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 .
Drawings
The petition from Applicant to accept colored photographs/drawings filed 3/24/2026 was granted by the Office of Quality Assurance on 5/22/2026. Accordingly, the colored versions of Fig 1-6 filed 1/12/2026 have been examined.
The colored drawings are objected to because the drawings do not possess satisfactory reproduction characteristics as required by 37 C.F.R. 1.84. Specifically, all of the text in Fig 1, 2, 3, 4 and 6, the text used for the exponents in the X axis in Fig 5, and the text of the legend in Fig 5 measures less than 0.32 cm (1/8 inch) and, therefore, does not permit adequate reproduction (see section (p)(3) of 37 C.F.R. 1.84).
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
The Examiner suggests providing larger graphs/images so that their accompanying text can be enlarged to meet the height requirement set forth in section (p)(3) of 37 C.F.R. 1.84. In doing so, the Applicant is encouraged to ensure that any enlarged graphs/images/text meets the requirements of section (l) of 37 C.F.R. 1.84 which stipulate that all lines, numbers and letters found in the Drawings to be durable, clean, sufficiently dark and dense, uniformly thick and well-defined.
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.
Claims 13, 15-18 and 20-22 are rejected under 35 U.S.C. 103 as being unpatentable over Jordao et al. (“Antibodies targeted to the Brain with Image-Guided Focused Ultrasound Reduces Amyloid-β Plaque Load in the TgCRND8 Mouse Model of Alzheimer’s Disease”. PLOs One. 2010 May 11;5(5):e10549)1 in view of Miles (WO 2019/169448).
Re claim 15, Jordao discloses a method of improving memory, motor skills, executive functions and/or cognitive function in a subject (“mouse”) with impaired memory and/or cognitive function (Page 1, Col 1, Lines 6-9), the method comprising: administering to the subject an antigen binding site that binds to or specifically binds to an amyloid beta protein (Page 2, Col 1, Lines 31-40); identifying a region of the brain of the subject to which acoustic energy is to be applied (Page 2, Col 1, Lines 26-31); and applying a clinically safe level of acoustic energy to the region, thereby saturating or substantially saturating the region with acoustic energy (Page 2, Col 1, Lines 26-31); thereby improving memory, motor skills, executive functions and/or cognitive function in the subject (Page 1, Col 1, Lines 6-9). Jordao does not explicitly disclose that the antigen binding site that binds to the amyloid beta protein has an affinity that is not statistically different from the antibody BIIB037 (aducanumab).
Miles, however, teaches a method of improving memory, motor skills, executive functions and/or cognitive function in a subject with impaired memory and/or cognitive function (Page 62, Lines 10-28) comprising the step of administering to the subject an antigen binding site that binds to or specifically binds to an amyloid beta protein (Page 3, Lines 9-14), wherein the antigen biding site that binds to amyloid-β has an affinity that is not statistically different from the antibody BIIB037 (aducanumab) (Page 4, Lines 3-4). Miles teaches that this antigen binding site is used in treating Alzheimer’s Disease (Page 1, Lines 12-19). Since this is the same use as Jordao’s antigen binding site, the antigen binding sites of Jordao and Miles were art-recognized equivalents at the time the invention was filed; therefore, it would have been obvious to one of ordinary skill in the art to substitute Miles’ antigen binding site (which binds to amyloid-β as one that has an affinity that is not statistically different from the antibody BIIB037 (aducanumab)) in place of Jordao’s antigen binding site since it has been held that substituting parts of an invention involves only routine skill in the art.
Re claim 13, Jordao discloses that the condition or disease for treatment is one associated with or caused by a pathological form of an amyloid beta protein (Page 2, Col 1, Lines 8-10).
Re claim 16, Jordao discloses that identifying a region of the brain as described herein includes determining a volume of the brain on the basis of symptoms displayed by the subject, or determining a volume of the brain on the basis of a known association with an amyloid beta protein, or determining a volume of the brain including a volume surrounding an site having an amyloid beta protein in a pathogenic form (Page 2, Col 1, Lines 11-14).
