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 .
Election/Restrictions
Applicant’s election without traverse of Group I (claims 1, 2, 6, 8-10, 13, 16, 18, 20, 27, 39, 44, 45, and 55) drawn to a composition of proteinaceous molecule; and Applicants’ election of species without traverse: the proteinaceous molecule of TGIRDRKKKNKARS (SEQ ID NO: 3); and Claims 1, 2, 8, 10, 20, 27, 39, 45, and 55 read on the elected species, in the reply filed on May 29, 2026 is acknowledged.
The species of group I, therefore claims 1, 2, 6, 8-10, 20, 27, 39, 44, 45, and 55 which read on the elected species has been considered. Claims 1, 2, 6, 8-10, 20, 27, 39, 44, 45, and 55 are hereby examined on the merits.
Claims 13, 16, 18, 29, and 35 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 May 29, 2026.
Priority
This application is a 371 of PCT/AU2022/050363, filed April 20, 2022.
This application claims priority to Australian Provisional Application No. 2021901169, filed April 20, 2021 and Australian Provisional Application No. 2022900358, filed February 18, 2022.
Status of Claims
Claims 1, 2, 6, 8-10, 13, 16, 18, 20, 27, 29, 35, 39, 44, 45, and 55 were filed June 27, 2024.
Claims 13, 16, 18, 29, and 35 are withdrawn for further consideration.
Claims 1, 2, 6, 8-10, 20, 27, 39, 44, 45, and 55 are currently examined on the merits herein.
Information Disclosure Statement
The information disclosure statements (IDS) is not submitted.
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code (see [0135]). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
The use of the term Triton X-100 (see [0035], [0036], [0039], [0040], [0041], [0208], [0228], [0251], and [0252]), which is a trade name or a mark used in commerce, have been noted in this application. The terms should be accompanied by the generic terminology; furthermore the terms should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Appropriate correction is required.
Claim Interpretation
The election of species of SEQ ID NO:3 read on claims 1, 2, 8, 10, 20, 27, 39, 45, and 55.
I. BRI of claim 9 is the proteinaceous molecule according to claim 8, wherein Z1 comprises an amino acid sequence represented by Formula III:BiX4X5X6 (Formula III) wherein: Bi is absent or is an N-terminal blocking residue; X4 is absent or is selected from any amino acid; X5 is absent or is selected from any amino acid; and X6 is absent or is selected from any amino acid. The claim is given this construction in view of the definition of Variant ACE2 peptides, of the specification, which states that the present invention also contemplates ACE2 peptides that are variants of wild-type or naturally-occurring ACE2 protein or their fragments. Such "variant" peptides include proteins derived from the native protein by deletion (so-called truncation) or addition of one or more amino acids to the N-terminal and/or C-terminal end of the native protein; deletion or addition of one or more amino acids at one or more sites in the native protein; or substitution of one or more amino acids at one or more sites in the native protein (see [0107]), and variant proteins encompassed by the present invention are biologically active, that is, they continue to possess a desired biological activity of the native protein (e.g., binding to an LSD1 polypeptide; or binding to an IMP a polypeptide). Such variants may result from, for example, genetic polymorphism or from human manipulation (see [0108]). Also, the instant specification states, in some embodiments, the proteinaceous molecules of the invention
generally comprise, consist, or consist essentially of an amino acid sequence represented by Formula Ill: X1 G I RX2RX3X4X5X6X7AX8S (see [0088]), X1 is selected from any small or polar amino acid (preferably, a T or S amino acid), or modified forms thereof (see [0089]); X2 is selected from a D or N amino acid, or modified forms thereof (see [0090]); X3, X4, and X5 are each independently selected from K and Q amino acids, or modified forms thereof (see [0091]); X6 is selected from any polar amino acid (e.g., an N, K, or D amino acid), or a modified form thereof (see [0092]); X7 is selected from a K or Q amino acid, or a modified form thereof (see [0093]); X8 is selected from an R, G, or S amino acid, or a modified form thereof (see [0094]).
Therefore, the election of species of SEQ ID NO:3 read on claim 9.
