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 .
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 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.
DETAILED ACTION
The amendments filed on 12/23/2025 which claims 1 and 13 were amended and claims 21-24 were newly added is acknowledged. Claims x-x were canceled.
Claims 1-24 are pending in the instant application.
Priority
This application is a 371 of PCT/EP2018/075464, filed on 9/20/2018 which claims priority to the European application EP17192532.4 filed on 9/22/2017.
Election/Restriction
Applicant’s election with traverse of Group II, claims 13-18, drawn to a method of detecting an antigen comprising contacting a multivalent antibody with an antigen to form a complex, in the reply filed on 2/9/2023 remains in effect remains in effect.
Claims 1-12 and 19-20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected group, there being no allowable generic or linking claim. Election was made with traverse in the reply filed on 2/9/2023.
The traversal is on the ground(s) that Groups I and II require the same antibody and so both may be searched without serious burden. This is not found persuasive because the groups were placed in separate classifications, which is evidence on its own that there is a search burden. Further, while both groups might require the antibody, a composition requires different searching considerations than a method for use. For example, the antibody might be used for reasons other than the particular method of Group II.
claims 13-18
Claims 13-18 and 21-24 are examined herein.
Claim Rejections – 35 USC § 103
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.
claim 1, 13-14, 17-18
Claim(s) 13, 14, 17-18, 21-24 are rejected under 35 U.S.C. 103 as being unpatentable over Miller (WO 01/77342; IDS 10/20/20 citation 7) in view of Rossi (IDS 10/20/20 citation 44) and further in view of Sias (form 892), Konterman (doi: 10.1111/j.1745-7254.2005.00008.x), Hansen (US7951921), and Song (US9164105). This rejection has been modified solely to address the amendments.
Regarding claim 13, Miller discloses figure 4b:
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Regarding claim 1, Miller teaches:
a chimeric or non-chimeric antibody: the molecule in figure 4b is an antibody. Since chimeric or non-chimeric covers all possibilities, the above antibody must be one or the other. Further, Miller teaches chimeric is one option for the antibody (p.25 L19).
a multivalent antibody: each VH/VL in the above figure is a binding site. As there is more than one, the antibody is multivalent. See also Miller p.32 L4-7.
a recombinant antibody: Miller teaches the antibody may be made using recombinant DNA (p.48 L16), indicating the resulting antibody is also recombinant. See also Miller p.59 L115-16.
a monospecific antibody, wherein the antibody has specificity for only one antigen p.42 L35-38.
comprising p=4 light chain Fabs: These are the VL/CL portions on the two arms, with two on each arm. It is recognized that this is not one of the values claimed (6, 8, or 10); this is addressed by the combination of Rossi discussed below.
a dimer of two heavy chains: VH->CH3 is one heavy chain, there are two of them, and they are connected via the indicated dimerization bond in the figure. See also Miller p.80 example 5 indicating the heavy chains dimerize.
Each heavy chain has the formula FabH-L-FabH-L-dd(FcH): The topmost VH/CH1 is the first FabH, the line represents the linker, the other VH/CH1 on the same chain is the second FabH, the next line is the linker, and the dimerized CH2/CH3 meets the limitations of a dd(FcH) as there clearly must be a dimerization domain if the two dimerize.
N = 1: the topmost VH/CH1 is n, whereas the second is the non-variable FabH in instant formula I.
The bonds are covalent: Miller teaches the polypeptide chain is joined by peptide bonds (p.30 L25-26), which are covalent bonds.
Where L is present, it is a variable linker amino acid sequence: Miller teaches the antigen binding sites (Fabs) are joined by flexible linkers, which refers to “two or more” (variable) amino acids (p.30 L27-33). Two examples—AS and GGGS—further support the conclusion that these linkers may vary in both length and sequence and are made of amino acids.
Each dd(FcH) is a heavy chain dimerization region of a heavy chain of a non-antigen binding immunoglobulin region: The CH2 in the above figure is part of the constant region, i.e., part of the non-antigen binding region. This is also dimerized as discussed above, indicating the presence of a dimerization region. CH2 is part of the heavy chain, meeting the limitations of being part of the heavy chain. See also Miller p.30 beginning at line 34 for further support of this limitation.
The dimer of two dd(FcH) are aligned with each other in physical proximity: as clear from the figure above, these two regions are aligned. As they are bound to one another, they must also be in physical proximity.
