Prosecution Insights
Last updated: April 19, 2026
Application No. 18/555,093

NEW METHOD TO IMPROVE THE ANTI-TUMORAL ACTIVITY OF MACROPHAGES

Non-Final OA §102§103§112
Filed
Oct 12, 2023
Examiner
DENT, ALANA HARRIS
Art Unit
1643
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Nantes Université
OA Round
1 (Non-Final)
44%
Grant Probability
Moderate
1-2
OA Rounds
3y 11m
To Grant
77%
With Interview

Examiner Intelligence

Grants 44% of resolved cases
44%
Career Allow Rate
324 granted / 730 resolved
-15.6% vs TC avg
Strong +33% interview lift
Without
With
+32.6%
Interview Lift
resolved cases with interview
Typical timeline
3y 11m
Avg Prosecution
62 currently pending
Career history
792
Total Applications
across all art units

Statute-Specific Performance

§101
11.0%
-29.0% vs TC avg
§103
29.7%
-10.3% vs TC avg
§102
23.1%
-16.9% vs TC avg
§112
27.4%
-12.6% vs TC avg
Black line = Tech Center average estimate • Based on career data from 730 resolved cases

Office Action

§102 §103 §112
DETAILED ACTION Notice of Pre-AIA or AIA Status 1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. 2. Claims 16-30 are pending. Claims 1-15 have been cancelled. Claims 16-30 have been added. Claims 16-30 are examined on the merits. Claim Rejections - 35 USC § 112 3. 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. 4. Claims 23 and 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. MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. A “representative number of species” means that the species which are adequately described are representative of the entire genus. See, e.g., AbbVie Deutschland GMBH v. Janssen Biotech , 759 F.3d 1285, 111 USPQ2d 1780 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus take into account the state of the art at the time of the invention. “Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species.” Ariad Pharmaceuticals Inc. v. Eli Lilly & Co ., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010). On 22 February 2018, the USPTO provided a Memorandum clarifying the Written Description Guidelines for claims drawn to antibodies, which can be found at www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf. That Memorandum indicates that, in compliance with recent legal decisions, the disclosure of a fully characterized antigen no longer is sufficient written description of an antibody to that antigen. The instant claims are drawn to an anti- O-acetylated disialoganglioside (OAcGD2) antibody compound comprising a light chain variable region (VL) and heavy chain variable region (VH) having a sequence that is at least 85% sequence identity with SEQ ID NO: 7 and SEQ ID NO: 8, respectively, as well as variants of VH sequences, SEQ ID NO: 9-SEQ ID NO: 12, SEQ ID NO: 16, SEQ ID NO: 17 and variants of VL sequences, SEQ ID NO: 13-SEQ ID NO: 15, SEQ ID NO: 18 and SEQ ID NO: 19 , the pharmaceutical composition comprising said antibody and methods of administering one of the antibod y cited, herein. The claims read on a number of possible alterations within the CDRs regions that could affect antigen binding. It is well-known in the antibody art, antibodies as a class share an overall structure generally comprising two heavy chain polypeptides that each comprises a heavy chain variable region (VH) and a heavy chain constant region made up of several domain (CH1, hinge, CH2, CH3, and for some antibodies, a CH4). Each of the heavy chains pairs with a light chain polypeptide that comprises a light chain variable region (VL) and a constant region. But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure each antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level. By the time the invention was made, it was well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs that provide the majority of the contact residues for the binding of the antibody to its target epitope, see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1 within Almagro et al. ( Frontiers in Bioscience 13: 1619-1633, January 1, 2008). Chimeric antibodies comprise the heavy and light chain variable regions of a rodent antibody linked to human constant regions and preserve the entirety of the VH and VL of the parent antibody. Id . at 1619-20. Humanized antibodies comprise only the CDRs, or in some cases an abbreviated subset of residues within the CDRs, of a parental rodent antibody in the context of human framework sequences, see Section 4 of Almagro. All of the CDRs of the heavy and light chain, in their proper order of CDR1, then CDR 2, then CDR 3, and in the context of framework sequences which maintain their required conformation are generally required to produce a humanized antibody in which the heavy and light chains associate to form an antigen-binding region that binds the same antigen as the parental rodent antibody, see Section 4. Almagro provides a detailed discussion regarding various methods of humanization, including