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 ( 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. DETAILED ACTION This action is in response to claims filed 9/11/23. Claims 1-4 are pending and under examination. Notice Applicant is reminded of their Duty to Disclose (MPEP §2000) and 37 CFR 1.56. The instant claims are substantively similar to those in parent application 16/623254, yet no IDS was filed . T he PTAB issued a decision on 7/14/23 —in particular on the written description rejection regarding the same claimed antibody defined by Kd to SpA and possessing an Fc region—yet no disclosure of that decision was made in the instant application filed 9/11/23. Further, it is noted that the Patent Trial and Appeal Board (P TAB ) decided on the written description issue during the appeal in parent application 16/623254 in favor of lacking written description, affirming the Examiner. While the instant claims add an amount of antibody (40 mg/kg) and change the function of “opsonization” to one of displacement, the instant claims add no additional structure to the antibody nor does the specification provide additional information regarding structure/function or additional representative species. The instantly claimed antibody does not contain any additional limitations which would weigh in favor of meeting the written description requirement for the antibody. Applicant did not appeal that decision and there is no opportunity for further Court review of that decision. Applicant is reminded of MPEP §2190(II), stating that Applicant may be precluded from seeking a claim that is not patentably distinct from a claim which was previously rejected and affirmed on appeal. As noted, the differences in the instant claim do not substantively alter the written description issue and the claim is not patentably distinct from the claim decided on by the Board. Claim Objections Claim 1 is objected to because of the following informalities: the claim recites “of a a purified” in line 4. This is the only claim set and so the strikethrough is not an amendment, further evidenced by the lack of any status identifiers. However, the struck-through “a” does not appear to serve any purpose in the claim but rather will confusingly appear like an amendment in future versions of the claim and therefore should be removed. Appropriate correction is required. Claim Rejections - 35 USC § 112 The following is a quotation of 35 U.S.C. 112(b): (b ) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention. The following is a quotation of 35 U.S.C. 112 (pre-AIA), second paragraph: The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the appl icant regards as his invention. Claims 1-4 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claim 1 recites the limitation "their Fc regions" in line 8 . There is insufficient antecedent basis for this limitation in the claim. The word “their” may be referring to the Fc regions of the “purified monoclonal antibody” or may be referring to the Fc regions of “human IgG immunoglobulins”. Dependent claims do not clarify this. Claim 1 also recites “its Fab region paratope”. A n intact antibody typically has two paratopes and so “its Fab region paratope” (singular) lacks antecedent basis as it is unclear which of the two p aratopes this term refers to. Alternately, the claims encompass only antibodies that have a single paratope. Claims 2 and 4 recite the phrase “humanized antibody”, which is defined in the specification at paragraph 12 to be th at the antibody contains “mostly sequences of a human Ab but also includes minimal sequences derived from a non-human…Ig”. The terms “mostly” and “minimal” are relative terms. The term s are not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. The example in this paragraph is replacing the whole of the hypervariable region with non-human sequences or altering the entire framework region. The humanized antibody may also comprise residues that are not in either the donor or the recipient antibody. Altering the entirety of the binding region of an antibody would not generally be considered a “minimal” change . These are also non-limiting examples, so there is no indication of any particular part of an antibody or percentage of an antibody that must be preserved as human. While it is clear that the entirety of the antibody cannot be non-human, there is no clear guidance on when an antibody would be considered to have dropped below the threshold of “mostly” or exceeded the threshold of “minimal”. Therefore, claims 1-4 are indefinite. For examination, pronouns will be interpreted as referring to the purified monoclonal antibody and “paratope” will be interpreted as “one or more paratopes”. The interpretation of “humanized” will be set forth where relevant. 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. Claims 1-4 are rejected 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. