DETAILED ACTION
1. The present application is being examined under the pre-AIA first to invent provisions.
2. Applicant’s amendment to the claims filed on January 27, 2025 is acknowledged.
Claims 1-19 have been canceled.
Claims 20-26 have been added.
Claims 20-26 are pending and currently under consideration.
3. The specification is objected to for following reasons:
Applicant’s amendment to the instant specification filed on January 27, 2025 is objected to under 35 USC 132 because it introduced and new amino acid sequences of SEQ ID NOs: 36-44. 35 U.S.C. 132 states that no amendment shall introduce new matter into the disclosure of the invention. Applicant asserts that the structure and amino acid sequences of omalizumab was introduced because the word omalizumab was mentioned in [131], [199], and [200] of the specification as-filed. Applicant further asserts that omalizumab was recognizable to one of ordinary skill in the art and was disclosed in US 2006/0088523 in [314]). As such, the amendment adding structure and sequences of omalizumab should be entered.
The is not found persuasive because the amendment to the specification added new matter to the instant specification. Specifically, the entire new Table 1 depicting subunits of omalizumab including heavy chain, VH, CH1, CH2, CH3, light chain, VL, and CL separately raise issues under new matter.
There are three disclosures of omalizumab in the instant specification as-filed in [131], [199], and [200].
[0131] of the instant specification as-filed discloses a laundry list of a antibodies and Fc fusions wherein omalizumab is one of the hundreds of antibodies and Fc fusions. [199] and [200] of the specification as-filed discloses the variable regions of the humanized antibody omalizumab and discloses the VH (SEQ ID NO:21) and VL (SEQ ID NO:22) amino acid sequences in Figure 4 as well as amino acid substitutions M428L/N434S in the Fc region of human IgG1 of omalizumab in Figure 12.
It appears that the newly added SEQ ID NOs:36 and 37 are identical to the SEQ ID NOs: 21 and 22 disclosed in Figure 4, respectively.
However, applicant has never contemplated each subunit of the amino acid sequences disclosed in newly added Table 1. Further, it is not necessary to resubmit existing SEQ ID NOs: 21 and 22 under SEQ ID NOs: 37 and 43. Furthermore, contrary to applicant’s reliance on US 2006/0088523 in [314] to support the structure and sequences of omalizumab, note nowhere in the instant specification discloses heavy chain, VH, CH1, CH2, CH3, light chain, VL, and CL currently listed in the newly added Table 1.
Applicant is required to cancel the new matter in the reply to this Office action.
Claim Interpretation
4. The following is a quotation of 35 U.S.C. 112(f):
(f) Element in Claim for a Combination. – An element in a claim for a combination may be expressed as a means or step for performing a specified function without the recital of structure, material, or acts in support thereof, and such claim shall be construed to cover the corresponding structure, material, or acts described in the specification and equivalents thereof.
The following is a quotation of pre-AIA 35 U.S.C. 112, sixth paragraph:
An element in a claim for a combination may be expressed as a means or step for performing a specified function without the recital of structure, material, or acts in support thereof, and such claim shall be construed to cover the corresponding structure, material, or acts described in the specification and equivalents thereof.
5. Claims 21-26 in this application are given their broadest reasonable interpretation using the plain meaning of the claim language in light of the specification as it would be understood by one of ordinary skill in the art. The broadest reasonable interpretation of a claim element (also commonly referred to as a claim limitation) is limited by the description in the specification when 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, is invoked.
As explained in MPEP § 2181, subsection I, claim limitations that meet the following three-prong test will be interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph:
(A) the claim limitation uses the term “means” or “step” or a term used as a substitute for “means” that is a generic placeholder (also called a nonce term or a non-structural term having no specific structural meaning) for performing the claimed function;
(B) the term “means” or “step” or the generic placeholder is modified by functional language, typically, but not always linked by the transition word “for” (e.g., “means for”) or another linking word or phrase, such as “configured to” or “so that”; and
(C) the term “means” or “step” or the generic placeholder is not modified by sufficient structure, material, or acts for performing the claimed function.
