DETAILED ACTION
Notice of Pre-AIA or AIA Status
1. 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
2. Applicant's election with traverse of Group I (claims 1-4, 8, 9, 12-15, 18-20, 22, 28 and 35-37) in the reply filed on November 26, 2025 is acknowledged. The traversal is on the ground(s) that “…at least Schellengerger does not disclose that the therapeutic protein in the fusion protein is a cytokine, which all the pending claims in Groups I and II recite. Accordingly, rejoinder of Groups I and II is respectfully requested...”, see “Response…” submitted November 26, 2026 This is not found persuasive because the prior art of record herein does disclose the said fusion protein, see rejections herein.
The requirement is still deemed proper and is therefore made FINAL.
3. Claims 1-4, 8, 9, 12-15, 18-20, 22, 28 and 35-39 are pending.
Claims 31, 38 and 39, drawn to non-elected inventions are not examined.
Claims 38 and 39 have been added.
Claims 5-7, 10, 11, 16, 17, 21, 23-27, 29, 30 and 32-34 have been added.
Claims 1-4, 8, 9, 14, 15, 18-20, 22, 28 and 31 have been amended.
Claims 1-4, 8, 9, 12-15, 18-20, 22, 28 and 35-37 are examined on the merits.
Claim Rejections - 35 USC § 112
4. 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.
5. Claim 22 is 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.
a. Claim 22 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite in that it fails to point out what is included or excluded by the claim language. In particular, the claim cites Table 1 on line 4 of the claim. Where possible, claims are to be complete in themselves. Incorporation by reference to a specific figure or table "is permitted only in exceptional circumstances where there is no practical way to define the invention in words and where it is more concise to
incorporate by reference than duplicating a drawing or table into the claim. Incorporation by reference is a necessity doctrine, not for applicant's convenience." Ex parte Fressola, 27 USPQ2d 1608, 1609 (Bd. Pat. App. & Inter. 1993) (citations omitted).
Claim Rejections - 35 USC § 102
6. 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.
7. Claim(s) 1, 2, 4, 9, 22, 28 and 35 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Schellenberger et al., WO 2010/091122 A1 (published 12 August 2010). Schellenberger discloses a fusion protein comprising linkages between an extended recombinant polypeptide(s) (XTEN(s)), sequence motif with 12 amino acid residues a biologically active protein and a payload, see sections 0008-0010 on page 3; section 00125. “[T]he XTEN is characterized in that the sum of glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P) residues constitutes more than about…or about 90%, …of the total amino acid sequence of the XTEN,” and “…designed to be substantially non repetitive. In a preferred embodiment, XTEN sequences have predominately four to six types of amino acids selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) or proline (P) that are arranged in a substantially non-repetitive sequence that is greater than about 100 to about 3000 amino acid residues, preferably greater than 400 to about 3000 residues in length. In some embodiments, XTEN… the sequence consists of non-overlapping sequence motifs wherein each of the motifs has 9 to 36 amino acid residues wherein each of the motifs consists of 4 to 6 types of amino acids selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P)”, see page 31, sections 00148 and 00149 spanning pages 31 and 32.
Biologically active proteins (BPs) XTEN are protein compositions that “…encompass fusion polypeptides that comprise one or two payload regions each comprising a biologically active protein that mediates one or more biological or therapeutic activities and at least one other region comprising at least one XTEN polypeptide.”, see page 44, section 00171.
“Examples of payloads include, but are not limited to, cytokines, enzymes, hormones and blood and growth factors. Payloads can further comprise genetically fused or chemically conjugated moieties such as chemotherapeutic agents, antiviral compounds, toxins, or contrast agents. These conjugated moieties can be joined to the rest of the polypeptide via a linker which may be cleavable or non-cleavable.”, see page 25, section 00126. The XTEN polypeptide may have multiple sites for proteolytic cleavage to release the XTEN, see page 16, sections 0079-0081; and page 44, section 00170. These sites are regarded by the Examiner as a release segment (RS) and capable of cleavage by a mammalian protease, see page 80, section 00260; and Table 10 on page 81.