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. Claim 1 is directed to a method of administering a monoclonal antibody which binds SpA with a certain Kd , has an Fc region able to interact with an FcR , and is able to displace human IgG bound to spA on S.aureus bacteria via their Fc regions. As such, the claim is directed to an antibody defined by function (binding ; displacement ). While “Fc region” or “Fab region” refer to some degree of structure, there is nothing implicit or inherent about these regions that confer the claimed functions. See MPEP §2163(I)(A) which states: "The claimed invention as a whole may not be adequately described where an invention is described solely in terms of a method of its making coupled with its function and there is no described or art recognized correlation or relationship between the structure of the invention and its function. A biomolecule sequence described only by a functional characteristic, without any known or disclosed correlation between that function and the structure of the sequence, normally is not a sufficient identifying characteristic for written description purposes, even when accompanied by a method of obtaining the claimed sequence.” A ntibodies generally share certain characteristics such as Fc regions or hinge regions. However, these structures are not correlated with the binding function of the antibody. The hyper variable regions (HVRs), i.e., complementarity determining regions (CDRs) of an antibody, are well established in the art as the portion of the binding region which imparts the specificity of an antibody. However, there is no way to a priori look at an antigen sequence ( SpA ) and envisage the combination of six CDRs that will bind that antigen. First, even highly related CDRs may not bind the same target. See for example Kussie ( form 892 ) who demonstrates that a single amino acid change in the heavy chain of an antibody which binds p- axophenylarsonate (Ars) completely abrogates the ability of the antibody to bind Ars but adds the functionality of binding the structurally related p- azophenylsulfonate (e.g., abstract). Second, even when provided with several related antibodies that bind the desired target, this does not represent the astronomical and potentially unknowable breadth of all possible amino acid sequences which will result in the desired binding properties. This is exemplified by the Court decision in Abbvie ( Abbvie v Janssen 759 F.3d 1285 (Fed. Cir. 2014 ) ), where Abbvie developed over 200 antibodies that shared 99.5% identity in the variable regions (p.7) and which bound the target, but in no way allowed one to envisage the unique structure of Centocor’s antibodies which bound the same target but shared only 50% sequence similarity (see table on page 11). Thus, the art recognizes that the CDRs define the binding properties of an antibody and that even single amino acid changes to this region can completely abrogate the binding specificity of an antibody. As a further exam ple, see Chen ( form 892 ) which demonstrates single amino acid changes in the VH CDR2 sequence can increase binding, decrease binding, destroy binding, or have no effect on binding when compared to the wild-type antibody. Thus, making changes to the CDR sequence of an antibody is a highly unpredictable process and the skilled artisan could not a priori make any predictions regarding such mutations with any reasonable expectation of success nor envisage the breadth of structurally unrelated CDR combinations that would still possess the required funct i ons. The specification discloses eight antibodies (p.14 sections i -viii) . However, as discussed above, without any way to determine the br eadth of the genus of such antibodies, there is no way to determine if these antibodies represent the full breadth of what is claimed. The disclosure of these specific antibodies would not convey to the artisan that App licant was in possession of the full genus of all antibodies which possess the required functions nor does it allow the skilled artisan to envisage the specific structure of such antibodies. Further note the decision in Amgen v. Sanofi 2017, where the Court supported previous decisions ( Centocor 2011; Abbvie 2014) that defining an antibody solely by what it binds does not satisfy the written description requirement, stating that this would allow patentees to “claim antibodies by describing something that is not the invention, i.e., the antigen”. MPEP 2163 states that disclosure of an antigen fully characterized by its structure, formula, chemical name, physical properties, or deposit does not, without more, provide an adequate written description of an antibody claimed by its binding affinity to that antigen. Here, while the antibody also comprises an Fc region, that region does not participate in binding to the SpA antigen and so does not serve to provide written description for those antibodies defined by a Kd to a specific antigen. Further, it is unclear from the claim whether the claimed monoclonal antibody displaces the human IgG because of the monoclonal Fc (i.e., the Fc region of the claimed antibody is responsible for the function) or if the human IgG