Use of the word “means” (or “step”) in a claim with functional language creates a rebuttable presumption that the claim limitation is to be treated in accordance with 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph. The presumption that the claim limitation is interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, is rebutted when the claim limitation recites sufficient structure, material, or acts to entirely perform the recited function.
Absence of the word “means” (or “step”) in a claim creates a rebuttable presumption that the claim limitation is not to be treated in accordance with 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph. The presumption that the claim limitation is not interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, is rebutted when the claim limitation recites function without reciting sufficient structure, material or acts to entirely perform the recited function.
Claim limitations in this application that use the word “means” (or “step”) are being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, except as otherwise indicated in an Office action. Conversely, claim limitations in this application that do not use the word “means” (or “step”) are not being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, except as otherwise indicated in an Office action.
This application includes one or more claim limitations that use the word “means” but are nonetheless not being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph because the claim limitation(s) recite(s) sufficient structure, materials, or acts to entirely perform the recited function.
Such claim limitation(s) is/are: “an anti-IgE antibody comprising a means for binding human IgE” in independent claim 21 and “wherein the VH and VL form means for binding human IgE protein” in independent claim 24.
Specifically, the independent claims 21 and 24 recite “means for binding human IgE” and thus satisfies prongs “A” and “B”. Dependent claims 23
However, the claim does not satisfy prong “C” which requires that “the generic placeholder is not modified by sufficient structure, material, or acts for performing the claimed function”.
Here, independent claims 21 and 24 modifies the “means for binding human IgE” to necessarily have the structure of being “an anti-IgE antibody” or an “anti-IgE antibody comprising two heavy chains comprising VH-CH1-hinge-CH2-CH3, and tow light chain comprising VL-CL”, therefore, the claims do provide structural limitations concerning the “means” that is binding human IgE so that is not generic.
For example, Robertson et al. (Biochemistry 1990 29;35:8093-8099) teach a human IgE-binding protein cloned from a human HeLa cell (e.g. see Abstract). However, human IgE-binding protein cannot serve as “means for binding human IgE” even though it is the protein for human IgE binding CD40 because it is not an antibody as required by the independent claims 21 and 24. Therefore, it is clear that the recited “means” is modified by structure of having to be an antibody rather than being a generic means with no structural limitation as required under 35 USC 112(f).
Because this/these claim limitation(s) is/are not being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, it/they is/are not being interpreted to cover only the corresponding structure, material, or acts described in the specification as performing the claimed function, and equivalents thereof.
If applicant intends to have this/these limitation(s) interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, applicant may: (1) amend the claim limitation(s) to remove the structure, materials, or acts that performs the claimed function; or (2) present a sufficient showing that the claim limitation(s) does/do not recite sufficient structure, materials, or acts to perform the claimed function.
6. The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
7. Claims 22 and 25 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.
Claims 22 and 25 recites the limitation "at least 95% identical to the amino acid sequence of the heavy chain of omalizumab, and ….. at least 95% identical to the amino acid sequence of the light chain of omalizumab". There is insufficient antecedent basis for this limitation in the independent claims 21 and 24, respectively.
8. 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.
9. Claims 21-24 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.
A) This is a Written Description, New Matter rejection
Claim 21 recites an anti-IgE antibody comprising a means for binding human IgE and a Fc domain comprising M428L/N434S substitutions as compared to a parent Fc polypeptide.
Claim 24 is drawn to an anti-IgE antibody comprising two heavy chains comprising CH-CH1-hinge-CH2-CH3 and two light chain comprising VL-CL, wherein the CH2-CH3 is an Fc domain and comprises amino acid substitution M428L/N434S as compared to a human Fc IgG polypeptide, wherein the anti-IgE antibody has increased in vivo half-life as compared to said antibody without the amino acid substitutions.
Dependent claims 22 and 25 further limits the anti-IgE antibody to comprise two heavy chains that each have an amino acid sequence that is at least 95% identical to the heavy chain of omalizumab and two light chains that each have an amino acid sequence that is at least 95% identical to the light chain of omalizumab.
