removal or depletion of rAAV vector binding antibodies from the pre-apheresis blood product upon contact with the AAV binding antibody affinity matrix (claim 5), wherein the AAV binding antibody affinity matrix comprises an AAV VP1, VP2 and/or VP3 capsid protein (claim 7); wherein the AAV binding antibody affinity matrix comprises at least one AAV VP1, VP2, or VP3 capsid protein serotype selected from the group consisting of AAV1, AAV2, AAV3, AAV4, AAV5, AAV6, AAV7, AAV8, AAV9, AAV10, Rh10, and Rh74 (claim 12); wherein the AAV binding antibody affinity matrix comprises said empty capsid, and said empty capsid is either an AAV1, AAV2, AAV3, AAV4, AAV5, AAV6, AAV7, AAV8, AAV9, AAV10, Rh10, or Rh74 capsid (claim 15); wherein the substrate and/or column, apparatus, chamber, device, filter, cartridge, or tube is configured from plastic or glass (claim 21); wherein the rAAV binding antibodies present in the pre-apheresis blood product, as measured by neutralization assay, are more than about 1:100, where 1 part of the pre-apheresis blood product diluted in 100 parts of isotonic buffer results in 50% AAV neutralization (claim 23); wherein the rAAV binding antibodies present in the pre-apheresis blood product, as measured by neutralization assay, are more than about 1:1000, where 1 part of the pre-apheresis blood product diluted in 1000 parts of isotonic buffer results in 50% AAV neutralization (claim 24); wherein 20% or more of the rAAV vector binding antibodies present in the pre-apheresis blood product are removed (claim 25); further comprising analyzing a sample from the subject taken after step (c) for the amount of rAAV vector binding antibodies present in the sample (claim 46), wherein the blood product is plasma (claim 48); wherein the human has a disease is caused by lost or reduced expression of a gene that encodes the first protein and the heterologous nucleic acid encodes said first protein (claim 50); wherein the disease is a blood clotting disorder (claim 51); wherein the disease is hemophilia A, hemophilia A with inhibitory antibodies, hemophilia B, a deficiency in any coagulation Factor: VII, VIII, IX and X, XI, V, XII, II, von Willebrand factor, or a combined FV/FVIII deficiency, or thalassemia, vitamin K epoxide reductase C1 deficiency or gamma-carboxylase deficiency (claim 52); and wherein step (a) and/or step (c) are performed two or more times (claim 68); and wherein the subject is a human (claim 69), wherein the disease is cystic fibrosis (claim 88); wherein disease is a bleeding disorder that is either hemophilia A with or without inhibitors or hemophilia B with or without inhibitors (claim 89); wherein the disease is anemia (claim 90); wherein the disease is Wilson's or Menkes disease (claim 91); wherein the disease is a glycogen storage disease (claim 92), wherein the glycogen storage disease is Pompe disease (claim 93); wherein the disease is an RPE65 deficiency or choroideremia (claim 94); wherein the disease is a solid organ disease that affects brain, liver, kidney or heart (claim 95); wherein the rAAV binding antibody affinity matrix comprises said empty capsid, and at least one structural protein of said empty capsid comprises the amino acid sequence of SEQ ID NO: 1 (claim 97) or of SEQ ID NO: 2 (claim 99); wherein said pre-apheresis blood product has an AAV antibody AAV antibody titer of up to 1:1000 and said step (d) administering is up to 1 hour after said step (c)(claim 106); wherein said pre-apheresis blood product has an AAV antibody titer of up to 1:300 and said step (d) administering is up to 3 hour after said step (c)(claim 107); wherein said pre-apheresis blood product has an AAV antibody AAV antibody titer of up to 1:100 and said step (d) administering is up to 12 hours after said step (c) (claim 108); wherein said pre-apheresis blood product has an AAV antibody AAV antibody titer of up to 1:30 and said step (d) administering is up to 24 hours after said step (c)(claim 109); wherein said pre-apheresis blood product has an AAV antibody AAV antibody titer of about 1:1000 and said step (d) administering is 1 hour after said step (c)(claim 110); and wherein said pre-apheresis blood product has an AAV antibody titer of about 1:300 and said step (d) administering is 3 hour after said step (c)(claim 111).