is displaced because of the human IgG Fc (i.e., the claimed antibody only displaces those human IgG antibodies that possess an Fc region). In either case, this is a function without any corresponding structure. The instant specification suggests that it is the binding affinity—a function provided by the CDRs—which provides the displacement function (paragraph 27). The specification does not describe any Fc region that displaces human IgGs nor does the specification appear to describe displacing human IgGs because the human IgG has an Fc region. Rather, the disclosure in the specification appears to indicate that human IgGs are displaced due to binding affinity (paragraphs 27 and 29), i.e., the monoclonal antibody displaces the IgG because of the binding properties , not the Fc region. Nevertheless, even if the function is tied to the Fc region of the monoclonal antibody, there is no description of any particular structure that confers this property. Turning to the instantly disclosed antibodies, i t is appreciated that the CDR s of these antibodies are disclosed. However, these are highly conserved. For example, CDR2 of the light chain of all eight antibodies is aligned below: Thus, much like the decision in Abbvie , the disclosure of certain highly related antibodies (8 in the instant application, 200 in Abbvie ) does not allow one to envisage other antibodies that have the same binding properties but a different structure commensurate with the breadth of the genus claimed. On the other end of the spectrum, the eight antibodies are aligned according to heavy chain CDR3: Clearly, CDR3 of the heavy chain is more structurally diverse. However, this only further emphasizes the lack of written description. Given that sometimes the sequences must be preserved and other times the sequences can vary, the specification as a whole fails to clearly indicate which amino acids are necessary and in what context. For example, only one sequence possess es the SPADI sequence; it could be that this sequence is unnecessary, this sequence might be necessary in the context of the remaining VTGYYPWWFDL sequence (which is also not found in any other sequence), or the CDR as a whole may tolerate some but not other mutations, though the specification does not convey to the skilled artisan that Applicant was in possession of this invention as broadly as claimed. One of skill in the art could not predict an as-yet-created antibody sequence with a reasonable expectation of meeting the claimed functional requirements and so the instant specification clearly fails to adequately describe this genus of antibodies. Such a conclusion is supported by Koenig ( form 892 ), which provides a large mutation analysis study where every amino acid in both variable regions is substituted with every other amino acid. Looking at figure 1 of Koenig, the bottom half of each section (labeled VEGF) relates to the ability of the mutant to bind the original target, with blue meaning a reduced affinity and black meaning a complete loss of binding ability. In VH-CDR2, for example, mutating any given residue to cysteine, which is encompassed by the instant claims, resulted in reduced binding at 12 residues and a complete loss of binding at 5 residues. That is, at 100% of the positions, mutation to cysteine reduced or ablated the antibody' s ability to bind the target. Looking at a specific position, in 100% of the mutations of residue 55, binding was reduced (15/19) or eliminated (4/19). While residues 56-65 appear more tolerant of change, residues 50-55 are generally intolerant of change. It is clear from Koenig that binding function /affinity as well as any function stemming from that binding is dependent on the contribution of every residue in every CDR and that changing even single residues can have dramatic and unpredictable effects on the binding function of that antibody. It is appreciated that Koenig is studying one specific antibody and there is no evidence that the instant antibodies would react in an identical way. However, this is part of the problem. It is entirely unclear from the specification which residues of Applicant 's CDRs are tolerant or intolerant to change, and whether those tolerant positions are only tolerant to conservative mutations. The fact that some residues tolerate mutation does not convey to the skilled artisan that Applicant knew which of the claimed residues in the genus of claimed antibodies were tolerant of such, i.e., does not convey that Applicant was in possession of those sequences which are different than the exact sequences disclosed ye t preserve the claimed function; mere naming of the genus is not sufficient . In other words, the specification fails to convey possession of an invention commensurate in scope with what is now claimed and therefore fails to meet the written description requirement. I t is well-known in the art that specificity of an antibody stems from the six CDRs but that CDRs are not generally recognized as interchangeable, such that using one CDR from one antibody would