Each FabH is selected from one of Formulae II, III, IV, or V: as seen in the above figure, each FabH is of the formula VH-CH1, which meets the criteria for formula II. This arrangement is allowed at least by independently selecting each FabH to be AH, and then independently selecting AH to be formula II. It is noted that the claimed definitions of VH, VL, CH1, and CL are the ordinary definition in the antibody arts and have the same definition in Miller.
Each FabL is selected from one of Formulae VI, VII, VIII, or IX: as seen in the above figure, each FabL is of the formula VL-CL, which meets the criteria for formula VII. This arrangement is allowed at least by independently selecting each FabL to be AL, and then independently selecting AL to be formula VII. It is noted that the claimed definitions of VH, VL, CH1, and CL are the ordinary definition in the antibody arts and have the same definition in Miller.
Each antigen binding site FabH:FabL is an aligned pair of the form [VH-CH1]H:[VL-CL]L: as seen in the above figure, each VH is aligned with a VL and each CH1 is aligned with a CL.
Wherein for each aligned pair, CL and CH1 are covalently linked via disulfide bond: as seen in the figure, each CL/CH1 is connected by a line. See also Miller p.1 L11-13, noting that disulfide bonds between the heavy and light chain is natural, with the line in the figure representing the only bond between the heavy/light chain. See also the description of figure 1 at page 16 establishing that the lines are disulfide bonds when they are between the CL/CH1 domains.
Because “ddFcH” is defined as any dimer of two heavy chain polypeptides that lack an antigen binding region, the Fc region of Miller satisfies the claim limitations. In the figure above, both all FabH portions are connected to this Fc region, a type of ddFcH according to the definition supplied, via a covalent linker; thus meeting the limitation of the “FabH polypeptides connect to the ddFcH”.
Because a “FabH” is defined as a VH-CH1 unit, a VL-CL unit, a VH-CL unit, or a VL-CH1 unit, the structure of Miller effectively teaches eight different “FabH” units as described. Thus meeting the limitation of comprising “three or more FabH polypeptides”.
Miller teaches the multivalent antibody immobilized and contacted with a sample containing the antigen in order to form a complex (p.68 section F). Miller teaches using the antibody to detect the antigen (p.68 section F). Miller teaches the antibody is labeled (p.68 section F). Miller teaches washing the immobilized antibody:antigen complex to remove non-complex material (p.68 section F). Furthermore, p.5 L18-21 establishes a reasonable teaching that the arrangement in Miller is according to the ordinary arrangement whereby the antigen binding region is the N-terminus and the CH3 is the C-terminus, establishing that the parts are in the correct orientation as claimed; see also Miller p.13-14.
Miller does not teach the L-Fab which is C-terminal to the FcH dimerization domain.
Rossi provides figure 3. While 3e is replicated below, 3b is also relevant:
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This antibody has six light chain VLs, two of which are Fabs (VLb/CL and VLc/CL). There are also two heavy chains of the formula FabH-FabH-ddFcH-FabH, excepting that the first “Fab” is only a Vh and lacks the associated CH1 region.
Konterman teaches the generation di-diabodies that are fused to the CH3 region of the Fc domain using recombinant techniques (Fig 1; pg 3, col 1, para 2; pg 3, col 2, para 3).
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Konterman teaches such single-chain diabodies (scDb) can also be used to a full Fc region and not just the CH3 domain of the Fc region (pg 5, col 1, para 4). Konterman teaches “The advantage of using single-chain diabodies for this approach is that a single polypeptide chain is expressed resulting in the assembly of defined molecules with identical size and binding activity” (pg 5, col 2, para 1). Konterman teaches that such single-chain antibodies exhibit high levels of expression and long in vivo half-lives (pg 6, col 1, para 1). Konterman teaches single-chain diabodies can be advantageously produced by bacteria as opposed to mammalian expression systems (pg 3, para 3). Konterman teaches that single-chain diabodies are more stable and possess greater activity than normal diabodies and tandem scFv molecules (pg 5, col 1, para 2).