“[T]he XTEN sequence consists of non-overlapping sequence motifs are from or more sequences…”, see page 4, lines 1 and 2; sections 00147- 00152 spanning pages 30-33. The sequence motifs that are the same as Applicant’s cited in Table 1 are disclosed at the end of the instant rejection.
Schellenberger teaches “…pharmaceutical compositions comprising the fusion protein of any of the foregoing embodiments and at least one pharmaceutically acceptable carrier.”, see page 8, section 0038.
The fusion proteins can be designed to have different configurations, N- to C-terminus, of a [biological active protein] BP, XTEN, an option spacer sequences.”, see page 8, section 0034.
RESULT 1 from 182.align450.rag database.
AYG93335
(NOTE: this sequence has 60 duplicates in the database searched.
See complete list at the end of this report)
ID AYG93335 standard; peptide; 12 AA.
XX
AC AYG93335;
XX
DT 30-SEP-2010 (first entry)
XX
DE XTEN sequence motif peptide SEQ ID 182.
XX
KW XTEN protein; acquired immune deficiency syndrome; anorectic;
KW antianginal; antiarthritic; antiinflammatory; cardiant;
KW cerebroprotective; coronary artery disease; crohns disease; cytostatic;
KW endocrine-gen.; extended recombinant polypeptide; factor ix deficiency;
KW factor vii deficiency; factor viii deficiency; gastrointestinal-gen.;
KW genetic-disease-gen.; glucagonoma; growth hormone deficiency;
KW growth-disorder-gen.; hypertension; hypotensive; immunostimulant;
KW immunosuppressive; ischemia; lipid metabolism disorder;
KW metabolic disorder; metabolic-gen.; multiple sclerosis;
KW muscular dystrophy; muscular-gen.; neuroprotective;
KW nutrition-disorder-gen.; ophthalmological; prader-willi syndrome;
KW protein therapy; recombinant protein; reperfusion injury;
KW retinal degeneration; rheumatoid arthritis; syndrome x; therapeutic;
KW turners syndrome; ulcerative colitis; vasotropic;
KW von willebrands disease; vulnerary.
XX
OS Unidentified.
XX
CC PN WO2010091122-A1.
XX
CC PD 12-AUG-2010.
XX
CC PF 03-FEB-2010; 2010WO-US023106.
XX
PR 03-FEB-2009; 2009US-0149669P.
PR 08-JUN-2009; 2009US-0185112P.
PR 08-JUN-2009; 2009US-0268193P.
PR 24-AUG-2009; 2009US-0236493P.
PR 25-AUG-2009; 2009US-0236836P.
PR 18-SEP-2009; 2009US-0243707P.
PR 24-SEP-2009; 2009US-0245490P.
PR 10-NOV-2009; 2009US-0280955P.
PR 10-NOV-2009; 2009US-0280956P.
PR 12-NOV-2009; 2009US-0281109P.
XX
CC PA (AMUN-) AMUNIX INC.
XX
CC PI Schellenberger V, Silverman J, Wang C, Spink B, Stemmer WP;
CC PI Geething N, To W, Cleland JL;
XX
DR WPI; 2010-K26088/55.
XX
CC PT New isolated extended recombinant polypeptide e.g. having non-repetitive
CC PT amino acid sequence, useful for treating a disease (e.g. obesity and
CC PT multiple sclerosis) and improving property (e.g. terminal half-life) of a
CC PT protein e.g. exendin-4.
XX
CC PS Claim 13; SEQ ID NO 182; 497pp; English.
XX
CC The present invention relates to a novel isolated extended recombinant
CC polypeptide (XTEN) e.g. having a non-repetitive amino acid sequence,
CC useful for treating a disease (e.g. obesity and multiple sclerosis) and
CC improving property (e.g. terminal half-life) of a protein e.g. exendin-4.
