DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s response and amendments received May 26, 2026 are acknowledged.
Claims 7-9, 12, 17, and 18 have been canceled.
Claims 3, 4, 10, and 11 have been amended.
Claims 1-6, 10, 11, 13-16, and 19-30 are pending in the instant application.
Claims 19-21 and 25-30 stand withdrawn from consideration as being drawn to a nonelected invention. See 37 CFR 1.142(b) and MPEP § 821.03, for reasons of record set forth in the restriction requirement mailed October 21, 2025.
Applicant’s election without traverse of the invention of group I, drawn to fusion proteins, and the species of anti-albumin Fab comprising the six CDRs of SEQ ID NOs: 35-37 and 52-54 in the reply filed on December 22, 2025 is acknowledged.
Claims 1-6, 10, 11, 13-16, and 22-24 are under examination in this office action as they read on species of anti-albumin Fab comprising the six CDRs of SEQ ID NOs: 35-37 and 52-54.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
The rejection of claims 1-6, 8, 10, 11, 13-16, and 22-24 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement has been withdrawn in view of applicant’s claim amendments received May 26, 2026.
The rejection of claims 8, 10, and 11 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement has been withdrawn in view of applicant’s claim amendments received May 26, 2026.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-5, 10, 11, 13-16, and 22-24 are rejected under 35 U.S.C. 103 as being unpatentable over Rubenstein et al. (US 2011/0177065) in view of Cha (US2016/0376350).
Rubenstein et al. disclose IL18BP fused to immunoglobulin Fc domains to extend half life when administered to patients as part of disease treatment methods (see entire document, particularly the abstract, claims, paragraphs [0013], [0078], and [0079], and most particularly claim 9). Notably, as per paragraph [0067] the term “fused protein” means IL-18BP fused with another protein to extend residence time in body fluids, with immunoglobulins being given as an example of such half-life extending proteins. Further, Rubenstein et al. disclose in paragraph [0075] that the sequence of IL-18BP is to be taken from WO99/09063 and as evidenced by the enclose sequence alignment the ‘063 WIPO publication discloses a polypeptide 100% identical to instant SEQ ID NO:7. Thus, the IL-18BP fusion proteins disclosed by Rubenstein et al. comprise instant SEQ ID NO:7. The fusion proteins of Rubenstein et al. are further disclosed as comprising linkers between the elements (see particularly paragraph [0078]) and as being present in pharmaceutical compositions and kits (see for example paragraphs [0086-0102]). Such teachings differ from what has been presently claimed in that Rubenstein et al do not disclose fusion proteins comprising antibodies or Fab fragments thereof that bind albumin.
Cha discloses that fusing a scFv that binds albumin to a molecule of interest has the advantages of extending serum half life similar to Fc domains and provides the advantage of allowing low cost expression of such fusion proteins in bacteria (see entire document, particularly the left column of page 2). In particular, Cha discloses fusions comprising the SL335 Fab which binds albumin, and that the fusion between the molecule of interest and the Fab can be made to either the N or C termini of either the heavy or light chain of the Fab (see particularly paragraph [0015] as well as Figure 4). As has been discussed earlier in this office action, the SL335 Fab comprises the CDRs of SEQ ID NOs:35-37 and 52-54, the VH of SEQ ID NO:60, the VL or SEQ ID NO:67, the heavy chain constant domain of SEQ ID NO:68, the light chain constant domain of SEQ ID NO:69, and VH-CH1 of SEQ ID NO:10, and the VL-Ck of SEQ ID NO:13 (see also enclosed sequence alignments). Pharmaceutical compositions and kits comprising such fusion proteins are disclosed (see for example paragraphs [0024-0028] as well as working examples 1-(16), 1-(18), 1-(19), 2-(3), and 2-(8)). The molecules of interest to which SL335 is joined to extend half life include a wide variety of well known biological proteins including interleukin binding proteins (see particularly paragraph [0023] as well as claims 11, 23, and 26) and working examples are disclosed concerning fusions to human growth hormone (example 1-(9)), GSCF (example 1-(10)), and IFNbeta which (example 1-(11)) comprise linker sequences between the Fab and molecule of interest (see also claim 9). Indeed, Cha et al. expressly teaches that fusion proteins utilizing his SL335 antibody are to be known as “anti-Serum Albumin Fab-Associated (SAFA) technology” and that it is to be used as a platform to develop long-acting biotherapeutics (see particularly paragraph [0030]).