Claim 23 and 26 further recites that the anti-IgE antibody wherein said means for binding human IgE comprises a VH at least 95% identical to SEQ ID NO:37 and a VL at least 95% identical to SEQ ID NO:43. Claims 23 appears to recite that the means for binding human IgE via modification in the VH and VL region.
These newly added claims are not supported by the original disclosure or claim as filed.
Applicant’s amendment, filed on January 27, 2025, directs to support to paragraphs 15, 16, 74, 113, newly inserted Table 1, 57, and 124 in the specification as-filed, and asserts that no new matter has been added.
However, the specification as filed does not provide sufficient written description of the above-mentioned new claims.
The specification does not provide sufficient support for the newly added claims described above.
For example,
[15], [16], [57], of the specification discloses Fc variant, not IgE or omalizumab;
[131] discloses a laundry list of antibodies and Fc fusions and only mention omalizumab once.
Newly inserted [132] introduces new matter to the instant specification thus cannot be relied upon to support the new claims.
[124] discloses variant IgG variant sequence preferably at least about 95% homology to those of the parent Fc polypeptide, but does not disclose IgE or omalizumab.
The instant claims now recite an anti-IgE antibody comprises a means for biding human IgR and a Fc variant comprsiing M428L/N434S as compared to a human Fc polypeptide or a VH and VL that are at least 95% identical in amino acid sequence of omalizumab or newly added SEQ ID NOs: 37 and 43, which were not clearly disclosed in the specification. Therefore, the claims represent a departure from the specification and claims originally filed. Applicant’s reliance on a single species of omalizumab do not provide sufficient direction and guidance to the features currently claimed. It is noted that a generic or a sub-generic disclosure cannot support a species unless the species is specifically described. It cannot be said that a subgenus is necessarily described by a genus encompassing it and a species upon which it reads. See In re Smith 173 USPQ 679 683 (CCPA 1972) and MPEP 2163.05.
Such limitations recited in the present claims, which did not appear in the specification, as filed, introduce new concepts and violate the description requirement of the first paragraph of 35 U.S.C. 112.
Applicant is required to cancel the new matter in the response to this Office Action.
Alternatively, applicant is invited to provide sufficient written support for the “limitations” indicated above. See MPEP 714.02, 2163.05-06 and 2173.05 (i).
B) claims 22, 23, 25 and 26 are drawn to an anti-IgE antibody comprising an amino acid sequence that is at least 95% identical to the VH of omalizumab or SEQ ID NO:37 and an amino acid sequence that is at least 95% identical to the VL of omalizumab or SEQ ID NO:43. SEQ ID NO:37 is the amino acid sequence of VH of omalizumab and SEQ ID NO:43 is the VL of omalizumab.
The specification discloses VH of SEQ ID NO:21 and VL of SEQ ID NO:22 of the anti-IgE antibody omalizumab (e.g. see Fig. 4) of the specification as filed.
There is insufficient written description in the specification as-filed of the anti-IgE antibody having a VH and a VL that are at least 95% identical to SEQ ID NOs: 37 and 43, respectively, as recited in the instant claims.
The claims recite a genus an anti-IgE antibody comprising a VH and a VL that are at least 95% identical to the heavy and light chain of omalizumab or at least 95% identical to SEQ ID NOs” 37 and 43, respectively as part of the invention without providing a physical structure or testable functional activity for the antibody.
The genus of the anti-IgE antibody are therefore extremely large. Applicant has disclosed only the VH and VL of omalizumab (see Fig. 4 of SEQ ID NOs: 21 and 22 of the specification as-filed). Thus Applicant has disclosed only a limited species of the anti-IgE antibody, namely omalizumab consisting of the amino acid substitutions in specific positions in the Fc region such as M428L and N434S. The claimed anti-IgR antibodies lack a common structure essential for their function and the claims do not require any particular structure basis or testable functions be shared by the instant antibodies.