rationale design approaches and empirical approaches based on random screening, see Almagro , Sections 4 and 5. Examples of antigen binding domains comprising only a VH (or less commonly, a VL) that in turn comprise only three CDRs certainly do exist in the literature, but those antibodies generally comprise unique structures such as CDR1 and CDR3’s that are elongated in length and that are often disulfide linked (see De Genst et al., Developmental and Comparative Immunology 30:187-198, available online 11 July 2006. “Shuffling” of the VL (or less commonly the VH) had also been used to improve affinity of a parent antibody in certain instances. But the procedure generally required a "dominant" VH (i.e., a VH that is primarily responsible for antigen specificity), see Yoshinaga et al., (J. Biochem 143:593-601, published online January 23, 2008). Applicant’s specification and claim 21 disclose all CDRs of the OAcGD2 antibody compound, 8B6 with defined pairings of CDRs 1-3 , see T able 1 spanning pages 12 and 13 . Overall, at the time the invention was made, the level of skill for preparing antibodies and then selecting those antibodies with desired functional properties was high. However, even if a selection procedure was, at the time of the invention, sufficient to enable the skilled artisan to identify antibodies with the recited functional properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad Pharm., Inc. v. Eli Lilly & Co ., 598 F.3d 1336 (Fed. Cir. 2010); see also Centocor Ortho Biotech Inc. v. Abbott Labs ., 97 USPQ2d 1870, 1876 (Fed. Cir. 2011) (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the [7,070,775] patent possessed such an antibody.”) Absent the conserved structure provided by CDRs of a parental antibody in the context of appropriate VH and VL framework sequences, the skilled artisan generally would not be able to visualize or otherwise predict, a priori, what an antibody with a particular set of functional properties would look like structurally. MPEP § 2163 states that a “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. The specification does not provide guidance on which 15 % of amino acid residues and variants within the CDRs can be altered and still retain antigen binding to OAcGD2 , however the claims as written encompass a broad scope of a large number of possible mutations. As noted above, the art generally accepted that the combination of the CDRs were essential for binding specificity. But the specification does not describe what residues within the CDRs confer the binding activity claimed. Accordingly, the skilled artisan would not be able to discern a structure/function correlation for antibodies other than those comprising 100% to the CDRs instantly claimed. Although Applicants may argue that it is possible to screen for antibodies which can bind to serum albumin, however the court found in ( Rochester v. Searle , 358 F.3d 916, Fed Cir., 2004) that screening assays are not sufficient to provide adequate written description for an invention because they are merely a wish or plan for obtaining the claimed chemical invention. “As we held in Lilly , “[a]n adequate written description of a DNA … ‘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.” 119 F.3d at 1566 (quoting Fiers , 984 F.2d at 1171). For reasons stated above, that requirement applies just as well to non-DNA (or RNA) chemical inventions.” In view of the prior art teaching, mentioned above, that variations within the CDRs render antigen binding unpredictable, one of skill in the art would conclude that applicant was not in possession of the structural attributes of a representative number of species possessed by the members of the genera of variant single domain variable antibodies recited in the instant claims. One of skill in the art would conclude that the specification fails to disclose a representative number of species to describe the claimed genera. Applicant is invited to amend the claims to recite 100% identity to both, the VH and VL recited in instant claim 23 and delete “or sequence having a percentage of identity of at least 85% with SEQ ID NO: 7 and SEQ ID NO: 8 ” from said claim and delete “or a variant thereof” from instant claim 24 . The definition of a variant in the instant specification reads on less than 100% identity and therefore alterations within the CDRs. Claim Rejections - 35 USC § 102 5 . The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action: A person shall be entitled to a patent unless – (a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention. 