Therefore, it would have been obvious to artisans to substitute the Fc in the IL18BP fusion construct of Rubenstein et al. for SL335 Fab that binds albumin as taught by Cha in order to maintain long serum half-life while gaining the advantage of lower cost production in bacterial expression systems as taught by Cha et al. Artisans would have more than a reasonable expectation of success in making such a substitution given the large number of fusion proteins to disparate biological molecules of interest as taught in the working examples of Cha and the fact that Cha explicitly teaches fusion constructs comprising interleukin binding proteins are encompassed by his invention.
Applicant's arguments filed May 26, 2026 have been fully considered but they are not persuasive. Applicant argues on many grounds. Applicant begins by stating the obvious that the IL-18BP fusion constructs of Rubenstein did not contain a Fab that binds albumin. Applicant then argues that Cha discloses “interleukin binding protein” in a long list of other potential fusion partners for the SL335 Fab, that IL-18BP is not specifically disclosed, and that based upon the working example of Cha wherein SL335 was fused to human growth hormone (HGH) the technology is too unpredictable to allow for a reasonable expectation of success. Applicant appears to believe this based upon paragraph [0015] of Cha (emphasis added by applicant)
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Applicant also argues that data collected using the fusion protein of the instant working example is different from that disclosed by Cha thereby indicating unpredictability. Lastly, applicant argues that the APB-R3 fusion protein of the working example has additional benefits as compared to IL-18BP alone, such as a need for less frequent dosing and tighter binding to IL-18. As such applicant believes the rejection would be withdrawn.
These arguments have been considered and are unpersuasive. The purpose of the fusion proteins of Rubenstein was to extend half life relative to native IL-18BP, and Rubenstein did so by joining IL-18BP to the Fc domain of an immunoglobulin. As set forth in the rejection of record, Cha discloses that the anti-albumin Fab named SL335 can be used similarly to an immunoglobulin Fc to enhace half-life in fusion proteins while also providing the advantage of lower cost bacterial production methods for fusion proteins. Thus artisans would substitute the Fc in the construct of Rubenstein for the SL335 Fab in order to gain the advantage being able to use of lower cost bacterial production methods when making fusion proteins as taught by Cha et al. With regard to the laundry list argument, artisans have long known that adding albumin binding moieties to a protein of interest can increase half life as readily demonstrated by the paragraph spanning the left and right columns of page 2 of Cha. Further, while the specific numbers obtained when comparing fusion proteins wherein SL335 is joined to either HGH (Cha) or IL-18BP (instant specification) are different as compared to the starting molecule, in all cases the measured half life was greater for the fusion protein as compared to the native protein, and given that HGH is not IL-18BP it would be extremely surprising is the numbers were identical as the half-lives of native HGH and native IL-18BP are different. Additionally, Cha discloses that it is not predictable which fusion protein format is optimal for expression, which is distinct from working at all which is what applicant’s arguments imply. Indeed, it should be pointed out that the working example of the APB-R3 construct has a very specific format (see instant Figure 2 for a graphical representation) while applicant has claimed all possible formats with regard as to where the IL-18BP is attached to the Fab as is readily evidenced by dependent claim 3. Given that applicant also owns US 9,879,077 which claims the anti-albumin Fab SL335 as part of a fusion protein with a vast array of partners including interleukin binding proteins generically wherein no particular format (i.e. structural arrangement of the components that make up the fusion protein) is recited, it perhaps good that applicant’s arguments concerning “unpredictability” are not persuasive as such arguments would serve as an admission by applicant that the full scope of the inventions claimed in the ‘077 patent are not enabled because artisans would not reasonably predict they would work (see all issued claims in the ‘077 patent, most particularly claims 7 and 10). Also, it is very well known in the art that if a biomolecule has a longer half-life it needs to be dosed less often, with such information even being explicitly explained by Cha (see particularly the right column of page 1 and the left column of page 2) and thus there is nothing unexpected or otherwise surprising by applicant’s argument that a molecule, such as APB-R3, which has a longer half life as compared to the starting native polypeptide, can be dosed less frequently than the staring native polypeptide. Finally, all claims under consideration are broader in scope than the APB-R3 construct of the working example and thus attributing its specific properties to the entire claimed genus, in the absence of additional evidence supporting such extrapolation amounts to arguing limitations not claimed. In view of all of the above none of applicant’s arguments are persuasive.