CC The invention also relates to compositions comprising extended
CC recombinant polypeptides (XTENs), isolated nucleic acids encoding the
CC compositions and vectors and host cells containing the same. XTENs are
CC generally extended length polypeptides with non-naturally occurring,
CC substantially non-repetitive sequences that are composed mainly of small
CC hydrophilic amino acids, with the sequence having a low degree or no
CC secondary or tertiary structure under physiologic conditions. XTEN
CC polypeptide compositions are useful as fusion partners that can be linked
CC to biologically active proteins (BPs), resulting in a BPXTEN fusion
CC proteins (e.g., monomeric fusions). XTENs can have utility as fusion
CC protein partners in that they can confer certain chemical and
CC pharmaceutical properties when linked to a biologically active protein to
CC a create a fusion protein. The novel composition is useful for: treating
CC glucose-related diseases, metabolic diseases, coagulation disorders, and
CC growth hormone-related disorders and conditions, such as type I or type
CC II diabetes, obesity, hyperglycemia, hyperinsulinemia, abnormal insulin
CC production, insulin resistance, syndrome X, excessive appetite,
CC insufficient satiety, glucagonoma, dyslipidemia, retinal
CC neurodegenerative processes, factor VII deficiency, factor X deficiency,
CC factor XII deficiency, hemophilia A, hemophilia B, Von Willebrand
CC disease, hypertension, acute coronary syndrome, rheumatoid arthritis,
CC reperfusion injury following ischemia, growth-hormone deficiency,
CC Turner's Syndrome, Prader-Willi Syndrome, idiopathic short stature, AIDS
CC wasting, multiple sclerosis, Crohn's disease, ulcerative colitis or
CC muscular dystrophy; and improving a property of a protein. The present
CC sequence represents a polypeptide sequence which was useful during the
CC invention as a component of a BPXTEN fusion protein.
XX
SQ Sequence 12 AA;
Query Match 100.0%; Score 61; Length 12;
Best Local Similarity 100.0%;
Matches 12; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 GESPGGSSGSES 12
||||||||||||
Db 1 GESPGGSSGSES 12
RESULT 1 from 183.align450.rag database.
AYG93336
(NOTE: this sequence has 61 duplicates in the database searched.
See complete list at the end of this report)
ID AYG93336 standard; peptide; 12 AA.
XX
AC AYG93336;
XX
DT 30-SEP-2010 (first entry)
XX
DE XTEN sequence motif peptide SEQ ID 183.
XX
KW XTEN protein; acquired immune deficiency syndrome; anorectic;
XX
OS Unidentified.
XX
CC PN WO2010091122-A1.
XX
CC PD 12-AUG-2010.
XX
CC PF 03-FEB-2010; 2010WO-US023106.
XX
PR 03-FEB-2009; 2009US-0149669P.
PR 08-JUN-2009; 2009US-0185112P.
PR 08-JUN-2009; 2009US-0268193P.
PR 24-AUG-2009; 2009US-0236493P.
PR 25-AUG-2009; 2009US-0236836P.
PR 18-SEP-2009; 2009US-0243707P.
PR 24-SEP-2009; 2009US-0245490P.
PR 10-NOV-2009; 2009US-0280955P.
PR 10-NOV-2009; 2009US-0280956P.
PR 12-NOV-2009; 2009US-0281109P.
XX
CC PA (AMUN-) AMUNIX INC.
XX
CC PI Schellenberger V, Silverman J, Wang C, Spink B, Stemmer WP;
CC PI Geething N, To W, Cleland JL;
XX
DR WPI; 2010-K26088/55.
XX
CC PT New isolated extended recombinant polypeptide e.g. having non-repetitive
CC PT amino acid sequence, useful for treating a disease (e.g. obesity and
CC PT multiple sclerosis) and improving property (e.g. terminal half-life) of a
CC PT protein e.g. exendin-4.
XX
CC PS Claim 13; SEQ ID NO 183; 497pp; English.
XX
CC The present invention relates to a novel isolated extended recombinant
CC polypeptide (XTEN) e.g. having a non-repetitive amino acid sequence,
CC useful for treating a disease (e.g. obesity and multiple sclerosis) and
CC improving property (e.g. terminal half-life) of a protein e.g. exendin-4.