It does not appear based upon the disclosure of a single anti-IgE antibody omalizumab consisting of specific amino acid substitutions in specific positions in the Fc region alone that Applicant was in possession of the necessary common attributes or features of the elements possessed by the members of the genus in view of the limited number of species disclosed and the extensive variation permitted within the genus of the anti-IgE antibodies having amino acid sequences at least 95% identical to the heavy and light chain of omalizumab or at least 95% identical to VH and VL of SEQ ID NOs: 37 and 43.
“Adequate written description requires a precise definition, such as by structure, formula, chemical name or physical properties, not a mere wish or plan for obtaining the claimed chemical invention.” Regents of the University of California v. Eli Lilly and Co. 43 USPQ2d 1398 (Fed. Cir. 1997).
The disclosure must allow one skilled in the art to visualize or recognize the identity of the subject matter of the claim. Id. 43 USPQ2d at 1406.
In the absence of disclosure of relevant, identifying characteristics of the anti-IgE antibody, there is insufficient written disclosure under 35 U.S.C. 112, first paragraph.
10. 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.
11. Claims 20-26 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims in following US Patents, all in view of Lowman et al. (US 2002/0054878) and Adams et al. (US 2006/0067930):
claim 1of US 8,088,376 (the ‘376 Patent, claim is drawn to a method of increasing antibody serum half-life by administering an antibody comprising a variant Fc region comprising 428L and 434S in the Fc region, wherein said antibody has increased in vivo half-life as compared to an antibody with a parent Fc polypeptide;
claims 1 of US 8,546,543 (the ‘543 Patent, claims is drawn to an antibody comprising a variant Fc region comprising M428L and N434S substitution in the Fc region); and
claims 1-4 of US 8,394,925 (the ‘925 Patent, claims are drawn to a polypeptide comprising a variant Fc region comprising 428L and N434S, wherein the polypeptide is an antibody or immunoadhesin).
The instant claims are drawn to an anti-human IgE antibody omalizumab or an anti-IgE antibody comprising VH and VL having amino acid sequences that are at least 95% identical to SEQ ID NOs: 37 and 43, respectively. SEQ ID NO:s 37 and 43 are the VH and VL amino acid sequences of omalizumab.
The claims in the conflicting US Patents are described above. They differ from the instant invention by not reciting an anti-IgE antibody having the VH and VL amino acid sequences that are at least 95% identical to SEQ ID NOs: 37 and 43, respectively or omalizumab.
Lowman et al. teach an anti-human IgE antibody having VH and VL that are 100% identical to the instantly claimed anti-IgE (see sequence alignment below):
Instant SEQ ID NO:37 alignment:
RESULT 5
US-09-920-171-25
(NOTE: this sequence has 6 duplicates in the database searched)
Sequence 25, US/09920171
Publication No. US20020054878A1
GENERAL INFORMATION
APPLICANT: Lowman, Henry B.
APPLICANT: Presta, Leonard G.
APPLICANT: Jardieu, Paula M.
APPLICANT: Lowe, John
TITLE OF INVENTION: Improved Anti-IgE Antibodies (as amended)
FILE REFERENCE: P1123C2US
CURRENT APPLICATION NUMBER: US/09/920,171
CURRENT FILING DATE: 2001-08-01
PRIOR APPLICATION NUMBER: US 08/887,352
PRIOR FILING DATE: 1997-07-02
PRIOR APPLICATION NUMBER: US 09/296,005
PRIOR FILING DATE: 1999-04-21
NUMBER OF SEQ ID NOS: 44
SEQ ID NO 25
LENGTH: 233
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Heavy chain F(ab)'2 sequence derived from MAE11
Query Match 100.0%; Score 655; Length 233;
Best Local Similarity 100.0%;
Matches 121; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLVESGGGLVQPGGSLRLSCAVSGYSITSGYSWNWIRQAPGKGLEWVASITYDGSTNY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLVESGGGLVQPGGSLRLSCAVSGYSITSGYSWNWIRQAPGKGLEWVASITYDGSTNY 60
Qy 61 NPSVKGRITISRDDSKNTFYLQMNSLRAEDTAVYYCARGSHYFGHWHFAVWGQGTLVTVS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 NPSVKGRITISRDDSKNTFYLQMNSLRAEDTAVYYCARGSHYFGHWHFAVWGQGTLVTVS 120
Qy 121 S 121
|
Db 121 S 121
Instant SEQ ID NO:43 alignment:
RESULT 71
US-09-920-171-9
(NOTE: this sequence has 3 duplicates in the database searched)
Sequence 9, US/09920171
Publication No. US20020054878A1
GENERAL INFORMATION
APPLICANT: Lowman, Henry B.