not be reasonably expected to confer the same binding properties or even the same binding target when combined with two to five CDRs from other antibodies. For example, comparing the antibodies of US 20150196663 ( form 892 ; rat brain endothelial cell targeting antibodies ) to those of US 20150266947 ( form 892 ; tau protein targeting antibodies) disclose that both publications screened for antibodies using the same library of antibodies (Sheet’s library; ‘663 paragraphs 50, 69 and ‘947 paragraph 131). The six CDRs of ‘947 SEQ ID NO: 11 and ‘663 scFv15 figure 5 are aligned below: The two antibodies share identical CDRs (e.g., CDR-L1), similar CDRs (e.g., CDR-H1, CDR-L2), and highly disparate CDR sequences (e.g., CDR-H3, CDR-L3) and have different targets. One could not envisage which portions of the CDRs are necessary to impart the binding properties or which could be mutated without affecting such properties, nor does the instant specification provide guidance to this effect, demonstrating that a specific combination of six CDRs provide the claimed functions but does not allow for definition by function alone . As such, the disclosure of these sequences does not convey possession of all possible antibodies with the claimed functions; possession of the precisely defined sequence of six CDRs is required. Taken as a whole, the instant disclosure coupled with knowledge in the art fails to allow the skilled artisan to envisage the claimed genus. The specification lacks a structure/function correlation and, for the reasons described above , eight antibodies do not meet the requirements of a representative number of species for the genus as a whole. Finally, it is noted that in certain situations, u nder MPEP §2163, elements “auxiliary to the invention must have a corresponding written description only so specific as to lead one having ordinary skill in the art to that class of compounds. Occasionally, a functional recitation of those known compounds in the specification may be sufficient as that description”. However, this is not such an occasion. The instantly claimed antibody is not “auxiliary” to the invention but rather represents a key element ; as noted by the PTAB decision in the parent application, the antibody is “critical” (p.7) . Other than the eight antibodies discussed above, there is no evidence that antibodies possessing the instantly claimed properties are “known” or recognized as a “class of compounds”. Further, while the instant claims are method claims, the claim must nevertheless meet the written description requirement for the compounds used in such method (University of Rochester v G.D. Searle & Co, 358 F.3d 916, 926 (Fed Cir 2004)). Regarding claim 3, this claim adds additional binding properties without any additional structure. Thus, the claim is deficient for the reasons above. Regarding claims 2 and 4 , these claims are directed to humanized antibodies where the “hypervariable region residues of the recipient Ab are replaced by hypervariable region residues from a non-human species” (specification paragraph 12). However, according to the specification, the eight residues were derived from human B-cells (paragraphs 62-63) and there does not appear to be any disclosure of a non-human hypervariable region, i.e., non-human CDRs. As such, the specification does not convey any examples of a humanized antibody (where the CDRs are non-human) nor does a human CDR sequence inform the skilled artisan of the structure of a non-human hypervariable region. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. PTAB in appeal 2022-003788 (form 892) supports the above rejection. The instant claims add no additional structure to the antibody than those which were before PTAB nor does the disclosure provide any additional salient information to support written description. Relevant portions are reproduced here: “ While the claims at issue are directed to method for treating a SA infection, the method employs certain antibodies that are defined, in part, by their ability to bind to Sp A ”. “ The claims require particular dissociation constants or strength of binding between the antibody and the antigen (i.e. KD) .” “ The antibodies are a critical element of the claims. Thus, the claims embrace a genus of antibodies that are defined by their function not their structure. Our reviewing court has held a ‘ sufficient description of a genus instead requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can 'visualize or recognize' the members of the genus. ’ Ariad, 598 F.3d at 1350. In the instant case, Appellant has not met either criteria. Appellant has not pointed to, not do we discern any disclosure of structural features common to the members of the genus. ” “ Similarly, while Appellant has identified 8 antibodies that can be used in practice of the claimed method, we agree with the Examine [r] that the number is insufficient support the current claims. Ans. 18. While Appellant has provided some information regarding the structure of the antibodies, see Spec. [paragraph] 