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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 17 Nov 2025 has been entered.
Claim Status
The amended claim set filed 17 Nov 2025 is acknowledged. Claims 38, 45-48, and 50-58 are currently pending. Of those, claim 38 is currently amended, and claim 58 is new. Claims 54-56 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 11 Dec 2024. Claims 1-37, 39-44, 49 are cancelled. Claims 38, 45-48, 50-53, and 57-58 will be examined on the merits herein.
Response to Arguments
The Applicants’ arguments filed 17 Nov 2025 are acknowledged. For clarity, in this action, said arguments will be referred to as “Remarks” and the Non-Final Office Action mailed 27 Jan 2025 will be referred to as “NFOA” and the Final Office Action mailed 17 July 2025 will be referred to as “FOA”.
Rejection(s) Maintained
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claim Rejections - 35 USC § 103
Claims 38, 45-48, 50-53, and 57 remain rejected and claim 58 is newly rejected under 35 U.S.C. 103 as being unpatentable over Uppuluri et al. (2018; hereafter Uppuluri; made of record in IDS filed 1 Sep 2021) in view of Gow et al. (US-20180037640-A1, published 8 Feb 2018; hereafter Gow; PTO-892), Wang-Lin et al. (2018; hereafter Wang-Lin; PTO-892), and Janeway (2001; PTO-892). The rejection is copied here and updated to reflect the claim amendments; a response to applicant’s arguments follows the rejection.
Regarding claims 38 and 45-46, Uppuluri teaches raising antibodies against recombinant peptides from the N-terminus of the Candida albicans Hyr1 protein (referred to as rHyr1p-N, Abstract), and teaches that the Hyr1 protein’s structure is strikingly similar to the outer membrane protein FhaB protein of Acinetobacter baumannii (pg. 3 par. 2-3, Figure 1). Uppuluri teaches that rabbit polyclonal antibodies raised against the Hyr1 peptides specifically bind to A. baumannii in vitro (pg. 4 col. 1, Figure 2). Uppuluri further teaches a method of passively immunizing subjects (mice) using pooled, polyclonal IgG raised against Hyr1p-N; administration of these antibodies was effective both as a prophylaxis to protect against future A. baumannii infection (pg. 9 par. 2-3, Figure 5C-D) and as a treatment to resolve existing A. baumannii infection (pg. 9 par. 4, Figure 5E). Uppuluri confirms that the therapeutic effect is specific to A. baumannii infection and does not protect mice from Pseudomonas aeruginosa infection (pg. 9 par. 2, Figure 5C). “These low doses of curative antibodies confirm their specific protection mechanism and their translational potential as a novel treatment for A. baumannii bacteremia and pneumonia in different hosts (diabetics and neutropenics).” (pg. 9 par. 4).
Regarding claim 48, Uppuluri teaches using whole IgG antibodies in the passive immunization method(pg. 9 col. 2).
Regarding claims 52 and 57, Uppuluri teaches that the anti-Hyr1 antiserum increases susceptibility to both imipenem (a carbapenem) and colistin (a polymyxin). “When the antibodies were combined with serial dilutions of imipenem, we observed a significant synergistic effect in which the IC50 was reduced from 32 to 4 μl/ml (Fig 8A). A modest but additive effect was observed with antisera combined with colistin, lowering the IC50 to 0.5 or 1.0 μg/ml when compared to either colistin or the anti-peptide serum alone (Fig 8B). Control pre-vaccinated serum at the identical dilution did not produce this inhibition effect. … Clear and significant synergistic effect was noticed in killing A. baumannii when the anti-peptide serum was combined with the sub-inhibitory colistin concentrations especially after 24 h of incubation resulting in 50-90% reduction of bacterial count when compared to colistin or anti-peptide serum alone with the highest effect seen with serum combined with the 0.5 MIC colistin (S3 Fig).” (pg. 12 par. 2). The polyclonal antibody is also synergistic with colistin in the A. baumannii/C. albicans mixed-species biofilms that are commonly seen in patients (pg. 12 par. 3).
Regarding claim 53, Uppuluri teaches the treatment experiment was performed in immunosuppressed, neutropenic subjects (pg. 9 par. 4).
