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
Responsive to claim set of 29SEP2025
Claims pending 1-13,20
Claims currently under consideration 1-13,20
Priority
This application has a filing date of 03/24/2022 and is a CON of
PCT/IL2020/051037 09/23/2020
PCT/IL2020/051037 has PRO 63/053,752 07/20/2020
Acknowledgment is made of applicant's claim for foreign priority based on an application filed in Israel on 09/25/2019. It is noted, however, that applicant has not filed a certified copy of the 269674 application as required by 37 CFR 1.55.
Withdrawn Objection(s) and/or Rejection(s)
Any rejection not reiterated from the previous action is hereby withdrawn.
Maintained Claim Rejection(s) - 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 1-5,8-11,13 and 6,7,20 are rejected under 35 U.S.C. 103 as being unpatentable over Heyman et al (2012 Nature Nanotechnology 7:374-8 – IDS entry 5/10/2022) in view of Nikolay et al (US PubApp 20160122749).
Heyman et al teach throughout the document and particularly the title cell-free protein synthesis on a chip. More specifically, in figures 1,2 and 5 especially when taken with the penultimate paragraph of p 377, Heyman et al provides: a chamber comprising at least one surface that has a plurality of immobilized nucleic acid molecules encoding two different (e.g. green fluorescent protein (GFP) and a HA affinity tag) of a proteinaceous complex that is specifically immobilized atop an antibody against HA, bound to onto at least one entire surface; then contacts said surface with agents including RNA polymerase (RNAP) for expression thereof the components from the nucleic acids, under conditions that allow expression and immobilization of the proteinaceous complex to said at least one surface, and thereby assembling and immobilizing at least 10 proteinaceous complex molecules such that said components are expressed as separate polypeptides that associate non-covalently to form the proteinaceous complex; and finally detects the complexes as functional. The foregoing reads on claims 1(in part),2,3,4,5,8,9,10,11,13 and claim 20 lines 3-6.
As in claims 6,7, Heyman et al do not teach: assembling proteinaceous complexes of RNAP or functioning ribosomes from large and small ribosome subunits; candidate agents that disrupt such assemblies, such as set forth inter alia in claim 20 nor analysis thereof in the manner set forth in the wherein clause of claim 20b.
As set forth inter alia in claim 20, Nikolay et al teach throughout the document and especially the abstract, screening for (candidate agents that disrupt) inhibitors of ribosome assembly. And toward this end, in paragraphs 0028,0070-0072,0091, Nikolay et al suggest assembling RNAP proteinaceous complexes and/or functional ribosomes (70S) from large (50S) and small (30S) subunits like claims 6,7
It would have been prima facie obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the protein synthesis chip of Heyman et al for identifying inhibitors of ribosome or RNAP assemblies like Nikolay et al.
One of ordinary skill in the art would have been motivated to have utilized the protein synthesis chip of Heyman et al for identifying inhibitors of ribosome or RNAP assemblies like Nikolay et al in the interest of developing new antibiotics against resistant bacteria, beneficial according to Nikolay et al in paragraphs 0002-0003.
One of ordinary skill in the art would have had a reasonable expectation of success in applying the chip system of Heyman et al toward screening for new antibiotics mentioned by Nikolay et al since the chip would greatly simplify analysis by not needing extraneous cellular materials complicating but required by Nikolay alone.
As interpreted in MPEP 2114.04 IV A I the courts have held where the only difference between the prior art and that claimed was a recitation of relative dimensions of a device and a device having the claimed relative dimensions would not perform differently than the prior art device, such dimensions do not serve to patentably distinguish from the prior art and/or alternatively as interpreted in 2144.05 the courts have alternatively held a prima facie case of obviousness exists where claimed ranges or amounts do not overlap with the prior art but are merely close. Titanium Metals Corp. of America v. Banner, 778 F.2d 775, 783, 227 USPQ 773, 779 (Fed. Cir. 1985).
Here, regarding a chamber having a volume between 1 picoliter to 10 milliliter of claim 1, in figure 1, the Heyman reference discloses a reaction container 70 x 70 microns that is 200 nm deep, that is a volume of 0.98 picoliters. Absent evidence to the contrary, Heyman’s slightly smaller reaction chamber would not perform any differently from that recited in claim 1.
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Please note that the above rejection has been updated from the original version to more clearly address applicants’ newly amended claims.
Claims 1-5,8-11,13 and 6,7,12 are rejected under 35 U.S.C. 103 as being unpatentable over Heyman et al (2012 Nature Nanotechnology 7:374-8 – IDS entry 5/10/2022) in view of Church et al (US PubApp 20120171720).