CC The invention also relates to compositions comprising extended
CC recombinant polypeptides (XTENs), isolated nucleic acids encoding the
CC compositions and vectors and host cells containing the same. XTENs are
CC generally extended length polypeptides with non-naturally occurring,
CC substantially non-repetitive sequences that are composed mainly of small
CC hydrophilic amino acids, with the sequence having a low degree or no
CC secondary or tertiary structure under physiologic conditions. XTEN
CC polypeptide compositions are useful as fusion partners that can be linked
CC to biologically active proteins (BPs), resulting in a BPXTEN fusion
CC proteins (e.g., monomeric fusions). XTENs can have utility as fusion
CC protein partners in that they can confer certain chemical and
CC pharmaceutical properties when linked to a biologically active protein to
CC a create a fusion protein. The novel composition is useful for: treating
CC glucose-related diseases, metabolic diseases, coagulation disorders, and
CC growth hormone-related disorders and conditions, such as type I or type
CC II diabetes, obesity, hyperglycemia, hyperinsulinemia, abnormal insulin
CC production, insulin resistance, syndrome X, excessive appetite,
CC insufficient satiety, glucagonoma, dyslipidemia, retinal
CC neurodegenerative processes, factor VII deficiency, factor X deficiency,
CC factor XII deficiency, hemophilia A, hemophilia B, Von Willebrand
CC disease, hypertension, acute coronary syndrome, rheumatoid arthritis,
CC reperfusion injury following ischemia, growth-hormone deficiency,
CC Turner's Syndrome, Prader-Willi Syndrome, idiopathic short stature, AIDS
CC wasting, multiple sclerosis, Crohn's disease, ulcerative colitis or
CC muscular dystrophy; and improving a property of a protein. The present
CC sequence represents a polypeptide sequence which was useful during the
CC invention as a component of a BPXTEN fusion protein.
XX
SQ Sequence 12 AA;
Query Match 100.0%; Score 61; Length 12;
Best Local Similarity 100.0%;
Matches 12; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 GSEGSSGPGESS 12
||||||||||||
Db 1 GSEGSSGPGESS 12
RESULT 1 from 184.align450.rag database.
AYG93337
(NOTE: this sequence has 61 duplicates in the database searched.
See complete list at the end of this report)
ID AYG93337 standard; peptide; 12 AA.
XX
AC AYG93337;
XX
DT 30-SEP-2010 (first entry)
XX
DE XTEN sequence motif peptide SEQ ID 184.
XX
KW XTEN protein; acquired immune deficiency syndrome; anorectic;
KW antianginal; antiarthritic; antiinflammatory; cardiant;
KW cerebroprotective; coronary artery disease; crohns disease; cytostatic;
KW endocrine-gen.; extended recombinant polypeptide; factor ix deficiency;
KW factor vii deficiency; factor viii deficiency; gastrointestinal-gen.;
KW genetic-disease-gen.; glucagonoma; growth hormone deficiency;
KW growth-disorder-gen.; hypertension; hypotensive; immunostimulant;
KW immunosuppressive; ischemia; lipid metabolism disorder;
KW metabolic disorder; metabolic-gen.; multiple sclerosis;
KW muscular dystrophy; muscular-gen.; neuroprotective;
KW nutrition-disorder-gen.; ophthalmological; prader-willi syndrome;
KW protein therapy; recombinant protein; reperfusion injury;
KW retinal degeneration; rheumatoid arthritis; syndrome x; therapeutic;
KW turners syndrome; ulcerative colitis; vasotropic;
KW von willebrands disease; vulnerary.
XX
OS Unidentified.
XX
CC PN WO2010091122-A1.
XX
CC PD 12-AUG-2010.
XX
CC PF 03-FEB-2010; 2010WO-US023106.
XX
PR 03-FEB-2009; 2009US-0149669P.
PR 08-JUN-2009; 2009US-0185112P.
PR 08-JUN-2009; 2009US-0268193P.
PR 24-AUG-2009; 2009US-0236493P.
PR 25-AUG-2009; 2009US-0236836P.
PR 18-SEP-2009; 2009US-0243707P.
PR 24-SEP-2009; 2009US-0245490P.
PR 10-NOV-2009; 2009US-0280955P.
PR 10-NOV-2009; 2009US-0280956P.
PR 12-NOV-2009; 2009US-0281109P.
XX
CC PA (AMUN-) AMUNIX INC.
XX
CC PI Schellenberger V, Silverman J, Wang C, Spink B, Stemmer WP;
CC PI Geething N, To W, Cleland JL;
XX
DR WPI; 2010-K26088/55.