II. BRI of claim 44 is the proteinaceous molecule of claim 39, wherein the C-terminal tail region corresponds to at least residues 763 to 805 of the wild-type human ACE-2 protein. The claim is given this construction in view of the definition of C-terminal ACE2 peptides of the specification, which states ACE2 peptide comprises, consists, or consists essentially of an amino acid sequence that corresponds to the C-terminal tail region (i.e., residues 763-805) of the full-length human ACE2 protein sequence (as set forth in SEQ ID NO: 1), or a fragment thereof (see [0080]). The election of species of SEQ ID NO:3 read on claim 44.
III. “consisting essentially of” in Claims 1 and 39
It is noted that for the purposes of searching for and applying prior art under 35 U.S.C. 102 and 103, absent a clear indication in the specification or claims of what the basic and novel characteristics actually are, "consisting essentially of" will be construed as equivalent to "comprising." See, e.g., PPG, 156 F.3d at 1355, 48 USPQ2d at 1355 (see MPEP 2111.03). The instant specification provides no such teaching or guidance, thus supporting the interpretation of "consisting essentially of' as equivalent to "comprising."
Claim Objections
Claim 9 objected to because of the following informalities: comma missing after the claim statement “The proteinaceous molecule according to claim 8”.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 39 rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 39 recites the broad recitation “comprising, consisting, or consisting essentially of, an amino acid sequence corresponding to the C-terminal tail region of an ACE-2 protein”, and the claim also recites “optionally wherein the molecule comprises less than 50 amino acid residues”, and also recites “or less than 25 amino acid residues, or less than 15 amino acid residues, optionally wherein the amino acid sequence comprises a nuclear localization sequence”, which is the narrower statement of the range/limitation. The claim is considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claim. The use of the optional phrase “comprising” is not clear; and the instant specification does not provide if the molecule comprises less than 50 amino acid residues, or less than 25 amino acid residues, or less than 15 amino acid residues, optionally wherein the amino acid sequence comprises a nuclear localization sequence. One of ordinary skill in the art would not be reasonably apprised of the scope of the invention. See MPEP §2173.05(d).
Appropriate clarification is required.
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 1, 2, 6, 8-10, 39, and 44, are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural phenomenon/natural product without significantly more. Claims 1, 2, 6, 8-10, 39, and 44, recite a naturally occurring product, which is not markedly different from its naturally occurring counterpart. See MPEP §§ 2106 et seq.
Claims 1, 2, 6, 8-10, 39, and 44, are directed to a composition proteinaceous molecule, species selected as TGIRDRKKKNKARS, an amino acid sequence corresponding to the C-terminal tail region of an ACE-2 protein.
The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception for the following reasons. This judicial exception is not integrated into a practical application because the claimed composition comprises naturally occurring components. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because for the following reasons.
Step 1: Is the claim to a process, machine, manufacture or composition of matter? The instant claims are directed to a statutory patent-eligible subject matter category, a composition of matter.
Step 2a Prong 1: Is the claim directed to a law of nature, a natural phenomenon (Product of nature), or an abstract idea? The claims are directed to a natural phenomenon, specifically a natural-based product limitation. The amino acid sequence TGIRDRKKKNKARS corresponds to both a methylation site and a ubiquitin site located in the C-terminal tail region of the human ACE2 sequence (see instant specification [0013]-[0015]).
Step 2a Prong 2: Does the claim recite additional elements that integrate the judicial exception into a practical application? This judicial exception is not integrated into a practical application because the composition being claimed comprises naturally occurring components (MPEP § 2106.04(d)(III)).
Step 2b: Does the claim recite additional elements that amount to significantly more than the judicial exception? Claims 1, 2, 6, 8-10, 39, and 44 only recite the peptide, which is a natural phenomenon exception. Because there are no additional claim elements besides the judicial exception, the claim does not amount to significantly more than the judicial exception (MPEP § 2106.05).
Therefore, claims 1, 2, 6, 8-10, 39, and 44 are patent ineligible.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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 1, 2, 6, 8-10, 44, and 55 are rejected under 35 U.S.C. 102 (a)(1) as being anticipated by over Mészáros et. al. (“Short linear motif candidates in the cell entry system used by SARS-CoV-2 and their potential therapeutic implications”; Bálint Mészáros, Hugo Sámano-Sánchez, Jesús Alvarado-Valverde, Jelena Čalyševa, Elizabeth Martínez-Pérez, Renato Alves, Denis C. Shields, Manjeet Kumar, Friedrich Rippmann, Lucía B. Chemes, Toby J. Gibson; Sci. Signal. 14, eabd0334; page 1-25; published January 12, 2021).