Claim 6 is rejected under 35 U.S.C. 103 as being unpatentable over Rubenstein et al. (US 2011/0177065) in view of Cha (US2016/0376350) as applied to claims 1-5, 10, 11, 13-16, and 22-24 above, and further in view of Chen et al.
The inventions rendered obvious by the combined teachings of Rubenstein et al. and Cha have been discussed above and differ from what is presently claimed in that while linker sequences are disclosed as being present in their fusion constructs, the exact linkers as recited by SEQ ID number in claim 6 do not appear to be disclosed.
Chen et al. disclose a wide variety of linkers used in fusion proteins, and teach that the sequence GGGGS is particularly attractive in linkers as it is known to increase the stability of folding as well as improve biological activity when used in fusion constructs (see entire document, most particular Table 3, and note that instant SEQ ID NO:72 is GGGGS).
Therefore, it would have been obvious to artisans to use linkers including GGGGS in fusion constructs comprising SL335 and IL-18BP in order to gain the advantages of increased stability and increased biological activity as taught by Chen et al.
Applicant's arguments filed May 26, 2026 have been fully considered but they are not persuasive. Applicant argues the base obviousness rejection is not sustainable and that its deficiencies are not rectified by the additional teachings of Chen et al.
Applicant’s arguments concerning the base obviousness rejection are not persuasive as discussed above. Given that no specific argument with regard to the teachings of Chen et al. directly have been made, the rejection is maintained for the reasons of record.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-5, 10, 11, 13-16, and 22-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 9,9879,077 in view of Rubenstein et al. (US 2011/0177065) and in view of Cha (US2016/0376350).
The issued claims of the ‘077 patent recite Fab that bind albumin as well as fusion proteins comprising said Fab, wherein the Fab has biological sequences which are identical to those as recited in the instant claims (i.e. they are those of the SL335 Fab, see enclosed sequence alignments). The claimed fusion protein are disclosed as comprising linkers (see for example claims 8 and 14) and as comprising interleukin binding proteins joined to the anti-albumin Fab (see particularly claim 10). Pharmaceutical compositions comprising fusion proteins are explicitly claimed (see issued claim 18). The issued claims differ from what is presently claimed in that the interleukin binding protein is not recited as being “interleukin-18 binding protein” and in that the location of wherein the fusion partner is joined to the anti-albumin Fab is not specified in the issued claims.
Rubenstein et al. disclose IL18BP fused to immunoglobulin Fc domains to extend half life when administered to patients as part of disease treatment methods (see entire document, particularly the abstract, claims, paragraphs [0013], [0078], and [0079], and most particularly claim 9). Notably, as per paragraph [0067] the term “fused protein” means IL-18BP fused with another protein to extend residence time in body fluids, with immunoglobulins being given as an example of such half-life extending proteins. Further, Rubenstein et al. disclose in paragraph [0075] that the sequence of IL-18BP is to be taken from WO99/09063 and as evidenced by the enclose sequence alignment the ‘063 WIPO publication discloses a polypeptide 100% identical to instant SEQ ID NO:7. Thus, the IL-18BP fusion proteins disclosed by Rubenstein et al. comprise instant SEQ ID NO:7. The fusion proteins of Rubenstein et al. are further disclosed as comprising linkers between the elements (see particularly paragraph [0078]) and as being present in pharmaceutical compositions and kits (see for example paragraphs [0086-0102]).
Cha discloses that fusing a scFv that binds albumin to a molecule of interest has the advantages of extending serum half-life similar to Fc domains and provides the advantage of allowing low cost expression of such fusion proteins in bacteria (see entire document, particularly the left column of page 2). In particular, Cha discloses fusions comprising the SL335 Fab which binds albumin, and that the fusion between the molecule of interest and the Fab can be made to either the N or C termini of either the heavy or light chain of the Fab (see particularly paragraph [0015] as well as Figure 4). As has been discussed earlier in this office action, the SL335 Fab comprises the CDRs of SEQ ID NOs:35-37 and 52-54, the VH of SEQ ID NO:60, the VL or SEQ ID NO:67, the heavy chain constant domain of SEQ ID NO:68, the light chain constant domain of SEQ ID NO:69, and VH-CH1 of SEQ ID NO:10, and the VL-Ck of SEQ ID NO:13 (see also enclosed sequence alignments). Pharmaceutical compositions and kits comprising such fusion proteins are disclosed (see for example paragraphs [0024-0028] as well as working examples 1-(16), 1-(18), 1-(19), 2-(3), and 2-(8)). The molecules of interest to which SL335 is joined to extend half-life include a wide variety of well-known biological proteins including interleukin binding proteins (see particularly paragraph [0023] as well as claims 11, 23, and 26) and working examples are disclosed concerning fusions to human growth hormone (example 1-(9)), GSCF (example 1-(10)), and IFNbeta which (example 1-(11)) comprise linker sequences between the Fab and molecule of interest (see also claim 9). Indeed, Cha et al. expressly teaches that fusion proteins utilizing his SL335 antibody are to be known as “anti-Serum Albumin Fab-Associated (SAFA) technology” and that it is to be used as a platform to develop long-acting biotherapeutics (see particularly paragraph [0030]).