Regarding claim 38, Uppuluri teaches administration of the antibodies to the subject via injection (Figure 5 legend).
Uppuluri does not teach the specific human anti-Candida antibody having CDRs with SEQ ID NOs: 53, 55, 57, 60, 62, and 64, as in claim 38. Uppuluri also does not teach the antibody has the framework domain sequences or VH and VL sequences in claims 39-44. Uppuluri does not teach intravenous administration of the antibody as in claim 58.
Regarding claims 38, Gow teaches recombinant, fully human IgG1 monoclonal antibodies made by single B cell cloning [Example 1, 0191-0193] that bind to the N-terminus of the Hyr1 protein [0194]. These antibodies are listed in Table S3 [0193, excerpt copied below], and include AB-123. By inspection, the CDRs of AB-123 are identical to SEQ ID NOs: 53, 55, 57 (Table VH, see below, and instant Tables VH and F), and SEQ ID NOs: 60, 62, and 64 (Table VL, see below, and instant Tables VL and F). Also, by inspection, the framework domains and VH and VL domains as a whole are identical to those in instant Tables VH and VL (compare to instant Tables VH, VL, and F), so the full heavy and light chain sequences of Gow are identical to instant SEQ ID NOs: 5 AND 9, respectively. Also, in the interest of compact prosecution, it is noted that Gow also teaches the other, non-elected HCDR and LCDR sequences in claim 38, which are referred to as AB-120, AB-121, and AB-122 in both the instant specification (Tables C-E) and in Gow (Tables VH and VL).
Regarding claims 38, 47, and 51, MPEP 2112.01 states that "Products of identical chemical composition can not have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id. The Gow antibody’s variable domain has an identical sequence to the instant AB123 antibody, so it necessarily has the same binding and opsonization properties. The instant specification provides evidence that AB123 binds the antigen with EC50 of 53.3 ng/mL [0223] (i.e. 1 to 1500 ng/mL) and that the antibodies opsonize A. baumanii [Example 6 at 0230, Figure 6], and that the antibodies can be used to treat an A. baumanii infection in an individual [Example 7 at 0231, Figure 7]. Further, it was known in the art at the time of filing that opsonization requires interactions between the IgG antibody’s constant (Fc) region and the phagocyte’s Fc receptor (Janeway Figure 9.32), and Gow teaches that the purified recombinant monoclonal antibodies opsonize the antigen C. albicans; the antibody-coated fungal cells are taken up more rapidly than saline-treated or control IgG-treated cells [Example 4, 0203]. Gow’s demonstration that the claimed antibody opsonizes C. albicans [0203] provides independent evidence that the claimed antibody has all structures required for opsonizing bound antigens.
Excerpt from Gow Table S3, pg. 48. AB-123 is an antibody raised against the Hyr1 protein.
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Excerpt from Gow Table VH, pg. 49. The sequence of 06-AB-123 is identical to the elected antibody species.
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Excerpt from Gow Table VL, pg. 50. The sequence of 06-AB-123 is identical to the elected antibody species.
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Regarding claim 48, Gow teaches the antibody may be a whole antibody, such as IgG [0024].
Regarding claim 50, the antibody may be conjugated to a toxic payload (e.g. ricin) [0081]. The instant specification provides evidence that ricin is a payload that is cytotoxic to Acinetobacter [instant 0106].
Regarding claim 53, the antibody can be administered to immunosuppressed patients [0095].
Regarding claim 58, Gow teaches that the antibody can be administered by injection such as intra-venous administration [0103]. Gow also teaches that “Those of relevant skill in the art are well able to prepare suitable solutions” [0103].