Hansen teaches a multispecific antibody comprising a first and second arm, wherein the second arm is fused to the C-terminus of the CH3 domain an IgG antibody via peptide bond, shown below (Fig 1; col 5, lines 8-41; col 7-8, lines 63-11). Hansen teaches their antibodies may be used to treat cancer or used to diagnose/detect cancer in a subject (col 9, para 2-3). Hansen teaches the antibodies may comprise a detectable label (col 9, para 3). Hansen teaches their multispecific antibodies exhibit increased affinity, high stability in vitro/vivo, and preferred pharmacokinetics (col 1, para 2). Hansen teaches the additional binding sites improve target affinity, providing more effective delivery of the bioactive agent (col 20, para 2). Hansen teaches their antibodies were generated using recombinant techniques (col 66, para 7-8).
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It would have been obvious to modify the antibody of Miller to add the C-terminal Fab of Rossi, using the peptide bond linker of Konterman or Hansen because (i) Rossi and Konterman teach the C-terminal CH3 domain can accommodate a Fab; (ii) Konterman teaches the Fab can be linked to the CH3 domain using a peptide bond; and (iii) Hansen teaches that the C-terminal CH3 domain of IgG antibodies can also accommodate an additional binding arm. As shown by the references, recombinant antibody structures are highly modular. Both Miller and Rossi are concerned with using multiple Fabs to create multivalent antibodies and do so in similar ways. Rossi teaches the additional C-terminal Fab remains fully functional and increases binding affinity (p.477 C2-478C1) and so adding this additional Fab represents combining known structures in known ways to achieve predictable results. Hansen echoes this finding, noting that increasing the number of binding arms increases the affinity. Further, Rossi teaches the combinations as modular (p.477-478), which would have made it obvious to the person of ordinary skill in the art that only one of the two C-terminal Fabs in figure 3 need be added and that this represents a predictable, obvious variation. By adding this C-terminal Fab, using the same covalent disulfide bonds and linkers taught by Miller for the relevant domains, a construct is arrived at meeting all of the limitations of the instantly claimed construct, including where p=6, m=1, and n=1, such that p=(2+2*(n+m)). Note that Rossi uses the same VH-CH1:VL-CL alignment as Miller does. The addition of Konterman underlines the capability of attaching a Fab also to the CH3 domain using recombinant techniques, in order to generating a single-chain diabody that is both highly expressed and physiologically more active. This peptide bond linkage is echoed by Hansen who uses it to attach an scFv to an IgG antibody.
It would have been obvious to utilize this in a method for detecting an antigen. Miller teaches the antibody binds (forms a complex) with the target antigen as discussed above. Miller also teaches the antibody binds the target antigen (p.478 C1). Thus, it would have been obvious to use the construct arrived at by combining Miller and Rossi to contact the antigen (taught by both Miller and Rossi), thereby forming a complex (Miller), and detecting said complex (see Miller’s discussion of adding a detectable label to the antibody (p.68 part F).
Regarding claim 14, Miller also teaches mixing the multivalent antibody with a sample suspected of containing the antigen and determining the binding of the antibody to the sample (p.15 L34-37). Binding meets the limitations of forming a complex (step b) while the mixing meets the limitations of step a. Miller teaches the antibody functions in liquid (e.g., example 2) which would have made it obvious to one of ordinary skill in the art that the suspected sample could be a liquid sample with an expectation of achieving predictable success. Miller teaches this method for “determining the presence of the antigen”, requiring that this complex is then detected in some way, meeting the limitations of step c. Further, Miller teaches the antibody may be labeled as above, making obvious this detection step.
Regarding claims 17 and 18, Miller teaches a 96-well plate (a solid phase) coated with HER2 extracellular domain according to Sias (example 2). Note that per Sias, these samples containing HER2 are liquid samples (p.74). Thus, the solid phase was capable of capturing the antigen and, prior to any of the steps in claim 17, this liquid sample known to contain—and therefore clearly suspected of containing—the antigen was contacted with the solid phase, whereby the antigen was captured by the solid phase. Miller then teaches the antibody was incubated (which requires the antibody was first added) to the solid phase comprising the antigen on its surface (example 2); it would have been an obvious variation to have the antibody itself labeled rather than using a secondary detection antibody because Miller explicitly teaches the antibody may be labeled as noted above. Miller then teaches washing the “unbound” antibody, both meeting the limitations of step c as well as indicating that other antibodies bound the antibody forming a complex. In Miller, the secondary antibody is used to detect and visualize the well, though this detection would have been obvious to perform on the labeled antibody as described above for the same reasons. Note that Sias teaches essentially the same process
Therefore, claims 13, 14, 17, and 18 would have been obvious.