6 . Claim(s) 16-19 , 22 and 28-30 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Gibbs et al., US 2020/0369767 (published November 26, 2020). Gibbs discloses methods of co-administration regimes including an “… immunotherapeutic agent specifically binding to CD47 is an antibody specifically binding to CD47” or “the immunotherapeutic agent specifically binding to SIRPα is an antibody” w ith an “ immunotherapeutic agent that binds an o-acetyl-GD2 ganglioside (O A cGD2) ” , as well as an additional anticancer agent to treat ablation of HSPCs, as well as solid cancers (i.e. breast cancer and small cell lung cancer (SCLC)) , see abstract; page 1, sections 0005; 0009 and 0010 ; page 2, sections 0013 and 0015 ; page 11, section 0082, 2 nd column (col.); page 12, section 0085; sections 0118 and 0119 spanning page 16 and 17; page 17, section 0128; and page 20, section 0155. The immunotherapeutic agent that binds O A cGD2 is a T cell receptor (TCR) or chimeric antigen receptor (CAR) antigen binding domain or the immunotherapeutic agent described herein (e.g., monospecific or multi- specific antibody or antigen-binding fragment thereof or antibody mimetic) than binds a tumor-associated antigen (TAA), such as ganglioside G2 (GD2) and OAcGD2, see page 11, section 0082 ; and page 14, 1 st col., 10 lines from the bottom. The disclosed antibody may be a humanized antibody, see sections 0134 and 0135 spanning pages 17 and 18. The immunotherapeutic agents administered as pharmaceutical compositions may be administered alone or in combination with other ingredients, thereby reading on simultaneously, see page 3, section 0038. The disclosed combination of immunotherapeutic agent s, CD47 antibody or SIRP a antibody with the O A cGD2 antibody may further include chemotherapeutic agents, “ retinoids such as retinoic acid”, see segment V. beginning on page 12, particularly, page 13, 2 nd col. , line 6. Claim Rejections - 35 USC § 103 7 . 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. 8 . Claim(s) 18-30 is/are rejected under 35 U.S.C. 103 as being unpatentable over Gibbs et al., US 2020/0369767 (published November 26, 2020) , and further in view of Terme et al., European Patent Application, EP 3269739 A1 (published 17 January 2018) and Barbas , III, US 2014/0127200 A1 (published May 8, 2014) . Gibbs teaches methods of co-administration regimes including an “… immunotherapeutic agent specifically binding to CD47 is an antibody specifically binding to CD47” or “the immunotherapeutic agent specifically binding to SIRPα is an antibody” w ith an “immunotherapeutic agent that binds an o-acetyl-GD2 ganglioside (O A cGD2) ”, as well as an additional anticancer agent to treat ablation of HSPCs, as well as solid cancers (i.e. breast cancer and small cell lung cancer (SCLC)), see abstract; page 1, sections 0005; 0009 and 0010; page 2, sections 0013 and 0015; page 11, section 0082, 2 nd column (col.); page 12, section 0085; sections 0118 and 0119 spanning page 16 and 17; page 17, section 0128; and page 20, section 0155. The immunotherapeutic agent that binds O A cGD2 is a T cell receptor (TCR) or chimeric antigen receptor (CAR) antigen binding domain or the immunotherapeutic agent described herein (e.g., monospecific or multi-specific antibody or antigen-binding fragment thereof or antibody mimetic) than binds a tumor-associated antigen (TAA), such as ganglioside G2 (GD2) and OAcGD2, see page 11, section 0082 ; and page 14, 1 st col., 10 lines from the bottom. The taught antibody may be a humanized antibody, see sections 0134 and 0135 spanning pages 17 and 18. The immunotherapeutic agents administered as pharmaceutical compositions may be administered alone or in combination with other ingredients, thereby reading on simultaneously, see page 3, section 0038. The taught combination of immunotherapeutic agent s, CD47 antibody or SIRP a antibody with the OAcGD2 antibody may further include chemotherapeutic agents, “retinoids such as retinoic acid”, see segment V. beginning on page 12, particularly, page 13, 2 nd col., line 6. Gibbs does not teach the anti-O A cGD2 antibody compound that comprises complementary-determining regions (CDRs) set forth in claim 21 and the light chain variable region (VL) with the sequence that is at least 85% sequence identical with Applicant’s SEQ ID NO: 7 and SEQ ID NO: 8 , nor the cancer treated by the said antibody compound in combination with the additional antibodies is neuroblastoma , wherein the combination of antibodies can be administered sequentially, separately but simultaneously, see page 23, section 0276 . Gibbs does not teach the anti-O A cGD2 compound is bispecific and tetravalent comprising at least two antigen binding sites directed to OacGD2 and at least one antigen directed to SIRP a or CD47 . However, Terme teaches the anti-O A cGD2 antibody compound comprising the same CDR sequences as Applicant’s cited in claim 21 , and VL and VH having at least 85% sequence identity to SEQ ID NO: 7 and SEQ ID NO: 8, respectively and a humanized antibody , see sequence alignment at close of rejection ; and page 2, sections 0006 and 0007 . Terme also teaches the sequences that share 100% sequence identity with