Also, Wang-Lin is a reference of the field of antibody therapies for bacterial infections at the time of filing, and teaches the level of background knowledge available to one of ordinary skill in the art at the time of filing. Wang-Lin teaches that “treatment with polyclonal antisera poses several drawbacks, including “serum sickness” or immune complex hypersensitivity that can occur in 10–50% patients, lot-to-lot variation in efficacy, low content of specific antibodies, and potential hazards in the transmission of infectious diseases” (pg. 1 Introduction). Wang-Lin also teaches that monoclonal antibodies have the advantages of being unlikely to exhibit cross-resistance with small-molecule antimicrobial drugs, having long half-lives to allow convenient dosing (Abstract), advances in hybridoma technology allow production of unlimited amounts of human mAbs, and mAbs are currently widely used to treat a variety of diseases. (pg. 2 par. 2). Also, monoclonal antibodies do not have a low content of specific antibodies like polyclonal antibodies, because all antibodies in the preparation are the specific antibody, and do not have infection transmission risks like polyclonal antibodies, because they are made from hybridomas rather isolated than from another subject.
One of ordinary skill in the art at the time of filing would consider it prima facie obvious to improve the Uppuluri method of passive anti-Hyr1 immunotherapy for treating Acinetobacter infections by using the anti-Hyr1 monoclonal antibodies of Gow, thereby arriving at the claimed invention, because using a monoclonal antibody of Gow instead of the polyclonal antibody of Uppuluri would have the well-known advantages of monoclonal antibodies taught by Wang-Lin. Additionally, using a human monoclonal antibody instead of a non-human polyclonal antibody would reduce the risk of a human subject’s immune system reacting against the antibodies. Therefore the combination would be desirable because these benefits would potentially increase the therapeutic efficacy. See MPEP 2144(II): “The strongest rationale for combining references is a recognition, expressly or impliedly in the prior art … that some advantage or expected beneficial result would have been produced by their combination.”
The person of ordinary skill would have a reasonable expectation of success because both the polyclonal antibody of Uppuluri and the monoclonal antibody of Gow bind to the same antigen: the N-terminal region of the C. albicans Hyr1 protein (Uppuluri Abstract, Gow par. 0194), and are IgG antibodies (Uppuluri pg. 9 par. 2 and 4, Gow par. 0193].
Additionally, KSR International Co. v. Teleflex Inc., 127 S. Ct. 1727, 1741 (2007), discloses that the simple substitution of one known element for another to obtain predictable results is obvious unless its application is beyond that person's skill. KSR International Co. v. Teleflex Inc., 127 S. Ct. 1727, 1741 (2007) also discloses that "the combination of familiar elements according to known methods is likely to be obvious when it does no more than yield predictable results". In the instant case, the prior art (Uppuluri) teaches a method that only differs from the claimed invention by the substitution of a single component (i.e. substitution of the anti-Hyr1 antibody used); the substituted element (i.e. the specific monoclonal anti-Hyr1 antibody) was already known and already shown to function as an anti-Hyr1 antibody, therefore no change in the function of the substituted element occurred; and one of ordinary skill in the art would be capable of substituting one IgG antibody for another that binds to the same target with a reasonable expectation of success (i.e. the substitution of the element would lead to predictable results). Therefore, the claimed invention is prima facie obvious in view of the teachings of the prior art, absent any convincing evidence to the contrary.
As an additional optional modification, one of ordinary skill in the art at the time of filing would consider it prima facie obvious to improve the Uppuluri method of passive anti-Hyr1 immunotherapy for treating Acinetobacter infections by administering the Gow antibodies intravenously, thereby arriving at the invention of claim 58, because Gow teaches administering the monoclonal antibodies intravenously and specifically states that “Those of relevant skill in the art are well able”[0103, emphasis added] to administer the antibody in this manner. KSR International Co. v. Teleflex Inc., 127 S. Ct. 1727, 1741 (2007), discloses that combining prior art elements according to known methods to yield predictable results, is obvious unless its application is beyond that person's skill. KSR International Co. v. Teleflex Inc., 127 S. Ct. 1727, 1741 (2007) also discloses that the combination of familiar elements according to known methods is likely to be obvious when it does no more than yield predictable results. Gow specifically discloses that this administration route for the antibody is a familiar element that can be used by one of ordinary skill in the art. Therefore, the claimed invention is prima facie obvious in view of the teachings of the prior art, absent any convincing evidence to the contrary.
Response to Arguments
Applicant argues (Remarks pg. 8) that there is no reasonable expectation of success for treating Acinetobacter infection based on the teachings of Uppuluri, Gow, Wang-Lin, and Janeway.