Re claim 17, Jordao discloses that the region of the brain is the entire brain, hemisphere, forebrain or a region of the brain of the subject known to be associated with a condition involving the presence of proteins adopting pathogenic structures in an extracellular region (“hemisphere”, Page 2, Col 1, Lines 29-31).
Re claim 18, Jordao discloses that the region may be any one or more of the following cerebrum, cerebral hemisphere, telencephalon, forebrain, cortex, frontal lobe, prefrontal cortex, precentral gyrus, primary motor cortex, premotor cortex, temporal lobe, auditory cortex, inferior temporal cortex, superior temporal gyrus, fusiform gyrus, parahippocampal gyrus, entorhinal cortex, parietal lobe, somatosensory cortex, postcentral gyrus, occipital lobe, visual cortex, insular cortex, cingulate cortex, subcortical, hippocampus, dentate gyrus, cornu ammonis, amygdala, basal ganglia, striatum, caudate, putamen, nucleus accumbens, olfactory tubercle, globus pallidus, subthalamic nuclei, piriform cortex, olfactory bulb, fornix, mammillary bodies, basal forebrain, nucleus basalis Meynert, diencephalon, thalamus, hypothalamus, midbrain, tectum, tegmentum, substantia nigra, hindbrain, myelencephalon, medulla oblongata, metencephalon, pons, cerebellum, spinal cord, brain stem and cranial nerves (“hemisphere”, Page 2, Col 1, Lines 29-31).
Re claim 20, Jordao discloses that the antigen binding site binds the same epitope on the amyloid beta protein as BIIB037 (aducanumab) (Jordao’s BAM-10 antibody is known in the art to have an antigen binding site that binds the same epitope on amyloid-β as BIIB037; this is evidenced by Arndt2 which sets forth that BIIB037 recognizes the amino acids 3-7 (N-terminus) and Fong3 which sets forth that BAM-10 recognizes these same amino acids plus more (1-12 (N-terminus))).
Re claim 21, Jordao discloses that the antigen binding site competes with BIIB037 (aducanumab) for binding to the amyloid beta protein (Jordao’s BAM-10 antibody is known in the art to have an antigen binding site that binds the same epitope on amyloid-β as BIIB037 and, thus, competes with BIIB037 for binding to amyloid-β; this is evidenced by Arndt which sets forth that BIIB037 recognizes the amino acids 3-7 (N-terminus) and Fong which set forth that BAM-10 recognizes the amino acids 1-12 (N-terminus)).
Re claim 22, Jordao as modified by Miles in the rejection of claim 15 above discloses all the claimed features with Miles teaching that the antigen binding site comprises, consists essentially of or consists of an antigen binding domain of an antibody, wherein the antigen binding domain binds to or specifically binds to amyloid-beta, wherein the antigen binding domain comprises: (i) a variable region of the heavy chain (VH) comprising a complementarity determining region (CDR) 1 comprising a sequence at least about 80%, at least 85%, at least 90%, at least 92%, at least 95%, at least 97%, at least 99% identical to a sequence set forth in SEQ ID NO: 1, a CDR2 comprising a sequence at least about 80%, at least 85%, at least 90%, at least 92%, at least 95%, at least 97%, at least 99% identical to a sequence set in SEQ ID NO: 2 and a CDR3 comprising a sequence at least about 80%, at least 85%, at least 90%, at least 92%, at least 95%, at least 97%, at least 99% identical to a sequence set forth in SEQ ID NO: 3; (ii) a VH comprising a sequence at least about 95% or 96% or 97% or 98% or 99% identical to a sequence set forth in SEQ ID NO: 15; (iii) a VH comprising a CDR1 comprising a sequence set forth in SEQ ID NO: 1, a CDR2 comprising a sequence set forth between in SEQ ID NO: 2 and a CDR3 comprising a sequence set forth in SEQ ID NO: 3; or (iv) a VH comprising a sequence set forth in SEQ ID NO: 