Heyman et al teach throughout the document and particularly the title cell-free protein synthesis on a chip. More specifically, in figures 1,2 and 5 especially when taken with the penultimate paragraph of p 377, Heyman et al provides: a chamber comprising at least one surface that has a plurality of immobilized nucleic acid molecules encoding two different components (e.g. green fluorescent protein (GFP) and a HA affinity tag) of a proteinaceous complex that is specifically immobilized atop an antibody against HA, bound to onto at least one entire surface; then contacts said surface with agents including RNAP for expression thereof the components from the nucleic acids, under conditions that allow expression and immobilization of the proteinaceous complex to said at least one surface, and thereby assembling and immobilizing at least 10 proteinaceous complex molecules, such that said components are expressed as separate polypeptides that associate non-covalently to form the proteinaceous complex; and finally detects the complexes as functional. The foregoing reads on claims 1(in part),2,3,4,5,8,9,10,11,13.
Heyman et al do not teach: expression with aminoacyl tRNA synthetases of claims 12 & 18; and functional ribosomes from large and small subunits like claims 6,7, as noted earlier.
As in claims 12,6,7,15,16,17 Church et al suggest throughout the document and especially the abstract and figure 21 as described in paragraph 0037 in vitro transcription and translation (IVTT) with a mini-genome that necessarily includes: expression of aminoacyl tRNA synthetases; DNA encoding functional RNAP; and self-assembled ribosomes from large (50S) and small (30S) subunits.
It would have been prima facie obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the protein synthesis chip of Heyman et al for IVTT of Church et al.
One of ordinary skill in the art would have been motivated to have utilized the protein synthesis chip of Heyman et al for IVTT of Church et al in the interest of designing novel ribosomes as factories to manufacture of proteins with non-natural components or even completely non-naturally occurring polymers, benefits noted by Church et al in paragraph 0009.
One of ordinary skill in the art would have had a reasonable expectation of success in applying the chip system of Heyman et al toward making new ribosomes as in Church in light of the considerable technical overlap between the references, each employing the same materials for DNA translation in much the same way.
As interpreted in MPEP 2114.04 IV A I the courts have held where the only difference between the prior art and that claimed was a recitation of relative dimensions of a device and a device having the claimed relative dimensions would not perform differently than the prior art device, such dimensions do not serve to patentably distinguish from the prior art and/or alternatively as interpreted in 2144.05 I, the courts have alternatively held a prima facie case of obviousness exists where claimed ranges or amounts do not overlap with the prior art but are merely close. Titanium Metals Corp. of America v. Banner, 778 F.2d 775, 783, 227 USPQ 773, 779 (Fed. Cir. 1985).
Here, regarding a chamber having a volume between 1 picoliter to 10 milliliter of claim 1, in figure 1, the Heyman reference discloses a reaction container 70 x 70 microns that is 200 nm deep, that is a volume of 0.98 picoliters. Absent evidence to the contrary, Heyman’s slightly smaller reaction chamber would not perform any differently from that recited in claim 1.
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Please note that the above rejection has been updated from the original version to more clearly address applicants’ newly amended claims.
Response to Arguments
Arguing both 35USC103 rejections together, the remarks accompanying the present response argue not all elements are taught.
Applicant’s arguments have been fully considered but they are not deemed persuasive for the following reasons.
More specifically, starting with the paragraph spanning pp 6-7, the remarks assert: the claimed subject matter is drawn to multi-subunit complexes from co-localized expression sources; and the present invention creates high local concentration of components that promote in situ non-covalent assembly of functional multimeric complexes like ribosomes for on-chip spatially resolved analysis, including screening for assembly inhibitors that is not achieved in Heyman, Nikolay nor Church.
In response to applicant's argument that the references fail to show certain features of applicant’s invention, it is noted that the features upon which applicant relies (i.e., multi-subunit complexes from co-localized expression sources, high localized concentration, nor even ribosomes) are not so limited in the rejected claim(s). 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).
Concerning promotion of in situ non-covalent assembly of functional multimeric complexes for on-chip spatially resolved analysis, Applicant’s attention is respectfully invited again to: Heyman figure 5 showing multiple functional complexes taken with the last sentence of the fourth paragraph at page 377, which explicitly states “[t]hese experiments demonstrate that a localized protein source provides a means for localized assembly on [a] biochip;” Church’s title “Method of making ribosomes” & abstract which clearly states “methods for making in vitro assembled ribosomal subunits and in vitro assembled ribosomes are provided” and lastly Nikolay’s abstract which plainly states “[t]he invention relates to a method...for identifying a compound, which interferes with ribosome ...assembly...” Thus, in contrast with Applicant’s arguments, the Church reference is drawn to co-expressing ribosomes from subunits thereof, Heyman indeed enables functional assembly of functional multimeric complexes and spatially resolved analysis thereof and finally Nikolay suggests candidate agents that disrupt assembly of a ribosome.
THIS ACTION IS MADE FINAL. 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 CHRISTOPHER M GROSS whose telephone number is (571)272-4446. The examiner can normally be reached M-F 10-6.
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/CHRISTOPHER M GROSS/
Primary Examiner, Art Unit 1684
1/13/2025
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