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
This Non-Final Office Action is responsive to the communication received 11/10/2025.
Election/Restrictions
Applicant’s election without traverse in the Reply filed on 11/10/2025 of group III, claims 33-38 is acknowledged.
Applicant has elected without traverse in the Reply filed on 11/10/2025 the following species:
A. the human-like VHH amino acid sequence is SEQ ID NO:1
The Restriction/Election Requirements are deemed proper and are made FINAL.
Claims 8-14, 21-26 and 33-38 are pending.
Claims 8-14 and 21-26 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the Reply filed on 11/10/2025.
Claims 33-38 are under examination in this Office Action.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 33-38 are rejected under 35 U.S.C. 101 because the claimed invention is directed to nonstatutory subject matter. The claim(s) does/do not fall within at least one of the four categories of patent eligible subject matter because the claimed invention is directed to a judicial exception, an abstract idea (mental processes), without significantly more. Claims 34-38 depend directly or indirectly from claim 33.
The claim 33 limitation directed to an abstract idea (mental processes) are selecting the host cells that express the human-like VHH fusion protein that binds the target of interest.
This judicial exception is not integrated into a practical application because selecting does not add a meaningful limitation as it is merely a nominal or token extrasolution component of the claim.
The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the claim recites additional elements that consist of well understood, routine, conventional activity already engaged in by the scientific community.
The claim 1 limitations directed to well understood, routine, conventional activity already engaged in by the scientific community are a method for identifying a human-like heavy chain antibody variable domain (VHH) that binds a target of interest, the method comprising: (a) providing a plurality of transformed host cells comprising (i) a plurality of first expression vectors, each first expression vector comprising a nucleic acid molecule encoding a human-like VHH fusion protein comprising (aa) comprising three synthetically generated complementarity determining region (CDR) areas in a human antibody heavy chain variable domain (VH) framework in which the amino acids at each of positions 44 and 45 of the human VH framework are substituted with the amino acids at the corresponding positions of a Camelid heavy chain antibody variable domain (VHH) framework, wherein the amino acid positions are according to Kabat numbering, and (bb) a first Fc polypeptide; and (ii) a multiplicity of second expression vectors, each second expression vector comprising a nucleic acid molecule encoding a bait polypeptide comprising a second Fc polypeptide fused to a polypeptide or peptide that enables the second Fc polypeptide to be displayed on the outer surface of a host cell, the first and second Fc polypeptides acting, when the human-like VHH fusion protein is produced in the host cell, to cause the display of the human-like VHH fusion protein via pairwise interaction between the first and second Fc polypeptides; (b) cultivating the transformed host cells under conditions to induce expression of the human-like VHH fusion proteins and the bait polypeptide to produce induced host cells in which the bait polypeptide is displayed on the outer surface of the transformed host cells and the human-like VHH fusion protein is in a pairwise interaction with the bait polypeptide; (c) contacting the induced host cells with the target of interest conjugated to a detection moiety; and (d) detecting the detection moiety.
Rouet et al. (2015) Journal of Biological Chemistry volume 290 pages 11905 to 11917 cited in the 8/31/2022 IDS (hereinafter known as "Rouet") teaches a method for identifying a human-like heavy chain antibody variable domain (VHH) that binds a target of interest, the method comprising: (a) providing a plurality of transformed host cells comprising (i) a plurality of first expression vectors, each first expression vector comprising a nucleic acid molecule encoding a human-like VHH fusion protein comprising (aa) comprising three synthetically generated complementarity determining region (CDR) areas in a human antibody heavy chain variable domain (VH) framework in which the amino acids at each of positions 44 and 45 of the human VH framework are substituted with the amino acids at the corresponding positions of a Camelid heavy chain antibody variable domain (VHH) framework, wherein the amino acid positions are according to Kabat numbering, and (bb) a first Fc polypeptide; and (ii) a multiplicity of second expression vectors, each second expression vector comprising a nucleic acid molecule encoding a bait polypeptide comprising a second Fc polypeptide fused to a polypeptide or peptide that enables the second Fc polypeptide to be displayed on the outer surface of a host cell, the first and second Fc polypeptides acting, when the human-like VHH fusion protein is produced in the host cell, to cause the display of the human-like VHH fusion protein via pairwise interaction between the first and second Fc polypeptides; (b) cultivating the transformed host cells under conditions to induce expression of the human-like VHH fusion proteins and the bait polypeptide to produce induced host cells in which the bait polypeptide is displayed on the outer surface of the transformed host cells and the human-like VHH fusion protein is in a pairwise interaction with the bait polypeptide; (c) contacting the induced host cells with the target of interest conjugated to a detection moiety; and (d) detecting the detection moiety (see entire document, especially Figures 1 and 3 and pages 11905 to 11910).