Claim Rejections - 35 USC § 102
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
(Rejection withdrawn.) The rejection of Claims 1-2, 5, 7, 12, 15, 21, 23-25, 46, 48, 50-52, 68-69, 88-95, and 101-105 under 35 U.S.C. 102(a)(2) as being anticipated by Ferreira (US20180169273A1, Pub. 06/21/2018, Priority 12/16/2016; CITED ART OF RECORD; hereafter “Ferreira”) is withdrawn in light of the amendments to the claims.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
(Rejection withdrawn.) The rejection of Claims 97 and 99 under 35 U.S.C. 103 as being unpatentable over Ferreira as applied to claims 1-2, 5, 7, 12, 15, 21, 23-25, 46, 48, 50-52, 68-69, 88-95, and 101-105 above, and further in view of High et. al. (US20190192693A1, Priority 09/02/2016; hereafter “High”) is withdrawn in light of the amendments to the claims.
(New rejection.) Claims 1-2, 5, 7, 12, 15, 21, 23-25, 46, 48, 50-52, 68, 88-95, and 106-111 are rejected under 35 U.S.C. 103 as being unpatentable over Ferreira (US20180169273A1, Pub. 06/21/2018, Priority 12/16/2016; CITED ART OF RECORD; hereafter “Ferreira”), and further in view of Nilsson (US20140284274A1; Pub. 09/25/2014; hereafter “Nilsson”.)
The Prior Art
Ferreira teaches the depletion of AAV-specific immunoglobulins from the blood (plasma) and subsequent treatment with rAAV vectors (entire document; see abstract.) Ferreira teaches a method of administering a recombinant adeno-associated virus (rAAV) to a subject, such as a human (¶[0037]), comprising depleting a subject's circulating immunoglobulins using immunoadsorption and subsequently administering a rAAV to the subject (reference claim 1) wherein the method utilizes a binding moiety attached to a matrix (¶[0051-0053]) wherein the binding moiety may be AAV epitopes, AAV proteins such as VP1, VP2, or VP3, or AAV empty capsids known to bind to anti-AAV antibodies (¶[0054], instant claim 7). Ferreira teaches the chromatography resin may be one that is commercially available that has AAV capsids from serotypes 1, 2, 3, or 5 (¶[0054]; instant claims 5, 12, 15). Ferreira teaches these columns would be useful in methods where recombinant AAV (rAAV) comprises a therapeutic gene and is used for gene therapy in humans, wherein the gene therapy is to repair a gene defect by replacing or correcting deficiency, to treat an epigenetic disorder or disease, or to treat a condition associated with dysregulation of a gene product (¶[0003][0077]; instant claim 50). Said gene therapy methods can treat cystic fibrosis, hypercholesterolemia, Duchenne muscular dystrophy, hemophilia A or B, or the like, and would preferably encode such genes as factor IX, factor VIII, LPL, or AGXT (¶[0077]; instant claims 50-52, 88-89). Ferreira teaches further diseases in which this method could be used, such as cystic fibrosis (¶[0077]; instant claim 88), anemia (¶[0078]; instant claim 90); glycogen storage diseases such as Pompe disease (¶[0078]; instant claims 92-93), retinal degenerative diseases such as RPE65 deficiency or choroideremia (¶[0078; instant claim 94), copper or iron accumulation disorders such as Wilson’s or Menkes disease (¶[0078]; instant claim 91); and congestive heart failure (¶[0078]; instant claim 95). Ferreira teaches the blood may be treated to one or more cycles of processing within the columns (¶[0085]; instant claim 68). Ferreira teaches the reduction of anti-AAV antibodies may be at least four fold up to at least 1000-fold, but may be even larger, and the levels of antibodies are measured in blood serum or plasma before and after apheresis (¶[0046]; Fig. 2; instant claims 23-25, 46, 48). Ferreira teaches the use of known commercial apheresis units, such as LIFE 18™ Apheresis unit, which, absent evidence to the contrary, is made from plastic, has parts which are glass or plastic, and utilizes plastic, glass, or other clinically relevant consumables in the unit (¶[0052]; instant claim 21). Ferreira teaches performing the apheresis no more than 24 hours prior to the administration of a booster of the rAAV5 vaccine (¶[0089]).