XX
CC PT New isolated extended recombinant polypeptide e.g. having non-repetitive
CC PT amino acid sequence, useful for treating a disease (e.g. obesity and
CC PT multiple sclerosis) and improving property (e.g. terminal half-life) of a
CC PT protein e.g. exendin-4.
XX
CC PS Claim 13; SEQ ID NO 184; 497pp; English.
XX
CC The present invention relates to a novel isolated extended recombinant
CC polypeptide (XTEN) e.g. having a non-repetitive amino acid sequence,
CC useful for treating a disease (e.g. obesity and multiple sclerosis) and
CC improving property (e.g. terminal half-life) of a protein e.g. exendin-4.
CC The invention also relates to compositions comprising extended
CC recombinant polypeptides (XTENs), isolated nucleic acids encoding the
CC compositions and vectors and host cells containing the same. XTENs are
CC generally extended length polypeptides with non-naturally occurring,
CC substantially non-repetitive sequences that are composed mainly of small
CC hydrophilic amino acids, with the sequence having a low degree or no
CC secondary or tertiary structure under physiologic conditions. XTEN
CC polypeptide compositions are useful as fusion partners that can be linked
CC to biologically active proteins (BPs), resulting in a BPXTEN fusion
CC proteins (e.g., monomeric fusions). XTENs can have utility as fusion
CC protein partners in that they can confer certain chemical and
CC pharmaceutical properties when linked to a biologically active protein to
CC a create a fusion protein. The novel composition is useful for: treating
CC glucose-related diseases, metabolic diseases, coagulation disorders, and
CC growth hormone-related disorders and conditions, such as type I or type
CC II diabetes, obesity, hyperglycemia, hyperinsulinemia, abnormal insulin
CC production, insulin resistance, syndrome X, excessive appetite,
CC insufficient satiety, glucagonoma, dyslipidemia, retinal
CC neurodegenerative processes, factor VII deficiency, factor X deficiency,
CC factor XII deficiency, hemophilia A, hemophilia B, Von Willebrand
CC disease, hypertension, acute coronary syndrome, rheumatoid arthritis,
CC reperfusion injury following ischemia, growth-hormone deficiency,
CC Turner's Syndrome, Prader-Willi Syndrome, idiopathic short stature, AIDS
CC wasting, multiple sclerosis, Crohn's disease, ulcerative colitis or
CC muscular dystrophy; and improving a property of a protein. The present
CC sequence represents a polypeptide sequence which was useful during the
CC invention as a component of a BPXTEN fusion protein.
XX
SQ Sequence 12 AA;
Query Match 100.0%; Score 61; Length 12;
Best Local Similarity 100.0%;
Matches 12; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 GSSESGSSEGGP 12
||||||||||||
Db 1 GSSESGSSEGGP 12
Claim Rejections - 35 USC § 103
8. 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.
9. Claim(s) 1-4, 8-15, 18-20, 22, 28 and 35-37 is/are rejected under 35 U.S.C. 103 as being unpatentable over Schellenberger et al., WO 2010/091122 A1 (published 12 August 2010) referenced herein as WOSchellenberger, and further in view of Schellenberger et al, US 2013/0165389 A1 (published June 27, 2013/ IDS reference A2 submitted November 26, 2025) referenced herein as USSchellenberger. WOSchellenberger a fusion protein comprising linkages between an extended recombinant polypeptide(s) (XTEN(s)), sequence motif with 12 amino acid residues a biologically active protein and a payload, see sections 0008-0010 on page 3; section 00125. “[T]he XTEN is characterized in that the sum of glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P) residues constitutes more than about…or about 90%, …of the total amino acid sequence of the XTEN,” and “…designed to be substantially non repetitive. In a preferred embodiment, XTEN sequences have predominately four to six types of amino acids selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) or proline (P) that are arranged in a substantially non-repetitive sequence that is greater than about 100 to about 3000 amino acid residues, preferably greater than 400 to about 3000 residues in length. In some embodiments, XTEN… the sequence consists of non-overlapping sequence motifs wherein each of the motifs has 9 to 36 amino acid residues wherein each of the motifs consists of 4 to 6 types of amino acids selected from glycine (G), alanine (A), serine (S), threonine (T), glutamate (E) and proline (P)”, see page 31, sections 00148 and 00149 spanning pages 31 and 32.
