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 12/15/2025.
Election/Restrictions
Applicant’s election without traverse in the Reply filed on 12/15/2025 of Group III, claims 16-33 is acknowledged.
Applicant has elected in the Reply filed on 12/15/2025 the following species:
A. the affinity tag is a histidine tag (His-tag) (claim 28)
Because applicant did not distinctly and specifically point out the supposed errors in the species election requirement, the election has been treated as an election without traverse (MPEP § 818.03(a)).
The Restriction/Election Requirements are thus deemed proper and are made FINAL.
Claims 1 and 15-33 are pending.
Claims 1 and 15 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 12/15/2025.
Claims 16-33 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 16-19 and 21-33 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 17-19 and 21-33 depend directly or indirectly from claim 16.
The claim 16 limitations directed to an abstract idea (mental processes) are 4) quantifying the polypeptides comprising signal peptide tags, the signal peptide tags or barcoding sequences of the signal peptide tags secreted to out of the transformed host cells.
This judicial exception is not integrated into a practical application because the data gathering steps required to use the quantifying do not add a meaningful limitation to the method as they are insignificant extra-solution activity.
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 16 limitations directed to well understood, routine, conventional activity already engaged in by the scientific community are 1) constructing vectors for various signal peptides to establish a library; 2) transforming host cells with the vectors; 3) expressing the polypeptides comprising signal peptide tags from the transformed host cells; and 4) quantifying the polypeptides comprising signal peptide tags, the signal peptide tags or barcoding sequences of the signal peptide tags secreted to out of the transformed host cells, wherein the vectors comprising each of the nucleic acid molecules encoding the polypeptides comprising signal peptide tags, and wherein each of the signal peptide tags comprises a barcoding sequence site consisting of three or more amino acids barcoding the corresponding signal peptide and the three or more amino acids are selected from the group consisting of leucine (L), proline (P), alanine (A), tryptophan (W), tyrosine (Y), threonine (T), serine (S), glutamate (E), and aspartate (D).
Egloff (04/22/2019) Nature Methods volume 16 pages 421 to 428 cited in the 12/1/2023 IDS (hereinafter referred to as "Egloff") teaches 1) constructing vectors for various signal peptides to establish a library; 2) transforming host cells with the vectors; 3) expressing the polypeptides comprising signal peptide tags from the transformed host cells; and 4) quantifying the polypeptides comprising signal peptide tags, the signal peptide tags or barcoding sequences of the signal peptide tags secreted to out of the transformed host cells, wherein the vectors comprising each of the nucleic acid molecules encoding the polypeptides comprising signal peptide tags, and wherein each of the signal peptide tags comprises a barcoding sequence site consisting of three or more amino acids barcoding the corresponding signal peptide and the three or more amino acids are selected from the group consisting of leucine (L), proline (P), alanine (A), tryptophan (W), tyrosine (Y), threonine (T), serine (S), glutamate (E), and aspartate (D) (see entire document especially Abstract, pages 426-427, Supplemental methods pages 1-2, Figures 1 and 3a; Supplemental Figures and Table 1).
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 16-30 and 32-33 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Egloff (04/22/2019) Nature Methods volume 16 pages 421 to 428 cited in the 12/1/2023 IDS (hereinafter referred to as "Egloff").
With regards to claims 16-30 and 32-33, Egloff teaches:
a) as in claims 16-30 and 32-33, a method for selecting specific signal peptides that express a target protein in host cells and secrete the target protein to out of the host cells, the method comprising: 1) constructing vectors for various signal peptides to establish a library; 2) transforming host cells with the vectors; 3) expressing the polypeptides comprising signal peptide tags from the transformed host cells; and 4) quantifying the polypeptides comprising signal peptide tags, the signal peptide tags or barcoding sequences of the signal peptide tags secreted to out of the transformed host cells, wherein the vectors comprising each of the nucleic acid molecules encoding the polypeptides comprising signal peptide tags, and wherein each of the signal peptide tags comprises a barcoding sequence site consisting of three or more amino acids barcoding the corresponding signal peptide and the three or more amino acids are selected from the group consisting of leucine (L), proline (P), alanine (A), tryptophan (W), tyrosine (Y), threonine (T), serine (S), glutamate (E), and aspartate (D); wherein the host cells are CHO cells; wherein step 3) further comprises 3-1) isolating and purifying the polypeptides comprising signal peptide tags using affinity tags after expression; wherein step 3) further comprises 3-2) treating the polypeptides comprising signal peptide tags with trypsin; wherein in step 4), the quantification is performed by LC-MS/MS; wherein each of the signal peptide tags further comprises a proteolytic cleavage site at the N-terminus (front end) of the barcoding sequence such that the barcoding sequence is cleaved by the protein; wherein the proteolytic cleavage site is a trypsin cleavage site; wherein the proteolytic cleavage site is selected from the group consisting of lysine (K) and arginine (R); wherein the proteolytic cleavage site is linked to the barcoding sequence via a linker; wherein the linker comprises one or more glycine (G) residues; wherein each of the polypeptides comprising signal peptide tags further comprises an affinity tag at the end of the barcoding sequence to isolate and purify the barcoding sequence from culture media of the host cells; wherein the affinity tag is a His-tag composed of 2 to 15 histidine residues; wherein each of the signal peptide tags is independently represented by Structure 1:
<Structure l>
Trypsin cleavage site-linker-barcoding sequence-linker-affinity tag-trypsin cleavage site; wherein the target protein is fused to the N-termini of the signal peptide tags of the polypeptides; wherein the signal peptides are fused to the N-terminus of the target protein (see entire document especially Abstract, pages 426-427, Supplemental methods pages 1-2, Figures 1 and 3a; Supplemental Figures and Table 1).
Thus, Egloff anticipates the present claims.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the Examiner should be directed to Christian Boesen whose telephone number is 571-270-1321. The Examiner can normally be reached on Monday-Friday 9:00 AM to 5:00 PM.
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/CHRISTIAN C BOESEN/Primary Examiner, Art Unit 1684
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