While Ferreira teaches the majority of the instantly claimed invention, Ferreira fails to teach an association between the timing when the rAAV vector is administered and the pre-apheresis blood product antibody titer. However, altering such a parameter in the apheresis therapy art was known, as evidenced by the teachings of Nilsson.
Nilsson teaches methods for the reduction or elimination of one or more components from a blood product or a fluid (entire document; see abstract.) Nilsson teaches that depending on the starting antibody titer that would be against the product or organ being delivered (in one example, Nilsson uses the amount of anti-A or anti-B antibody titers when a subject is receiving a blood group incompatible transplantation), the plasma volume of the patient, the filter (i.e. normally for an adult a plasma filter for treatment of an adult), and the quantity of adsorbent with ligands which the antibody desired for removal would bind, the expert could adjust the apheresis parameters, such as the flow rate of the blood line to ensure that more antibodies were removed from the blood product. Therefore, if the antibody titer/concentration in the patient against the product being delivered to the patient is high, then the flow rate would be lowered, to ensure the most amount of antibodies are cleared prior to delivery of the rAAV (¶[0015][0026][0029-0030][0042-0045]).
Given the teachings of Ferreira, one of skill in the art would be aware of methods to perform anti-AAV plasmapheresis prior to recombinant AAV treatment. Given the teachings of Nilsson, one of skill in the art would be apprised as to the mechanisms and parameters that may be adjusted to ensure the greatest amount of anti-AAV antibodies are removed from the subject prior to administering the therapeutic rAAV. According to Nilsson, one of those parameters subject to adjustment is the flow rate, meaning the flow rate can be reduced in order to ensure the most amount of antibodies are removed, and would be adjusted according to the pre-apheresis existing antibody titers. Given the combined teachings of Nilsson and Ferreira, one of skill in the art would be apprised as to determining the pre-apheresis anti-AAV antibody titers, and adjusting the apheresis time accordingly, meaning the time of rAAV delivery occurs sooner for those with low pre-apheresis anti-AAV antibody titers and later for those with higher anti-AAV antibody titers. Therefore, arriving at the limitations of instant claims 1-2 and 106-111 would be obvious to a skilled artisan.
It would have been obvious to one of ordinary skill in the art to modify the methods taught by Ferreira in order to analyze the pre-apheresis anti-AAV antibody titer and adjust the flow rate, thereby taking more time to clear the blood of anti-AAV antibodies in a patient with a higher anti-AAV titer. One would have been motivated to do so, given the suggestion by Nilsson that the flow rate in a plasmapheresis method could be lowered to ensure that more undesired product, such as antibodies against the product to be used in therapy, could be removed. There would have been a reasonable expectation of success, given the knowledge that adjustment of these parameters was known to a skilled artisan, as taught by Ferreira and Nilsson. Thus, the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art at the time the invention was made.
(New rejection.) Claims 97 and 99 are rejected under 35 U.S.C. 103 as being unpatentable over Ferreira and Nilsson as applied to claims 1-2, 5, 7, 12, 15, 21, 23-25, 46, 48, 50-52, 68, 88-95, and 106-111 above, and further in view of High et. al. (US20190192693A1, Priority 09/02/2016; CITED ART OF RECORD; hereafter “High”.)
The Prior Art
The teachings of Ferreira and Nilsson have been set forth supra. While Ferreira teaches that a variety of serotypes and sequences of AAV capsids and VP1, VP2, and/or VP3 proteins thereof may be used in the apheresis methods, and that said capsids, empty capsids, and/or VP1-3 proteins may be bound to the matrix, Ferreira fails to explicitly teach SEQ ID NOs: 1-2. Nilsson fails to cure this deficiency. However, a variety of sequences for AAV, especially rAAV, were known in the art at the time of filing and would be obvious to use in such a method, as evidenced by High.