This argument has been carefully considered but is not found persuasive. The statement of treating Acinetobacter infection is found in the preamble and is an intended use of the administering step. See MPEP 2111.02: “If the body of a claim fully and intrinsically sets forth all of the limitations of the claimed invention, and the preamble merely states, for example, the purpose or intended use of the invention, rather than any distinct definition of any of the claimed invention’s limitations, then the preamble is not considered a limitation and is of no significance to claim construction. Shoes by Firebug LLC v. Stride Rite Children’s Grp., LLC, 962 F.3d 1362, 2020 USPQ2d 10701 (Fed. Cir. 2020)… To satisfy an intended use limitation which is limiting, a prior art structure which is capable of performing the intended use as recited in the preamble meets the claim. See, e.g., In re Schreiber, 128 F.3d 1473, 1477, 44 USPQ2d 1429, 1431 (Fed. Cir. 1997)”. The body of the method has one step that states that the antibody is administered “to an individual in need thereof” (i.e. the claim references back to the preamble to limit the subject population to those in need to treatment for Acinetobacter infections).
However, other than this limitation to the subject population, the broadest reasonable interpretation is that the “treating” statement is only an intended use and therefore does not limit the administration step. This interpretation is supported by the instant specification not clearly defining limits on administration steps that are not capable of treating Acinetobacter infections, such as defining that administration steps for treating only include certain dosages, routes, etc. Instead, the instant specification teaches that treatment with either AB120, AB121, AB122 or AB123 protects against A. baumanii infection [Example 6 at 0230], and there is insufficient evidence of record to show that treatment is not an inherent property of the elected antibody structure when it is administered “to an individual in need thereof”.
In contrast to applicant’s assertion that there is not a reasonable expectation of success, the examiner’s position is that treating Acinetobacter is a property that inherently results from the combination of the antibody structure of Gow and the choice to administer anti-Hyr1 antibodies to subjects with Acinetobacter infections as taught by Uppuluri. See MPEP 2145.II: “Mere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention. In re Wiseman, 596 F.2d 1019, 201 USPQ 658 (CCPA 1979) (Claims were directed to grooved carbon disc brakes wherein the grooves were provided to vent steam or vapor during a braking action. A prior art reference taught noncarbon disc brakes which were grooved for the purpose of cooling the faces of the braking members and eliminating dust. The court held the prior art references when combined would overcome the problems of dust and overheating solved by the prior art and would inherently overcome the steam or vapor cause of the problem relied upon for patentability by applicants. Granting a patent on the discovery of an unknown but inherent function (here venting steam or vapor) "would remove from the public that which is in the public domain by virtue of its inclusion in, or obviousness from, the prior art." 596 F.2d at 1022, 201 USPQ at 661.)… "The fact that appellant has recognized another advantage which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious." Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985) (The prior art taught combustion fluid analyzers which used labyrinth heaters to maintain the samples at a uniform temperature. Although appellant showed that an unexpectedly shorter response time was obtained when a labyrinth heater was employed, the Board held this advantage would flow naturally from following the suggestion of the prior art.).” In this case, as in Wiseman and Obiaya, the property of the specific monoclonal antibody being capable of treating Acinetobacter infection flows naturally from the structure of the antibody (see also par. 13 above) once applied to a person with an Acinetobacter infection and cannot form a basis for patentability because the use of that antibody would be obvious for the reasons laid out above (see also par. 19-21 above).
Applicant argues (Remarks pg. 8) that Uppuluri demonstrates that the polyclonal antibodies used recognize at least four unique cell surface proteins. “Uppuluri states, "we do not know which of these antigens might be the targets for the protective activity seen with mice passively or actively vaccinated with Hyrlp" (pg. 14, 2nd paragraph). Upon analysis of these cross-reactive targets, Uppulari finds that several of these targets are involved in iron acquisition, and Uppuluri hypothesizes the antibodies exert their inhibitory effect by iron starvation (pg. 12, 1st paragraph). Thus, Applicant contends Uppulari teaches the benefit of the use of polyclonal antibodies, which target multiple distinct epitopes in the bacterial iron acquisition pathway, and Uppulari does not teach or suggest that a monoclonal antibody, with one target would have the same effect or which antibody target is needed for the response reported.”