*Claim 21
Regarding claim 21, Miller teaches their antibodies can comprise a detectable label (pg 39, para 2) such as a radioisotope, fluorescent label, or chromogenic substrates (pg 68, para 3-6).
*Claim 22-23
Regarding claims 22-23, Miller is silent on the label being a ruthenium complex.
Song teaches a diagnostic kit for detecting pancreatic cancer comprising an immobilized antibody and a label-conjugated secondary antibody (col 7, para 2-3). Song teaches the label may be a ruthenium complex, such as [Ru(bpy)3]2+ (col 8, para 1).
It would have been obvious to modify the antibody of Miller to comprise a ruthenium label because Miller teaches their antibodies can accommodate a luminescent label and Song teaches that ruthenium complexes are an exemplary luminescent label that can be conjugated to antibodies as part of a method of detecting cancer cells. One of skill in the art would have had a reasonable expectation of success because both references teach that antibodies are amenable to appended labels to permit the detection of an antigen within a sample.
*Claim 24
Regarding claim 24, variables m and n have been previously discussed in the rejection of claims 1, 13-14, and 17-18, above. To reiterate, Miller provides the first half of the formula 1: (VH-CH1)1-(VH-CH1)-Fc, thus satisfying instant variable n being 1. Miller also provides two light chain FabL of (VL-CL)-(VL-CL). Rossi provides the second half of formula 1 being: Fc-(VH-CH1)1, thus satisfying instant variable m being 1. Rossi also provides one light chain FabL of (VL-CL). The further criteria of requiring a peptide bond between the C-terminus of the Fc domain and the (VH-CH1) unit, is supplied by Konterman and Hansen.
claim 13-14, 17-18
Claim(s) 13-14, 17, and 18 is/are rejected under 35 U.S.C. 103 as being unpatentable over Miller (WO 01/77342; IDS 10/20/20 citation 7) in view of Rossi (IDS 10/20/20 citation 44) and further in view of Kemeny (Wo1988004430; form 892), and Konterman (doi: 10.1111/j.1745-7254.2005.00008.x).
The teachings of Miller, Rossi, and Konterman as well as the reasons for their combination are discussed above and incorporated herein. In addition to those teachings, Kemeny teaches a method of immunoassay, similar to the disclosure of Miller using antibodies for detection (immunoassay). Kemeny teaches (claim 1) contacting a sample liquid containing an analyte (liquid sample suspected of containing the antigen) with an absorbent carrier with an immobilized binding material (a solid phase capable of capturing the antigen) wherein the analyte is bound to the material, followed by contacting the bound analyte with a labelled indicator, removing the unbound indicator (washing) and then detecting the bound (complexed) indicator. This meets all of the limitations of instant claims 17-18 where it would have been obvious that the “labeled indicator” of Kemeny could be predictably substituted with the labeled antibody of Miller/Rossi because they are both labeled for the purpose of binding a target and then detecting the presence/levels of those targets. Note further that Kemeny teaches these labeled indicators can be antibodies (p.2, 9).
Therefore, claims 13, 14, 17, and 18 would have been obvious.
claim 13-16
Claim(s) 13-16 is/are rejected under 35 U.S.C. 103 as being unpatentable over Miller (WO 01/77342; IDS 10/20/20 citation 7) in view of Rossi (IDS 10/20/20 citation 44) and further in view of Whitman (US 20160032373; form 892), and Konterman (doi: 10.1111/j.1745-7254.2005.00008.x).
The teachings of Miller, Rossi, and Konterman as well as the reasons for their combination are discussed above and incorporated herein. In addition to those teachings, Whitman teaches a method of immunoassay, similar to the disclosure of Miller using antibodies for detection (immunoassay). In claim 38, Whitman teaches a method of detecting a target molecule by forming a complex between a capture antibody, target molecule if present (antigen), and detection antibody. Whitman teaches the sample containing the suspected target may be a liquid sample (paragraph 24). This meets the limitations of claim 15 step a. This meets the limitations of claim 16 step a where the antibody is labeled as taught by Miller and include being the labeled detection antibody of Whitman. Whitman teaches in claim 38 that this contacting results in the formation of a complex (instant claims 15/16 step b). Whitman in claim 38 teaches that, subsequent to this step, a magnetic field is used “in order to immobilize the…complex”, meeting the limitations of step c in both instant claims 15 and 16. Finally, Whitman in claim 38 teaches the final step is detecting the target molecule, meeting the limitations of step d.