High teaches methods and uses of treating a disease in a mammal through administration of rAAV comprising heterologous genes (entire document; see abstract; ¶[0049]). High teaches exemplary AAV capsid sequences, including SEQ ID NO: 1 (AAV-LK03 VP1 capsid protein, aligns with 100% identity to instant SEQ ID NO:2) and SEQ ID NO:2 (AAV 401 VP1 capsid protein, aligns with 100% identity to instant SEQ ID NO:1). High teaches these non-natural variants would be useful as their sequences would be distinct from other serotypes, and therefore would be useful for treatment purposes in individuals (¶[0060-0061]). However, it would be obvious to a skilled artisan that after the initial priming delivery/vaccination of the LK03 or 4-1 AAV serotypes, that one would likely need to use apheresis to clear the blood of antibodies which would subsequently be present and prevent the efficacy of subsequent booster administrations of the LK03 or 4-1 rAAV. Additionally, it would be helpful even prior to administration of these engineered rAAV to perform apheresis to ensure that any antibodies present in the patient that had any sort of cross-reactivity to the LK03 and/or 4-1 rAAV would be precleared from the subject to ensure the efficacy of rAAV delivery of the heterologous gene payload to the host. Therefore, given the teachings of Ferreira, Nilsson, and High, a skilled artisan would find it obvious to arrive at instant claims 97 and 99.
It would have been obvious to one of ordinary skill in the art to modify the methods taught by Ferreira and Nilsson in order to deliver a variety of genes either lost or upregulated in genetic disorders, thereby providing therapeutic options to treat said disorders, and to utilize apheresis to preclear the subject’s blood of any potential anti-AAV interfering antibodies. One would have been motivated to do so, given the suggestion by High to use AAV gene therapy to treat disorders, and to use rAAV that would have lower seroprevalence in the host. There would have been a reasonable expectation of success, given the knowledge that AAV gene therapy methods could be more successfully employed after removing AAV-specific antibodies prior to the AAV gene therapy vector treatment, as taught by Ferreira, and also given the knowledge that engineering AAV vectors to be less immunogenic and to encode proteins important to treat diseases had been suggested in the art, as taught by High. Thus the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art at the time the invention was made.
Response to Arguments
Applicant’s arguments, see “Remarks”, filed 09/18/2025, with respect to the rejection of the claims under 35 USC 102 in view of Ferreira have been fully considered and are persuasive. Therefore, the rejection has been withdrawn, as has the 35 USC 103 rejection of Ferreira in further view of High. However, upon further consideration, new grounds of rejection are made in view of Nilsson. In the interest of compact prosecution, the arguments presented regarding Ferreira and High will be addressed as applicable herein.
Applicant argues Ferreira fails to describe adjusting the timing of the rAAV administration based upon the pre-apheresis antibody titer. The Office found this argument persuasive. However, the art was apprised as to determining pre-apheresis antibody titers against the therapeutic meant to be delivered, and adjusting parameters of the apheresis method accordingly, as taught by Nilsson. Nilsson teaches that if the antibody titers to the target therapeutic are high, then the flow rate of the apheresis method (e.g. removing the blood product, clearing said product of antibody by running through a filter/matrix, and returning to subject) could be reduced, thus increasing the time for the overall apheresis method and increasing the time between when the blood product is returned to the subject and when said subject finally receives the therapeutic. Therefore, while Ferreira may not teach this limitation, this optimization was known in the art for apheresis methods, as evidenced by Nilsson as set forth supra.
Applicant argues that High fails to cure the deficiencies of Ferreira. While this was persuasive with respect to adjustment of rAAV delivery after apheresis, it was not persuasive in light of the new 35 USC 103 rejection in view of both Ferreira and Nilsson. High still renders obvious the AAV sequences for reasons set forth supra.
For at least these reasons, the claimed invention is still determined to be obvious in light of the teachings of the prior art.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to RACHEL B GILL whose telephone number is (571)272-3129. The examiner can normally be reached on M to F 8:00 AM to 5:00 PM Eastern.
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/RACHEL B GILL/Primary Examiner, Art Unit 1671