This argument has been carefully considered but is not found persuasive. Respectfully, it is believed that this argument misrepresents Uppuluri’s teachings. The researchers identified a conserved protein epitope which is found on several different proteins: “Bioinformatic, homology and energy-based modeling identified a number of conserved physicochemical structural domains within Hyr1p and several Gram-negative antigens. In particular, these algorithms identified multiple β-helical structures composed of parallel β-strands that typically create either two or three faces along within the holoprotein structure. Examples of β-helical templates identified included the phage φAB6 tailspike protein, which specifically binds oligosaccharides on the A. baumannii surface [47], the Haemophilus influenzae high molecular weight (HMW1) adhesin, and the filamentous hemagglutinin adhesin (FhaB) from Bordetella pertussis. Notably, FhaB has also been identified as an outer membrane protein of A. baumannii and is considered a protective immunogen [48].” (pg. 3 par. 2). This shared protein structure is shown in the protein structures of Figure 1. Figure 1 also shows the location on the protein structure for the peptides that were used to raise antibodies, showing how these peptides result in antibodies that target this shared structure. See also the discussion of the shared structure in par. 6 above.
Turning to the sections pointed out by the applicants, the paragraph bridging pg. 11-12 states that a siderophore outer membrane binding protein and OmpA are potential targets on A. baumanii due to both the western blotting analysis and the structural homology modelling (i.e. these proteins were known to contain the shared structure targeted by the antibody). The paragraph on pg. 14 cited by applicant states that “Bioinformatic analysis and computational modeling of these proteins further revealed that peptide 5 shares significant sequence identity with FhaB, OmpA and an immunoglobulin protein (Blg) that was not detected in our Western blotting analysis.” The Examiner cannot find any evidence that Uppuluri believes off-target binding of non-anti-Hyr1 antibodies from the polyclonal antibody mixture is responsible for the anti-A. baumanii effect. Instead, Uppuluri specifically states “The observed protection among cross-kingdom antigens are likely due to highly conserved B cell epitopes given the nature of high degree of 3-D structural homology” (pg. 14 par. 1). When viewing the sections quoted by the applicant in this context, it appears clear that Uppuluri teaches the specific anti-Hyr1 antibodies within the polyclonal antibody used in Uppuluri binds to multiple proteins because the same protein structure is found on multiple proteins. Therefore, the examiner remains of the opinion that the modification to replace this polyclonal antibody with a monoclonal antibody binding the same target would be obvious (see par. 19-21 above).
If applicant is arguing that having a reasonable expectation of success at treating Acinetobacter infection requires knowing what proteins are bound by the antibody on the bacterial surface, it is noted that the instant specification also does not identify what specific protein(s) are bound by the antibodies disclosed in both Gow and the instant specification.
Applicant argues (Remarks pg. 8): “With Uppulari in hand, one of skill in the art would have no expectation that the phenotype observed in Uppulari could be reproduced with a monoclonal antibody. Thus, Uppuluri does not teach or suggest that a monoclonal antibody would be sufficient to treat an Acinetobacter bacterial infection and also does not provide a reasonable expectation of success in doing so. This deficiency is not cured by the addition of Gow, Wang-Lin, or Janeway.”
This argument has been carefully considered but is not found persuasive. See MPEP 2143.02: “Conclusive proof of efficacy is not required to show a reasonable expectation of success. OSI Pharm., LLC v. Apotex Inc., 939 F.3d 1375, 1385, 2019 USPQ2d 379681 (Fed. Cir. 2019) ("To be clear, we do not hold today that efficacy data is always required for a reasonable expectation of success. Nor are we requiring ‘absolute predictability of success.’")”. Applicant has not provided any evidence to demonstrate why one of ordinary skill in the art would believe there would not be a reasonable expectation of success at treating Acinetobacter infection when the Uppuluri antibody can treat Acinetobacter infection and the Gow antibody is raised against the same target. See MPEP 2145.I: “Arguments presented by applicant cannot take the place of evidence in the record. See In re De Blauwe, 736 F.2d 699, 705, 222 USPQ 191, 196 (Fed. Cir. 1984); In re Schulze, 346 F.2d 600, 602, 145 USPQ 716, 718 (CCPA 1965);”
Applicant argues (Remarks pg. 8-9) that “The teachings of Gow demonstrate that while antibodies may opsonize fungi, as demonstrated in Fig. 8E, this does not always lead to decreased fungal burden, as shown in Figure 11. Gow teaches that merely identifying a monoclonal antibody that binds to Hyrl, is not predictive of its effectiveness of treating fungal infection. Finally, Gow is silent regarding the effectiveness in treating an Acinetobacter bacterial infection. Therefore, the combination of Uppuluri and Gow does not teach or suggest the use of the claimed monoclonal antibodies for the treatment of an Acinetobacter infection.”