15; and(v) a variable region of the light chain (VL) comprising a CDR1 comprising a sequence at least about 80%, at least 85%, at least 90%, at least 92%, at least 95%, at least 97%, at least 99% identical to a sequence set forth in SEQ ID NO: 4, a CDR2 comprising a sequence at least about 80%, at least 85%, at least 90%, at least 92%, at least 95%, at least 97%, at least 99% identical to a sequence set forth in SEQ ID NO: 5 and a CDR3 comprising a sequence at least about 80%, at least 85%, at least 90%, at least 92%, at least 95%, at least 97%, at least 99% identical to a sequence set forth in SEQ ID NO: 6; (vi) a VL comprising a sequence at least about 95% identical to a sequence set forth in SEQ ID NO: 16; (vii) a VL comprising a CDR1 comprising a sequence set SEQ ID NO: 4, a CDR2 comprising a sequence set forth in SEQ ID NO: 5 and a CDR3 comprising a sequence set forth in SEQ ID NO: 6; or (viii) a VL comprising a sequence set forth in SEQ ID NO: 16 (see Table 1, on pages 71,72; wherein SEQ ID No. 5 of Miles is the same as Applicant’s SEQ ID No. 1, wherein SEQ ID No. 6 of Miles is the same as Applicant’s SEQ ID No. 2, wherein SEQ ID No. 7 of Miles is the same as Applicant’s SEQ ID No. 3, wherein SEQ ID No. 8 of Miles is the same as Applicant’s SEQ ID No. 4, wherein SEQ ID No. 9 of Miles is the same as Applicant’s SEQ ID No. 5, wherein SEQ ID No. 10 of Miles is the same as Applicant’s SEQ ID No. 6, wherein SEQ ID No. 19 of Miles is the same as Applicant’s SEQ ID No. 15, and wherein SEQ ID No. 20 of Miles is substantially the same as Applicant’s SEQ ID No. 16). The motivation cited in the rejection of claim 15 also applies to this claim.
Response to Arguments
Applicant's arguments filed 2/25/2026 have been fully considered but they are not persuasive.
Applicant argues that Miles does not teach an antigen binding site that binds to or specifically binds to an amyloid beta protein and that has an affinity that is not statistically different from the antibody BIIB037 (aducanumab) as required by previous claim 19 and current claim 15.
Specifically, Applicant argues that “the Miles document relates to multi-specific antibodies, providing an antigen binding site that binds to or specifically binds to CD33 and a pathogenic protein (page 2 lines 1-5 of Miles, see also page 3 lines 9-10)” while Applicant’s invention “relates to providing an antigen binding site that binds to or specifically binds to the amyloid beta protein (in the absence of simultaneous binding to CD33)”. Applicant asserts that an antigen binding site that can simultaneously bind to both CD33 and an amyloid beta protein “must be structurally and functionally different from one that binds only amyloid beta [protein] because both amyloid beta [protein] and CD33 are structurally unrelated to one another”. This argument is not persuasive because the feature upon which applicant relies (i.e. the binding of the amyloid beta protein in the absence of simultaneous binding to CD33) is not recited in the rejection claim. Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to KAMI A BOSWORTH whose telephone number is (571)270-5414. The examiner can normally be reached Monday - Thursday 8 am - 4 pm.
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, Kevin Sirmons can be reached at (571)272-4965. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/KAMI A BOSWORTH/Primary Examiner, Art Unit 3783
1 A copy of this reference was provided by Applicant on 12/5/2022.
2 Arndt JW, Qian F, Smith BA, Quan C, Kilambi KP, Bush MW, Walz T, Pepinsky RB, Bussière T, Hamann S, Cameron TO, Weinreb PH. Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-β. Sci Rep. 2018 Apr 23;8(1):6412.
3 PG PUB 2002/0182660
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