Biologically active proteins (BPs) XTEN are protein compositions that “…encompass fusion polypeptides that comprise one or two payload regions each comprising a biologically active protein that mediates one or more biological or therapeutic activities and at least one other region comprising at least one XTEN polypeptide.”, see page 44, section 00171.
“Examples of payloads include, but are not limited to, cytokines, enzymes, hormones and blood and growth factors. Payloads can further comprise genetically fused or chemically conjugated moieties such as chemotherapeutic agents, antiviral compounds, toxins, or contrast agents. These conjugated moieties can be joined to the rest of the polypeptide via a linker which may be cleavable or non-cleavable.”, see page 25, section 00126. The XTEN polypeptide may have multiple sites for proteolytic cleavage to release the XTEN, see page 16, sections 0079-0081; and page 44, section 00170. These sites are regarded by the Examiner as a release segment (RS) and capable of cleavage by a mammalian protease, see page 80, section 00260; and Table 10 on page 81.
“[T]he XTEN sequence consists of non-overlapping sequence motifs are from or more sequences…”, see page 4, lines 1 and 2; sections 00147- 00152 spanning pages 30-33. The sequence motifs that are the same as Applicant’s cited in Table 1 are disclosed at the end of the pending 102 rejection.
Schellenberger teaches “…pharmaceutical compositions comprising the fusion protein of any of the foregoing embodiments and at least one pharmaceutically acceptable carrier.”, see page 8, section 0038.
The fusion proteins can be designed to have different configurations, N- to C-terminus, of a [biological active protein] BP, XTEN, an option spacer sequences.”, see page 8, section 0034.
WOSchellenberger does not teach the XTEN fusion polypeptide including a tumor targeting domain. Schellenberger does not teach the cytokine is IL-12, IL-12 p35 subunit or IL-12 p40 subunit.
However, USSchellenberger teaches a fusion protein comprising a tumor targeting moiety, a tumor-associated antigen (TAA), see page 15, section 0129; and Table 2 spanning pages 15-17.
USSchellenberger teaches cytokines, “biologically active IL-12 exists as a heterodimer comprised of 2 covalently linked subunits of 35 (p35) and 40 (p40) kD, the latter being known as IL-23. IL-12 is a cytokine that is an important part of the inflammatory response, and stimulates the production of interferon-gamma (IFN-g) and tumor necrosis factor-a (TNF-a) from T and natural killer (NK) cells, and reduces IL-4 mediated suppression of IFN-g.”, see page 50, sections 0227 and 0228.
It would have been obvious to one of ordinary skill in the art at the
effective filing date of the claimed invention was made to design a therapeutic fusion polypeptide comprising biologically active proteins, additional therapeutic agents including cytokines and cleavable release segments in an arrangement conducive for in vivo treatment and packaging in a pharmaceutical composition, see both documents in their entirety.
One of ordinary skill in the art would have been motivated to do so
with a reasonable expectation of success by teachings in both references, the different molecules arranged within the fusion protein there is different molecules conferring different activities and functions “…that can be useful for enhancing the biological, pharmaceutical, safety and/or therapeutic properties of biologically active proteins [as well as] for enhancing the pharmacokinetic properties, such as half- life, and increasing the time spent within the therapeutic window of a biologically active protein, see both documents in their entireties and in particular, Summary of the Invention beginning on page 2 of WOSchellenberger; and USSchellenberger, page 40, XTEN Segments beginning at section 0159. As also taught by WOSchellenberger,”[t]he choice of configuration can, …, confer particular pharmacokinetic, physico/chemical, or pharmacologic properties.”, see page 8, section 0034.
Conclusion
10. Any inquiry concerning this communication or earlier communications from the Examiner should be directed to ALANA HARRIS DENT whose telephone number is (571)272-0831. The Examiner works a flexible schedule, however she can generally be reached 8AM-8PM, Monday through Friday.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the Examiner by telephone are unsuccessful, the examiner’s supervisor, Julie Wu can be reached at 571-272-5205. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
ALANA HARRIS DENT
Primary Examiner
Art Unit 1643
22 December 2025
/Alana Harris Dent/Primary Examiner, Art Unit 1643