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
Claims 33-38 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Rouet et al. (2015) Journal of Biological Chemistry volume 290 pages 11905 to 11917 cited in the 8/31/2022 IDS (hereinafter known as "Rouet").
With regards to claims 33-38, Rouet teaches:
a) as in claims 33-38, a method for identifying a human-like heavy chain antibody variable domain (VHH) that binds a target of interest, the method comprising: (a) providing a plurality of transformed host cells comprising (i) a plurality of first expression vectors, each first expression vector comprising a nucleic acid molecule encoding a human-like VHH fusion protein comprising (aa) comprising three synthetically generated complementarity determining region (CDR) areas in a human antibody heavy chain variable domain (VH) framework in which the amino acids at each of positions 44 and 45 of the human VH framework are substituted with the amino acids at the corresponding positions of a Camelid heavy chain antibody variable domain (VHH) framework, wherein the amino acid positions are according to Kabat numbering, and (bb) a first Fc polypeptide; and (ii) a multiplicity of second expression vectors, each second expression vector comprising a nucleic acid molecule encoding a bait polypeptide comprising a second Fc polypeptide fused to a polypeptide or peptide that enables the second Fc polypeptide to be displayed on the outer surface of a host cell, the first and second Fc polypeptides acting, when the human-like VHH fusion protein is produced in the host cell, to cause the display of the human-like VHH fusion protein via pairwise interaction between the first and second Fc polypeptides; (b) cultivating the transformed host cells under conditions to induce expression of the human-like VHH fusion proteins and the bait polypeptide to produce induced host cells in which the bait polypeptide is displayed on the outer surface of the transformed host cells and the human-like VHH fusion protein is in a pairwise interaction with the bait polypeptide; (c) contacting the induced host cells with the target of interest conjugated to a detection moiety; and (d) detecting the detection moiety and selecting the host cells that express the human-like VHH fusion protein that binds the target of interest; wherein the human VH framework further includes substitution of each of the amino acids at positions 37 and 47 with the amino acid at corresponding positions 37 and 47 of the Camelid VHH framework, wherein the amino acid positions are according to Kabat numbering; wherein the VH framework comprises the amino acid sequence of the human VH framework encoded by the IGHV3-23*04 gene in which the amino acids at positions 44 and 45 of the human VH framework are each substituted with the corresponding amino acid at positions 44 and 45 of the Camelid VHH framework encoded by the alpaca IGHV3S53 gene, wherein the amino acid positions are according to Kabat numbering; wherein the VH framework comprises the amino acid sequence of the human VH framework encoded by the IGHV3-23*04 gene and the amino acids at positions 37, 44, 45, and 47 of the human VH framework are each substituted with the corresponding amino acid at positions 37, 44, 45, and 47 of the Camelid VHH framework encoded by the alpaca IGHV3 S53 gene, wherein the amino acid positions are according to Kabat numbering; wherein each human-like VHH comprises the amino acid sequence wherein the human-like VHH comprises the amino acid sequence set forth in SEQ ID NO:1, wherein the host cell is a yeast (see entire document, especially Figures 1 and 3 and pages 11905 to 11910).
Thus, Rouet anticipates the present claims.
Conclusion
No claim is allowed.
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/CHRISTIAN C BOESEN/Primary Examiner, Art Unit 1684