Mészáros et. al. identifies several molecular links and testable hypotheses that could uncover mechanisms of SARS-CoV-2 attachment, entry, and replication against which it may be possible to develop host-directed therapies that dampen viral infection and disease progression (see Abstract). Mészáros et. al. teaches SARS-CoV-2, like SARS-CoV, uses the angiotensin-converting enzyme 2 (ACE2) as a receptor to attach to host cells. ACE2 is a single-pass type I membrane protein with a short cytosolic C-terminal region (see Introduction). Mészáros et. al. examined the sequences of ACE2 and integrins with the Eukaryotic Linear Motif resource and identified candidate short linear motifs in their short, unstructured, cytosolic tails with potential roles in endocytosis, membrane dynamics, autophagy, cytoskeleton, and cell signaling (see Abstract). Thus, Mészáros et. al. identified a set of conserved candidate short linear motifs in the ACE2 and integrin proteins, which are likely to act in the cell entry system of SARS-CoV-2 and provide molecular links to understand how the virus recognizes target membranes, enters into cells, and repurposes intracellular membrane components to drive its replication, the molecular links might provide clues toward drugging SARS-C0V-2 infections (see page 2, right col, paragraph 3). Mészáros et. al. discloses that short linear motif candidates in the ACE2 tail is intrinsically disordered across the region following the transmembrane helix (residues 769 to 805) (see page 5, right col, paragraph 3) and (see Table 1) [e.g., C-terminal residues 769 to 805 of Mészáros et. al. overlaps with the amino acid residues of the instant invention].
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As shown above, Mészáros et. al. illustrates the alignment of ACE2 conserved motifs in the cytosolic C-terminal tail following the transmembrane helix. Multiple sequence alignment of ACE2 transmembrane and C-terminal regions using 25 homologous sequences from different vertebrate lineages and showing their motif conservation. The names (bold) and key residues of the motifs are displayed above the alignment (ɸ stands for a bulky hydrophobic residue), including a conserved tyrosine (bold) and excluded positions (red and crossed). Red boxes mark the conservation range of the binding motif (all sequences) and NPY motif (in mammals, birds, and some fish). Organism names, UniProt IDs (UniParc for hagfish), and sequence numberings are listed on the left side of the alignment. The location of the region shown in the alignment is indicated in a representative diagram of the ACE2 protein (see page 9, Fig. 3) [e.g., C-terminal residues 741 to 805 of H. sapiens (Q9BYF1) overlaps with the amino acid residues of the instant invention].
Mészáros et. al. teaches Tyr781 in the ACE2 tail creates a potential multiway molecular switch regulated via phosphorylation (see page 11, left col, paragraph 1).
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Mészáros et. al. summarizes ACE2 C-terminus phosphorylation, acetylation, ubiquitylation, sites (see page 11, Fig. 4.). For claims 1, 2, 8-10, 44, and 55: SEQ ID: Q9BYF1 of Mészáros et. al. have exact same and/or shares at least 80% sequence identity with an amino acid sequence as in instantly claimed sequence.
For claim 6: Mészáros et. al. teaches the methylated K (marked in red boxes below) residues in the C-terminus ACE2 (see page 11, Fig. 4).
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Accordingly, the claims are anticipated.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
Claims 20 and 27 are rejected under 35 U.S.C. 103 as being unpatentable over Mészáros et. al. (“Short linear motif candidates in the cell entry system used by SARS-CoV-2 and their potential therapeutic implications”; Bálint Mészáros, Hugo Sámano-Sánchez, Jesús Alvarado-Valverde, Jelena Čalyševa, Elizabeth Martínez-Pérez, Renato Alves, Denis C. Shields, Manjeet Kumar, Friedrich Rippmann, Lucía B. Chemes, Toby J. Gibson; Sci. Signal. 14, eabd0334; page 1-25; published January 12, 2021), as previously applied to claims 1, 2, 6, 8-10, 44, and 55; and further in view of Kliche et. al. (“Cytoplasmic short linear motifs in ACE2 and integrin β3 link SARS-CoV-2 host cell receptors to mediators of endocytosis and autophagy”; Johanna Kliche, Hanna Kuss, Muhammad Ali, Ylva Ivarsson; Sci. Signal. 14, eabf1117; page 1-12; published January 12, 2021).