Therefore, it would have been obvious to artisans to use IL-18BP as the specific interleukin binding proteins in the fusion proteins claimed in the ‘077 patent. Artisans would be motivated to do so in order to gain the advantages of maintaining long serum half-life as compared to Fc while gaining the advantage of lower cost production in bacterial expression systems as taught by Cha et al. Artisans would have more than a reasonable expectation of success in making such a substitution given the large number of fusion proteins to disparate biological molecules of interest explicitly claimed in the ‘077 patent, the number of working examples to disparate biological molecule of interest as taught by Cha., and the fact that fusion proteins of anti-albumin Fab to interleukin binding proteins generically are present in the issued claims of the ‘077 patent.
Applicant's arguments filed May 26, 2026 have been fully considered but they are not persuasive. Applicant argues that the reasons why the rejection under 103 is improper are directly applicable to the instant double patenting rejection as the application which published as the Cha reference (i.e. US2016/0376350) ultimately became the ‘077 patent.
These arguments are not persuasive as discussed above. It is perhaps worth reiterating that if applicant’s arguments concerning unpredictability were persuasive, such an arguments reasonably would be admission evidence (see MPEP 2145(I) in particular) indicating that the breadth of the claims issued in the ‘077 patent are inoperable and would need to be pulled post allowance. Luckily, such arguments have not been found to be persuasive.
Claim 6 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 9,9879,077 in view of Rubenstein et al. (US 2011/0177065) and in view of Cha (US2016/0376350) as applied to claims 1-5, 10, 11, 13-16, and 22-24 above, and further in view of Chen et al.
The obvious variations of the issued claims in view of the prior art have been discussed above and differ from what is presently claimed in that while linker sequences are disclosed as being present in their fusion constructs, the exact linkers as recited by SEQ ID number in claim 6 do not appear to be disclosed.
Chen et al. disclose a wide variety of linkers used in fusion proteins, and teach that the sequence GGGGS is particularly attractive in linkers as it is known to increase the stability of folding as well as improve biological activity when used in fusion constructs (see entire document, most particular Table 3, and note that instant SEQ ID NO:72 is GGGGS).
Therefore, it would have been obvious to artisans to use linkers including GGGGS in fusion constructs comprising SL335 and IL-18BP in order to gain the advantages of increased stability and increased biological activity as taught by Chen et al.
Applicant's arguments filed May 26, 2026 have been fully considered but they are not persuasive. Applicant argues the base nonstatutory double patenting rejection is not sustainable and that its deficiencies are not rectified by the additional teachings of Chen et al.
Applicant’s arguments concerning the base rejection are not persuasive as discussed above. Given that no specific argument with regard to the teachings of Chen et al. directly have been made, the rejection is maintained for the reasons of record.
Claims 1-5, 10, 11, 13-16, and 22-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. 10,618,953 in view of Rubenstein et al. (US 2011/0177065) and in view of Cha (US2016/0376350).
The issued claims of the ‘953 patent recite methods of increasing soluble expression in E coli (independent claims 1, 6, and 7) and increasing in vivo half-life (independent claims 8 and 11) by genetically fusing an Fab that binds albumin to a biological molecule of interest, wherein the Fab has biological sequences which are identical to those as recited in the instant claims (i.e. they are those of the SL335 Fab, see enclosed sequence alignments). The fusion proteins of the issued methods are disclosed as comprising linkers (see for example claims 9 and 12) and as comprising interleukin binding proteins joined to the anti-albumin Fab (see particularly claims 5, 10, and 13). The issued claims differ from what is presently claimed in that the interleukin binding protein is not recited as being “interleukin-18 binding protein” and in that the location of wherein the fusion partner is joined to the anti-albumin Fab is not specified in the issued claims.