This argument has been carefully considered but is not found persuasive. As stated above (see par. 13), “MPEP 2112.01 states that "Products of identical chemical composition can not have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id. The Gow antibody’s variable domain has an identical sequence to the instant AB123 antibody, so it necessarily has the same binding and opsonization properties.” The argument that the antibody might not opsonize or lead to decreased burden with fungal infections is not relevant to the instant antibacterial treatment method because the specification shows that the antibody does in fact have the properties of treating and opsonizing. As discussed above, Gow does not need to show effectiveness in treating Acinetobacter infection because this part of the claim is only an intended use resulting from the inherent properties of the antibody (see par. 25-27) and because efficacy data is not required for a reasonable expectation of success (see par. 33).
Applicant argues (Remarks pg. 9) that “Wang-Lin, which teaches the challenges of antibacterial monoclonal antibodies, and Janeway, which teaches the interaction between an Fc region and Fc receptor for opsonization, do not cure these deficiencies.”
This argument has been carefully considered but is not found persuasive. Wang-Lin and Janeway are not relied upon in the rejection to teach the features applicant is arguing is deficient. Arguments about the alleged deficiency are not persuasive as discussed above.
Applicant argues (Remarks pg. 9) that “Applicant further contends there is no reasonable expectation of success of treating Acinetobacter bacterial infection, with the claimed antibodies, wherein the antibody opsonizes, or increases the rate of opsonization of, an Acinetobacter cell based on the cited art.”
This argument has been carefully considered but is not found persuasive. The rejection of record argues that the ability of the antibody to opsonize Acinetobacter is an inherent property. “The Gow antibody’s variable domain has an identical sequence to the instant AB123 antibody, so it necessarily has the same binding and opsonization properties.” (par. 13 above). See MPEP 2112.V: “once a reference teaching product appearing to be substantially identical is made the basis of a rejection, and the examiner presents evidence or reasoning to show inherency, the burden of production shifts to the applicant… The burden of proof is similar to that required with respect to product-by-process claims. In re Fitzgerald, 619 F.2d 67, 70, 205 USPQ 594, 596 (CCPA 1980) (citing Best, 562 F.2d at 1255)… See MPEP § 2113 for more information on the analogous burden of proof applied to product-by-process claims”. Applicant has not presented evidence showing that the opsonization properties of the antibody do not follow inherently from the structure.
The discussion in par. 25-27 of the similar functional limitation of treating Acinetobacter infection is also relevant to this functional limitation. See also MPEP 2111.04 which addresses “wherein” clauses specifically instead of preambles, but similarly states that “Claim scope is not limited by claim language that suggests or makes optional but does not require steps to be performed, or by claim language that does not limit a claim to a particular structure.” Like the similar functional limitation of treating Acinetobacter infection, the broadest reasonable interpretation of the wherein clause is that the statement is only an intended use and therefore does not place any limitations or requirements on the administration step. Like the similar functional limitation of treating Acinetobacter infection, opsonization is merely a latent property of the antibody which is revealed when the antibody is administered to infected subjects.
Therefore, the rejection is maintained for the reasons of record and the reasons herein.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to AMELIA NICOLE DICKENS whose telephone number is (571)272-0381. The examiner can normally be reached M-R 8:30-4:30, and every other F 8:30-4:30 (EDT/EST).
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/AMELIA NICOLE DICKENS/Examiner, Art Unit 1645
/VANESSA L. FORD/Supervisory Patent Examiner, Art Unit 1674