63. Appellant has not pointed to nor do we discern any common feature that allows each of the antibodies to perform the functions recited in the claims. ” "One needs to show that one has truly invented the genus, i.e., that one has conceived and described sufficient representative species encompassing the breadth of the genus. Otherwise, one has only a research plan, leaving it to others to explore the unknown contours of the claimed genus." AbbVie, 759 F .3d at 1300. Abbvie noted the need to "describe representative antibodies to reflect the structural diversity of the claimed genus" and teaching that the binding affinity or " koff rate is merely a desired result, rather than the actual means for achieving that result." Id. at 1301. ” "[T]he asserted claims constitute a wish list of properties that a ...antibody should have ” Centocor Ortho Biotech, Inc. v. Abbott Laboratories, 636 F.3d 1341, 1351 (Fed. Cir. 2011). “ But a 'mere wish or plan' for obtaining the claimed invention is not sufficient." Therefore, claims 1-4 do not meet the written description requirement. 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. The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness . Claim (s) 1-4 is/are rejected under 35 U.S.C. 103 as being unpat entable over Simard (US 20150344548; form 892). Regarding claim 1 , Simard teaches a pharmaceutical composition comprising “a pharmaceutically acceptable carrier and a purified monoclonal antibody which specifically binds Staphylococcus aureus protein A ( SpA ) with a K d of less than 1x10 -10 M via its Fab region paratope ” (claim s 1 and 6 ) where the antibody “is able to displace human IgG immunoglobulins bound to SpA on Staphylococcus aureus bacteria via their Fc regions” (claim 6). Simard teaches these antibodies “bind a target epitope of SpA on a SA bacterium while their Fc regions are still able to interact with an FcR ” (paragraph 6) ; binding the target epitope indicates the region is bound by the Fab paratope as noted in the Simard claim 1 . Simard teaches the antibody “used in methods of treating…[ S.aureus ] infections” (abstract). Simard teaches such infections are the second most frequent cause of bloodstream infections in humans (paragraph 4), clearly suggesting treating such bloodstream infections in a human. Simard teaches the subject being a hospitalized patient ( “subject admitted to a hospital”; paragraph 78) . Simard teaches a subject “having a SA infection”, meeting the limitations of the infection being “confirmed”. Alternately, the teaching of treating SA bloodstream infections as described above would suggest that such condition could be confirmed prior to pharmaceutical treatment because the suggestion to treat this population clearly suggests identifying that population. With respect to administering 40 mg/kg , Simard teaches administering various doses including 0.1-10,000 mg/day (paragraph 75). Simard teaches this dose will vary by body weight, which would have made obvious to the ordinary artisan the “mg/kg” units. For average human weights, the Simard range overlaps with the instant value. Further, Simard teaches this as a result-effective variable, optimizing the dose by body weight, age, administration, and states that a suitable dose is “well within the purview of those skilled in the art” (paragraph 75). In the case where the claimed ranges “overlap or lie inside ranges disclosed by the prior art” a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990). See MPEP §2144.05(I). Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCP A 1955). See MPEP §2144.05(II). Such is the case here, where the same antibody was administered to the same people for the same reasons , the difference being solely in the concentration (dose) administered as the results themselves are not an active step and flow from the method itself . Optimization of the dose is a matter of routine experimentation and does not serve to support patentability. “ [I] t is a settled principle of law that a mere carrying forward of an original patented conception involving only change of form, proportions, or degree, or the substitution of equivalents doing the same thing as the original invention, by substantially the same means, is not such an invention as will sustain a patent, even though the changes of the kind may produce better results than prior inventions” (MPEP §2144.05(II)(A)). Thus, even if the result of reduced hospitalization or reduced serious adverse effects is “better” than in Simard—of which there is no objective evidence—this change would be insufficient. With respect to the limitation “ reducing the occurrence of serious adverse event s and length of hospitalization ”, this is a result flowing from the administration itself. MPEP § 2112 (II ), states, "there is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the time of invention, but only that the subject matter is in fact inherent in the prior art reference. Schering Corp. v. Geneva Pharm. Inc., 339 F.3d 1373, 1377, 67 USPQ2d 1664, 1668 (Fed. Cir. 2003)." The fact that the