Rubenstein et al. disclose IL18BP fused to immunoglobulin Fc domains to extend half life when administered to patients as part of disease treatment methods (see entire document, particularly the abstract, claims, paragraphs [0013], [0078], and [0079], and most particularly claim 9). Notably, as per paragraph [0067] the term “fused protein” means IL-18BP fused with another protein to extend residence time in body fluids, with immunoglobulins being given as an example of such half-life extending proteins. Further, Rubenstein et al. disclose in paragraph [0075] that the sequence of IL-18BP is to be taken from WO99/09063 and as evidenced by the enclose sequence alignment the ‘063 WIPO publication discloses a polypeptide 100% identical to instant SEQ ID NO:7. Thus, the IL-18BP fusion proteins disclosed by Rubenstein et al. comprise instant SEQ ID NO:7. The fusion proteins of Rubenstein et al. are further disclosed as comprising linkers between the elements (see particularly paragraph [0078]) and as being present in pharmaceutical compositions and kits (see for example paragraphs [0086-0102]).
Cha discloses that fusing a scFv that binds albumin to a molecule of interest has the advantages of extending serum half-life similar to Fc domains and provides the advantage of allowing low cost expression of such fusion proteins in bacteria (see entire document, particularly the left column of page 2). In particular, Cha discloses fusions comprising the SL335 Fab which binds albumin, and that the fusion between the molecule of interest and the Fab can be made to either the N or C termini of either the heavy or light chain of the Fab (see particularly paragraph [0015] as well as Figure 4). As has been discussed earlier in this office action, the SL335 Fab comprises the CDRs of SEQ ID NOs:35-37 and 52-54, the VH of SEQ ID NO:60, the VL or SEQ ID NO:67, the heavy chain constant domain of SEQ ID NO:68, the light chain constant domain of SEQ ID NO:69, and VH-CH1 of SEQ ID NO:10, and the VL-Ck of SEQ ID NO:13 (see also enclosed sequence alignments). Pharmaceutical compositions and kits comprising such fusion proteins are disclosed (see for example paragraphs [0024-0028] as well as working examples 1-(16), 1-(18), 1-(19), 2-(3), and 2-(8)). The molecules of interest to which SL335 is joined to extend half-life include a wide variety of well-known biological proteins including interleukin binding proteins (see particularly paragraph [0023] as well as claims 11, 23, and 26) and working examples are disclosed concerning fusions to human growth hormone (example 1-(9)), GSCF (example 1-(10)), and IFNbeta which (example 1-(11)) comprise linker sequences between the Fab and molecule of interest (see also claim 9). Indeed, Cha et al. expressly teaches that fusion proteins utilizing his SL335 antibody are to be known as “anti-Serum Albumin Fab-Associated (SAFA) technology” and that it is to be used as a platform to develop long-acting biotherapeutics (see particularly paragraph [0030]).
Therefore, it would have been obvious to artisans to use IL-18BP as the specific interleukin binding proteins in the fusion proteins recited in the methods of the ‘953 patent. Artisans would be motivated to do so in order to gain the advantages of maintaining long serum half-life as compared to Fc while gaining the advantage of lower cost production in bacterial expression systems as taught by Cha et al. Artisans would have more than a reasonable expectation of success in making such a substitution given the large number of fusion proteins to disparate biological molecules of interest explicitly recited in the ‘953 patent, the number of working examples to disparate biological molecule of interest as taught by Cha., and the fact that fusion proteins of anti-albumin Fab to interleukin binding proteins generically are present in the issued claims of the ‘953 patent.
Additionally, it is noted that the issued ‘953 claims are drawn to methods whereas the instant claims are directed to products. However, a method comprising a product always has additional limitations, and therefore is narrower in scope, that the product itself. Further, there is no restriction requirement which necessitated separation of the instant application from that which gave rise to the ‘953 patent, and indeed as evidenced by the filing receipt of 6/4/2024 in the instant application there is no relationship whatsoever between the instant application and that which gave rise to the ‘953 patent. As has been made abundantly clear in recent court decisions, including Pfizer v. Teva and Amgen Inc. v. F. Hoffman-La-Roche Ltd., “the § 121 safe harbor provision does not protect continuation applications or patents descending from only continuation applications. The statute on its face applies only to divisional applications, and a continuation application, like a continuation-in-part application, is not a divisional application.” Given that the instant application is not a divisional of the application which gave rise to the issued patent, any restriction requirements (or the lack thereof) appearing in unrelated lineages do not serve to shield the instant application and therefore the instant rejection has been set forth.