It would have been obvious to combine the reference because Miller and Whitman are generally concerned with detecting target antigens using antibodies. Whitman presents a method of doing so and one could have predictably adapted this method to utilize the Miller/Rossi antibody.
Therefore, claims 13-16 would have been obvious.
Response to Arguments
Applicant’s arguments filed on 12/23/2025 have been fully considered but they are not persuasive.
103; pg 10, para 5
Applicant argues the amendments to claim 1, regarding “-“ being a peptide bond, excludes the teachings of Rossi and the other references fail to address this deficiency.
In their analysis, Applicant has neglected the teachings of Konterman which fuse a single chain diabody to the C-terminus of a CH3 domain using a peptide bond. To substantiate the rejection regarding the newly added limitation of requiring peptide bonds, the reference of Hansen has been added to show that recombinant techniques can also be used to fuse a second binding domain to the C-terminal end of the CH3 domain of an IgG antibody, wherein said fusion is via peptide bond formation and not via the dock-and-lock system of Rossi.
103; pg 12, para 2
Applicant argues that the reference of Rossi uses the dock-and-lock system as opposed to the peptide bond instantly claimed. Applicant argues that Konterman teaches fusing single-chain diabodies and not full Fab fragments and also fails to teach the complete antibody region of the IgG (i.e. the VH-CH1-CH2-CH3 heavy chain and the VL-CL light chain).
This argument was addressed above. It is noted that Hansen teaches fusing a second binding domain to the C-terminal end of an IgG.
103; pg 13, para 5
Applicant argues there is no motivation to combine the references. Applicant argues that Rossi’s dock-and-lock method teaches away from the instantly claimed method of using recombinant techniques. Applicant argues impermissible hindsight was used in formulating the rejection.
Because applicant’s formula does not require specificity, the dock-and-lock technology that permits such specificity is not a required or claimed feature of the instant invention, thus this property of Rossi’s method fails to constitute a teaching away. Rossi’s teaching regarding the control over which particular binding domains are combined and where they are located, is not a requirement of the instant invention, as the instant invention is ambivalent towards what epitopes the binding domains bind and their location. In essence, Rossi exemplifies a specific embodiment of the instant invention (e.g. where specificity is desired), whereas the instant invention as a whole is also drawn to multivalent antibody structures that lack this specificity and the ease of generating combinatorial libraries. When faced with the generation of the generic antibodies of instant Formula I, one of skill in the art would prefer to use recombinant techniques because it requires the isolation of a single recombinant product, whereas the dock-and-lock technique requires the synthesis of the two-part DNL domain and the fusion of an anchor domain to the IgG, followed by combination step to generate the product.
In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971). The teachings of Konterman and Hansen clearly show that it was known in the prior art that conjugation to the CH3 domain of an antibody could be performed using recombinant techniques, thus forming a peptide bond adjoining these two units.
103; pg 14, para 3
Applicant argues that Rossi uses a modular system to avoid the challenges of generating separate specific recombinant antibodies.
This argument was not found convincing because the instant claims are drawn to a generic structure that obviates the technical challenges posed by selecting what fragments need to be fused. For example, Formula (I) is sufficiently generic, encompassing any multivalent antibody including those that entirely lack a VH region and CH1 region. Formula (I) also includes substantial latitude in the linker sequences, which can be composed of any amino acid sequence of any length. Because the claims are drawn to substantial variation in the combination of parts, selective synthetic outcomes are not required by the instantly claimed formula. Applicant is not particular on which domains bind what, where they are located, or even the identity of their most generic design (e.g. VH-CH1 versus VL-CH1 domains). In other words, applicant’s formula does not promise specificity or selectivity, thus arguments regarding a person of skill in the art preferring the selectivity of Rossi’s system were found unsubstantiated given the instant formula does not require such a technical feature. Absent that requirement for specificity, one of skill in the art would prefer the simpler recombinant method over that of Rossi.
103; pg 15, para 2
Applicant argues new claims 21-24 which contain a ruthenium label constitute a new invention. Applicant argues that the former rejection does not address these newly added limitations.
This has been addressed by the inclusion of the reference of Song.
Conclusion
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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/L.A.E./
Examiner, Art Unit 1675
/JEFFREY STUCKER/Supervisory Patent Examiner, Art Unit 1675
Prosecution Insights