The teachings of Mészáros et. al. are discussed above. However, Mészáros et. al. does not teach specifically about the experimental conditions. Kliche et. al. teaches about the binding affinity and testing conditions of several motifs in the receptor C-terminal tail protein sequences.
Kliche et. al. measured the binding affinity of predicted interactions between
short linear motifs in the cytoplasmic tails of ACE2 and integrin β3 with proteins that mediate endocytic trafficking (see Abstract). Kliche et. al. teaches molecular links between cell receptors and mediators of endocytosis and autophagy that may facilitate viral entry and propagation (see Abstract).
It would have been obvious to combine the teaching of Mészáros et. al. and Kliche et. al. before the effective filing date of the claimed invention by utilizing the cytosolic potential of the receptor tails and considering the several motifs in the receptor tails as potential peptide inhibitor, and arrive at the instantly claimed invention. One of ordinary skill in the art would have been motivated to utilize the teachings of Mészáros et. al. that the very C-terminal region of ACE2 contains a binding motif candidate, and the tail of ACE2 is facing the cytosol, it is available to interact with the appropriate specificity (see page 10, right col, paragraph 2);
with a reasonable expectation of success because Kliche et. al. validates potent inhibitors of viral replication (see page 7, right col, paragraph 4). Thus, one skilled in the art can predict peptide interactions that could uncover mechanisms of SARS-CoV-2 attachment, entry, and replication, with an expectation to succeed in developing host-directed therapies that dampen viral infection and disease progression (Mészáros et. al., see Abstract).
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Regarding claim 20: Kliche et. al. discloses the binding conditions as phosphate-buffered saline (PBS) (pH 7.4) (see MATERIALS AND METHODS, page 8-9). The constituents are in direct correlation with the pharmaceutically acceptable carriers/diluents as defined by instant specification which states the formulations of the invention are administered in pharmaceutically acceptable solutions, which may routinely contain pharmaceutically acceptable concentrations of salt, buffering agents, preservatives (see instant Specification [0189]).
Regarding claim 27: Mészáros et. al. teaches that combination therapies using remdesivir together ….with other kinase inhibitors depending on the infection stage might provide promising avenues for fighting COVID-19 infection (see page 19, left col, paragraph 2).
Claim 39 is rejected under 35 U.S.C. 103 as being unpatentable over Mészáros et. al. (“Short linear motif candidates in the cell entry system used by SARS-CoV-2 and their potential therapeutic implications”; Bálint Mészáros, Hugo Sámano-Sánchez, Jesús Alvarado-Valverde, Jelena Čalyševa, Elizabeth Martínez-Pérez, Renato Alves, Denis C. Shields, Manjeet Kumar, Friedrich Rippmann, Lucía B. Chemes, Toby J. Gibson; Sci. Signal. 14, eabd0334; page 1-25; published January 12, 2021) and Kliche et. al. (“Cytoplasmic short linear motifs in ACE2 and integrin β3 link SARS-CoV-2 host cell receptors to mediators of endocytosis and autophagy”; Johanna Kliche, Hanna Kuss, Muhammad Ali, Ylva Ivarsson; Sci. Signal. 14, eabf1117; page 1-12; published January 12, 2021) as previously applied to claims 1, 2, 6, 8-10, 20, 27, 44, and 55 and further in view of Nguyen Ba et. al. (“NLStradamus: a simple Hidden Markov Model for nuclear localization signal prediction”; Alex N Nguyen Ba, Anastassia Pogoutse, Nicholas Provart and Alan M Moses; BMC Bioinformatics 2009, 10:202, page 1-11; published June 29, 2009).
The teachings of Mészáros et. al. and Kliche et. al. are discussed above. Mészáros et. al. and Kliche et. al. do not teach about the “the amino acid sequence comprises a nuclear localization sequence”.