inventor 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. See Ex parte Obiaya , 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985). Such is the case here, where administering the same antibody to the same population for the same reason will produce the same results. Furthermore, Integra Life Sciences I Ltd. v. Merck KGaA , 50 USPQ2d 1846 (DC SCalif , 1999) makes clear that a reference teaching a process may anticipate claims drawn to a method comprising the same process steps, despite the recitation of a different intended use in the preamble or the later discovery of a particular property of one of the star ting materials or end products. Further, the court has noted that a "‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’" Id. (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003). See MPEP § 2111.04). Similarly, this phrase appears only in the preamble and not as a positively recited step or achieved goal. When reading the preamble in the context of the entire claim, the recitation “for reducing the occurrence…and length…” is not limiting because the body of the claim describes a complete invention and the language recited solely in the preamble does not provide any distinct definition of any of the claimed invention’s limitations. Thus, the preamble of the claim(s) is of no significance to claim construction. See Pitney Bowes, Inc. v. Hewlett-Packard Co. , 182 F.3d 1298, 1305, 51 USPQ2d 1161, 1165 (Fed. Cir. 1999). See MPEP § 2111.02. Further, these results would have been obvious. The art makes obvious treating a human in a hospital for a bacterial bloodstream infection. It would have been an obvious inference by the person of ordinary skill in the art that treating an infection would reduce the occurrence of serious adverse events associated with that infection as well as reducing the length of hospitalization compared to letting a bacterial infection run untreated. See MPEP 2141(II)(C): "A person of ordinary skill in the art is also a person of ordinary creativity, not an automaton." KSR, 550 U.S. at 421, 82 USPQ2d at 1397. "[I]n many cases a person of ordinary skill will be able to fit the teachings of multiple patents together like pieces of a puzzle." Id. at 420, 82 USPQ2d at 1397. Office personnel may also take into account "the inferences and creative steps that a person of ordinary skill in the art would employ." Id. at 418, 82 USPQ2d at 1396. Regarding claim 3, Simard teaches the antibodies bind the IgG binding and Xr repeat sequences of SpA (paragraph 84). Regarding claim s 2 and 4 , these limitations are taught by Simard , which states “the selected clones were sequenced and the heavy and light chains were cloned into vectors with an IgG3 constant (Fc) region (one that lacks the SpA recognition site in the Fab regions)” (paragraph 85). These IgG3 constant regions were human (paragraphs 6, 8, 12, 84). Therefore, claims 1-4 would have been obvious. 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 . Note that, “[t] he specification can be used as a dictionary to learn the meaning of a term in the patent claim. Toro Co. v. White Consol. Indus., Inc. , 199 F.3d 1295, 1299, 53 USPQ2d 1065, 1067 (Fed. Cir. 1999)( ‘ [W] ords in patent claims are given their ordinary meaning in the usage of the field of the invention, unless the text of the patent makes clear that a word was used with a special meaning. ’ ); Renishaw PLC v. Marposs Societa ' per Azioni , 158 F.3d 1243, 1250, 48 USPQ2d 1117, 1122 (Fed. Cir. 1998) ( ‘ Where there are several common meanings for a claim term, the patent disclosure serves to point away from the improper meanings and toward the proper meanings. ’ ). See also MPEP § 2111.01 . Further, those portions of the specification which provide support for the patent claims may also be examined and considered when addressing the issue of whether a claim in the application defines an obvious variation of an invention claimed in the patent. In re Vogel , 422 F.2d 438, 441-42, 164 USPQ 619, 622 (CCPA 1970). The court in Vogel recognized ‘ that it is most difficult, if not meaningless, to try to say what is or is not an obvious variation of a claim, ’ but that one can judge whether or not the invention claimed in an application is an obvious variation of an embodiment disclosed in the patent which provides support for the patent claim. According to the court, one must first ‘ determine how much of the patent disclosure pertains to the invention claimed in the patent ’ because only ‘ [t]his portion of the specification supports the patent claims and may be considered. ’ The court pointed out that ‘ this use of the disclosure is not in contravention of the cases forbidding its use as prior art, nor is it applying the patent as a reference under 35 U.S.C. 103 , since only the disclosure of the invention claimed in the patent may be examined. ’’’ MPEP §804(II)(B)(1) . Claims 1-4 are rejected on the ground of nonstatutory double patenting a s being unpatentable over claims 1-8 of U.S. Patent No. 9486523 . Although the claims at issue are