Applicant's arguments filed May 26, 2026 have been fully considered but they are not persuasive. Applicant argues that the reasons why the rejection under 103 is improper are directly applicable to the instant double patenting rejection as the application which published as the Cha reference (i.e. US2016/0376350) is the parent of the application which became the ‘953 patent.
These arguments are not persuasive as applicant’s arguments concerning the rejection under 35 USC 103 were not persuasive as discussed above. The rejection is maintained.
Claim 6 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. 10,618,953 in view of Rubenstein et al. (US 2011/0177065) and in view of Cha (US2016/0376350) as applied to claims 1-5, 8-11, 13-16, and 22-24 above, and further in view of Chen et al.
The obvious variations of the issued claims in view of the prior art have been discussed above and differ from what is presently claimed in that while linker sequences are disclosed as being present in their fusion constructs, the exact linkers as recited by SEQ ID number in claim 6 do not appear to be disclosed.
Chen et al. disclose a wide variety of linkers used in fusion proteins, and teach that the sequence GGGGS is particularly attractive in linkers as it is known to increase the stability of folding as well as improve biological activity when used in fusion constructs (see entire document, most particular Table 3, and note that instant SEQ ID NO:72 is GGGGS).
Therefore, it would have been obvious to artisans to use linkers including GGGGS in fusion constructs comprising SL335 and IL-18BP in order to gain the advantages of increased stability and increased biological activity as taught by Chen et al.
Applicant's arguments filed May 26, 2026 have been fully considered but they are not persuasive. Applicant argues the base nonstatutory double patenting rejection is not sustainable and that its deficiencies are not rectified by the additional teachings of Chen et al.
Applicant’s arguments concerning the base rejection are not persuasive as discussed above. The rejection is maintained.
A rejection based on double patenting of the “same invention” type finds its support in the language of 35 U.S.C. 101 which states that “whoever invents or discovers any new and useful process... may obtain a patent therefor...” (Emphasis added). Thus, the term “same invention,” in this context, means an invention drawn to identical subject matter. See Miller v. Eagle Mfg. Co., 151 U.S. 186 (1894); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Ockert, 245 F.2d 467, 114 USPQ 330 (CCPA 1957).
A statutory type (35 U.S.C. 101) double patenting rejection can be overcome by canceling or amending the claims that are directed to the same invention so they are no longer coextensive in scope. The filing of a terminal disclaimer cannot overcome a double patenting rejection based upon 35 U.S.C. 101.
The provisional rejection of claims 1-6, 8, 9, 15, 16, and 23 under 35 U.S.C. 101 as claiming the same invention as that of claims 1-6, 8, 9, 15, 16 and 23 of copending Application No. 18/895,157 has been withdrawn as the amendments to the instant claims made May 26. 2026 no longer make the claims (and therefore the inventions) 100% identical in scope.
The following is a new ground of rejection necessitated by applicant’s claim amendments received May 26, 2026.
Claims 1-6, 15, 16, and 23 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-6, 8, 9, 15, 16, 19-21, 23, 25-28, and 30 of copending Application No. 18/895,157. Although the claims at issue are not identical, they are not patentably distinct from each other because the copending claims recite additional limitations as compared to the instant claims.
It should be noted that the ‘157 application is a child of the instant application filed 9/24/2024, and this date predates any restriction requirement set forth in the instant application. As such the child application filed as a continuation cannot be said to have been filed in response to a restriction requirement by the USPTO.
The ‘157 application claims fusion proteins wherein a Fab that binds albumin is joined to IL-18BP, with such Fab being limited by SEQ ID number concerning their CDR sequences (see all copending claims , particularly copending claims 1, 8, and 9). Notably all possible N terminal and C terminal attachment points for the IL-18BP to the Fab are claimed (compare instant claim 3 to copending claim 3, and compare instant claim 4 to copending claim 4). The copending claims recite the same genetic linker polypeptide sequences (compare instant claim 6 to copending claim 6) and recite that their fusion proteins are present in pharmaceutical compositions (see particularly copending claim 23. Given the additional biological sequences recited in the copending claims, the copending claims are more limited that that which is presently claimed.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
No claims are allowable.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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.
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Michael Szperka
Primary Examiner
Art Unit 1641
/MICHAEL SZPERKA/Primary Examiner, Art Unit 1641
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