Nguyen Ba et. al. teaches Nuclear localization signals (NLSs) are stretches of residues within a protein that are important for the regulated nuclear import of the protein; the classical NLS contains specific patterns of basic residues (see Abstract). Nguyen Ba et. al. further teaches that classical NLSs show characteristic patterns of basic residues loosely matching two consensus sequences, K(K/R)X(K/R) and KRX10–12KRXK (see page 2, left col, paragraph 2). Nguyen Ba et. al. disclosed a simplified approach to predicting nuclear localization signals and show that this method can be applied to multiple species ( see Conclusion, page 9, left col, paragraph 2).
It would have been obvious to combine the teachings of Mészáros et. al., Kliche et. al., and Nguyen Ba et. al., before the effective filing date of the claimed invention to identify stretches of basic residues in protein sequences (Nguyen Ba et. al. page 7, right col, paragraph 2) as an effective and stable peptide with high-affinity nuclear localization sequence. One of ordinary skill in the art would have been motivated to do so with an expectation to succeed in preparing potent nuclear-specific ACE2 peptide inhibitors. Therefore, the presently claimed invention was prima facie obvious to one of ordinary skill in the art at the time of the effective filing date.
Claim 45 is rejected under 35 U.S.C. 103 as being unpatentable over Mészáros et. al. (“Short linear motif candidates in the cell entry system used by SARS-CoV-2 and their potential therapeutic implications”; Bálint Mészáros, Hugo Sámano-Sánchez, Jesús Alvarado-Valverde, Jelena Čalyševa, Elizabeth Martínez-Pérez, Renato Alves, Denis C. Shields, Manjeet Kumar, Friedrich Rippmann, Lucía B. Chemes, Toby J. Gibson; Sci. Signal. 14, eabd0334; page 1-25; published January 12, 2021) and Kliche et. al. (“Cytoplasmic short linear motifs in ACE2 and integrin β3 link SARS-CoV-2 host cell receptors to mediators of endocytosis and autophagy”; Johanna Kliche, Hanna Kuss, Muhammad Ali, Ylva Ivarsson; Sci. Signal. 14, eabf1117; page 1-12; published January 12, 2021) as previously applied to claims 1, 2, 6, 8-10, 20, 27, 44, and 55 above and further in view of Ense˜nat-Waser et. al. (“Direct Visualization by Confocal Fluorescent Microscopy of the Permeation of Myristoylated Peptides Through the Cell Membrane”; Roberto Ense˜nat-Waser, Franz Martin, Fernando Barahona, Jes´us Vazquez, Bernat Soria, and Juan A. Reig; IUBMB Life, 54: 33–36; published January 3, 2008).
The teachings of Mészáros et. al. and Kliche et. al. are discussed above. Mészáros et. al. and Kliche et. al. do not teach about the “proteinaceous composition comprises a protecting moiety, optionally Myr”.
Ense˜nat-Waser et. al. studied the permeability through the cellular membrane of synthetic peptides containing an hydrofobic moiety, used a 13-mer myristoylated peptide labeled with a N-terminal fluorescent probe (see Abstract). Ense˜nat-Waser et. al. discloses use of the modified peptides, including a myristoylated chain in the N-terminal side, to improve their intrinsically low permeability for functional experiments in intact cells(see page 1, right col, paragraph 2). Ense˜nat-Waser et. al. demonstrated that the inclusion of a myristoylated chain in short peptides enhances their liposolubility, allowing the diffusion through the cell membrane and their interaction with cytoplasmatic constituents (see page 2, right col, paragraph 2).
It would have been obvious to combine the teachings of Mészáros et. al., Kliche et. al. and Ense˜nat-Waser et. al., before the effective filing date of the claimed invention utilizing N-terminal myristoylated peptides as an effective and stable peptide improving their permeability through cell membrane. One of ordinary skill in the art would have been motivated to do so with an expectation to succeed in preparing potent cell penetrating peptide inhibitors. Therefore, the presently claimed invention was prima facie obvious to one of ordinary skill in the art at the time of the effective filing date.
Conclusion
No claim is allowed.
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/KOYELI BANERJEE/Examiner, Art Unit 1658
/Melissa L Fisher/Supervisory Patent Examiner, Art Unit 1658
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