APPLICANT: Presta, Leonard G.
APPLICANT: Jardieu, Paula M.
APPLICANT: Lowe, John
TITLE OF INVENTION: Improved Anti-IgE Antibodies (as amended)
FILE REFERENCE: P1123C2US
CURRENT APPLICATION NUMBER: US/09/920,171
CURRENT FILING DATE: 2001-08-01
PRIOR APPLICATION NUMBER: US 08/887,352
PRIOR FILING DATE: 1997-07-02
PRIOR APPLICATION NUMBER: US 09/296,005
PRIOR FILING DATE: 1999-04-21
NUMBER OF SEQ ID NOS: 44
SEQ ID NO 9
LENGTH: 114
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Light chain sequence derived from MAE11
Query Match 98.8%; Score 575; Length 114;
Best Local Similarity 98.2%;
Matches 109; Conservative 2; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DIQLTQSPSSLSASVGDRVTITCRASQSVDYDGDSYMNWYQQKPGKAPKLLIYAASYLES 60
|||||||||||||||||||||||||||||||:||||:|||||||||||||||||||||||
Db 1 DIQLTQSPSSLSASVGDRVTITCRASQSVDYEGDSYLNWYQQKPGKAPKLLIYAASYLES 60
Qy 61 GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSHEDPYTFGQGTKVEIK 111
|||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSHEDPYTFGQGTKVEIK 111
Lowman et al. further teach that IgE mediates allergic response such as asthma (e.g. see [0003]) and anti-IgE antibodies can be administered to treat disorders mediated by IgE (e.g. see claims 1-31).
Adams et al. teach anti-IgE antibodies having improved Fc effector functions (e.g. see [0151]). Adams et al. teach that FcRn binds to IgG; the FcRn-IgG interaction has been studied extensively and appears to involve residues at the CH2, CH3 domain interface of the Fc region of IgG, including N434 and 428, these residues interact with residues primarily located in the .alpha.2 domain of FcRn. Mutations such as N434F/W/Y can increase Fc’s affinity to FcRn, thereby increase serum half-life of the antibody (e.g. see [0026]-[0038]).
It would thus be obvious to one of ordinary skill in the art to mutated the known anti-IgE antibody disclosed by Lowman et al. and Adams et al. in M428L and N434S as recited in the conflicting claims in the ‘376 Patent, the ‘543 Patent, and the ‘925 Patent, and have a reasonable expectation of success. This is because the conflicting claims in the US Patents described above recite amino acid substitutions M428L/N434S in the Fc region of an antibody and method of increasing the antibody’s serum half-life by mutating these two positions in the Fc region. Given that the instantly recited omalizumab or anti-IgE antibody having the VH and VL amino acid sequences were known in the art to be therapeutic for allergy, and in view of the well known amino acid substitutions M428L/N434S for increase antibody’s serum half life as recited in the claims in US Patents described above, one of ordinary skill in the art at the time the invention was filed would have been motivated to mutate the well-known therapeutic anti-IgE antibody omalizumab having the VH and VL amino acid sequences as recited in the instant claims by
substituting M428L and N434S in the Fc region as recited in claims in the 376 Patent, the ‘543 Patent, and the ‘925 Patent with a reasonable expectation of success. As such, the claims in the 376 Patent, the ‘543 Patent, and the ‘925 Patent would render the instant claims obvious.
12. No claim is allowed.
13. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHUN DAHLE whose telephone number is (571)272-8142. The examiner can normally be reached Mon-Fri 6:30am-4:00pm.
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/CHUN W DAHLE/Primary Examiner, Art Unit 1641