not identical, they are not patentably distinct from each other because : R eference claim 1 is directed to treatment of any S.aureus infection (not just bloodstream infections as instantly claimed) using an antibody meeting all of the claimed requirements; the CDRs in reference claim 1 are those of an instantly disclosed antibody which meets the requirements, therefore the antibody in reference claim 1 either explicitly or inherently possesses the same functions. The use of the antibody meets the requirements of the instant composition claims and, when evaluating the meaning of “infection” in the reference claims, the reference specification discloses only two: cardiovascular and bloodstream (C1), which makes the instant method of treating specifically bloodstream infections obvious. The reference claims also specifically claim s the displacement limitation and being a human or humanized antibody, while the treatment group of the reference claims include, e.g., subjects which were hospitalized with an S.aureus adverse event (e.g. C15). Regarding the dose of 40 mg/kg, this would have been obvious for the same reasons articulated in the Simard rejection above, incorporated herein. Briefly, the reference teaches doses are a result effective variable, will alter based on body weight, and discloses overlapping ranges (C13-14) . Claims 1-4 are rejected on the ground of nonstatutory double patenting a s being unpatentable over claims 1-10 of U.S. Patent No. 9783598 . Although the claims at issue are not identical, they are not patentably distinct from each other because : R eference claim 4 is directed to treatment of any S.aureus infection (not just bloodstream infections as instantly claimed) using an antibody with the same target, Kd , and other inherent functions as that which is now claimed. When evaluating the meaning of “infection” in the reference claims, the reference specification discloses only two: cardiovascular and bloodstream (C1), which makes the instant method of treating specifically bloodstream infections obvious. The reference claims also specifically claim the displacement limitation and being a human or humanized antibody, while the treatment group of the reference claims include, e.g., subjects which were hospitalized with an S.aureus adverse event (e.g. C15). Finally, when looking to the specification to determine how e.g., written description support is supplied for the instant genus of antibodies, the antibody of identical amino acid sequence is disclosed (C17). Regarding the dose of 40 mg/kg, this would have been obvious for the same reasons articulated in the Simard rejection above, incorporated herein. Briefly, the reference teaches doses are a result effective variable, will alter based on body weight, and discloses overlapping ranges (C13-14). Claims 1-4 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-10 of U.S. Patent No. 10214581. Claims 1-4 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of U.S. Patent No. 10577410. Claims 1-4 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-8 of U.S. Patent No. 9416172. The ‘581, ‘410, and ‘172 patents individually serve as the basis for nonstatutory double patenting by the same rationale as described above. Claims 1-4 are rejected on the ground of nonstatutory double patenting a s being unpatentable over claims 1-2 of U.S. Patent No. 11370831 . Although the claims at issue are not identical, they are not patentably distinct from each other because : T he reference claim is to a n antibody in a pharmaceutical composition meeting all of the instantly claimed requirements, including the same target, Kd , displacement, and other inherent functions as that which is now claimed. Th e reference c laims do not explicitly claim the purpose of the antibody. However, the specification can be used to determine the utility of a composition; see the decisions in Sun Pharmaceuticals v Eli Lily Fed Cir July 28, 2010; Geneva v GlaxoSmithKline 349, F.3d 1373; and Pfizer v Teva 518 F3d 1353 supporting the Office’s use of disclosed utilities of compositions when applying double patenting rejections to method claims. The reference document clearly discloses its use in treating S.aureus infection. Further as above, the specification may be used to understand the terms in a claim and the reference specification notes that an “infection” includes a bloodstream infection (paragraph 4) and that the antibody meeting the criteria of the instant claim also has an identical amino acid sequence (PA8-G3; C17 ) and doses would have been obvious as above (C13-14) . Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT ADAM M WEIDNER whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-3045 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-T 9-18; W-R 9-15 . Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, FILLIN "SPE Name?" \* MERGEFORMAT Jeffrey Stucker can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT 571-272-0911 . The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /Adam Weidner/ Primary Examiner, Art Unit 1675