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 .
Claims 1-14 and 16-20 have been canceled.
Claims 15-17 are pending and under examination.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claim(s) 15-17 are rejected under 35 U.S.C. 103 as being unpatentable over Nitsch (US 20100202968) in view of Pereira (J. Biomedicine & Biotechnology 2012 Vol. 2012: 1-12 total 12 pages).
The current invention directs to use of yeast display library for large-scale screening of antibodies to monomeric form (designated as “negative” screening) as well as aggregate form (as “positive” screening) of a protein (e.g. amyloid beta), and identifying one or more antibodies having higher affinity to aggregate form than that of monomeric form of the protein.
Nitsch teaches manufacturing therapeutic antibodies for treating neurodegenerative diseases, including Alzheimer’s disease, Prion disease, Huntington’s disease. These pathological diseases are associated with fibril (aggregate form of specific protein relative to monomeric form). Nitsch discloses antibody screening by immobilizing synthetic Abeta-peptides (both monomeric and aggregate form) on the ELISA microplates for screening antibodies followed by different kind of further characterizations, e.g. RT-PCR, cloning, sequencing variable regions on the antibody (section 0292, 0295; Example 1). The disclosure reads on the “negative” monomeric peptide and “positive” aggregate peptide. The results in Example 2 show that few antibodies, including NI-101.11; NI-101.22, NI-101.13A and NI-101.13B were obtained.
Figure 8 shows that NI-101.11 antibody has capability to bind to aggregate (100 times “open square” fold more) and monomeric (filled square)(see description section 0323). Moreover,
Nitsch also characterizes the other NI-101.13A and NI-101.13B antibodies in binding to monomeric and aggregate (fibrillar form) and show different binding affinity (Figure 13)(section 0328).
However, the screening-scale of Nitsch is NOT a high-throughput and Nitsch does not explicitly teach using yeast display library for screening.
Pereira reference is in analogous field and is a review article focused on using yeast library in neurodegeneration research (See Title). Pereira reviews the advantage of using yeast display library in the study of amyloid-beta-peptide (see section 3 “Amyloid-beta-peptide”). Pereira reviews the advantage of amenability of using the yeast display library in high-throughput in optimal protein solubility, maintaining active and proper form on the surface and decreasing toxic effect in the cytosol (see page 4, left column and Figure 1).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the yeast display library as aught by Pereira for a large scale high-throughput screening identifying more potential candidate antibodies having preferential binding affinity to aggregate form of amyloid-beta protein than that of monomeric form . One ordinary skilled person in the field would have been motivated to use yeast library in taking the advantages of the amenability of yeast system in high-throughput screening for better results.
As to claim 16, the experiment above was conducted using amyloid beta target antigen.
Conclusion
No claim is allowed.
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CHANGHWA J. CHEU
Primary Examiner
Art Unit 1678
/CHANGHWA J CHEU/Primary Examiner, Art Unit 1678