Applicant’s heavy chain variable region (VH) sequences for SEQ ID NO: 9, SEQ ID NO: 10 , SEQ ID NO: 13, SEQ ID NO: 14 , as well as variants of SEQ ID NO: 11, SEQ ID NO: 12 , SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19. Terme teaches a bispecific antibody that has binding specificity for two targets, see section 0048 spanning pages 6 and 7. Terme further teaches the O A cGD2 ganglioside is expressed by neuroblastoma , as well as breast cancer and small cell lung cancer, see page 8, sections 0065; and page 9, sections 0073 and 0077. It would have been obvious to one of ordinary skill in the art at the effective filing date of the claimed invention to substitute the anti-O A cGD2 antibody of Gibbs with the anti- O A cGD2 antibody compound of Terme with known structure given it has successfully targeted the OacGD2 antigen for treatment of cancers expressing the O A cGD2 ganglioside , see the abstract; page 3, sections 0009, 0012, 0013; and entire document. Moreover, it would have been obvious to manufacture multispecific antibody with binding specificity for O A cGD2 and either, SIRP a or CD47 as presented in the art. One of ordinary skill in the art would have been motivated to do so with a reasonable expectation of success by teachings in Terme that the target of the antibodies with known CDRs are art recognized as a plausible alternative , as well as the antibody within a pharmaceutical composition is suitable for intravenous administration for cancer therapy, see page 7, sections 0049-0053 ; page 8, sections 0064, 0065, 0071; and page 9, section 0073 . Furthermore, one of ordinary skill in the art would have motivated to manufacture the multispecific antibody as it is art known they are able to target to molecules for the enhancement of effective treatment of cancers expressing a multitude of targets and/or antigens. Additionally, Barbas , III teaches therapeutic compositions comprising multispecific and/or multivalent molecule that target two or more cancer targets simultaneously to treat cancer, see Figures 1 and 2; page 1, section 0012 ; page 4, section 0031; sections 0065-0067 spanning pages 6 and 7; page 10, section 0127; and page 19, sections 0225, 0227 . It would have been obvious to one of ordinary skill in the art at the effective filing date of the claimed invention to manufacture bispecific tetravalent antibodies with modular recognition domains (MRDs) able to target the antibodies to O A cGD2 and SIRP a or CD47 to treat cancer, see abstract and entire document. One of ordinary skill in the art would have been motivated to do so with a reasonable expectation of success by teachings in Barbas , III that this technology and method of making antibodies containing one or MDR s will have “…superior drug properties with substantially reduced production costs as compared to conventional bispecific antibodies and combinations of monoclonal antibodies.”, see page 4, section 0032. RESULT 4 from 1fus2fus3fus.aling450.rag database. BEW79471 (NOTE: this sequence has 1 duplicate in the database searched. See complete list at the end of this report) ID BEW79471 standard; protein; 119 AA. XX AC BEW79471; XX DT 08-MAR- 2018 ( first entry) XX DE Humanized anti-OAcGD2 antibody heavy chain variable region, SEQ 70. XX KW OAcGD2 protein; antibody therapy; cancer; cytostatic; diagnostic test; KW glioma; heavy chain variable region; humanized antibody; neuroblastoma; KW neuroprotective; ophthalmological; prophylactic to disease; KW retinoblastoma; therapeutic; tumor marker. XX OS Mus musculus. OS Synthetic. XX CC PN EP3269739-A1. XX CC PD 17-JAN-2018. XX CC PF 15-JUL-2016; 2016EP-00001564. XX PR 15-JUL-2016; 2016EP-00001564. XX CC PA ( OGDT-) OGD2 PHARMA. XX CC PI Terme M, Le Doussal J, Dorvillius M, Assouline B; XX DR WPI; 2018-04937Q/08. XX CC PT New humanized antibody against O-acetylated GD2 ganglioside (OAcGD2), CC PT useful for preventing and/or treating cancer expressing the OAcGD2 CC PT ganglioside, e.g. neuroblastoma, glioma, and retinoblastoma. XX CC PS Example; SEQ ID NO 70; 122pp; English. XX CC The present invention relates to a novel humanized antibody against O- CC acetylated GD2 ganglioside (OAcGD2) useful for preventing and/or treating CC cancer. The invention further relates to: (1) a method for diagnosing a CC cancer expressing the OAcGD2 ganglioside in a subject; and (2) a kit for CC diagnosing a cancer expressing the OAcGD2 ganglioside in a subject. The CC cancer chosen from neuroblastoma, glioma, retinoblastoma. The present CC sequence is a humanized anti-OAcGD2 antibody heavy chain variable region, CC used in the invention for preventing and/or treating cancer. XX SQ Sequence 119 AA; Query Match 83.8 %; Score 131.5; Length 119; Best Local Similarity 33.7%; Matches 28; Conservative 0; Mismatches 0; Indels 55; Gaps 2; Qy 1 EFTFTDYY-----------------IRNRANGYTT------------------------- 18 |||||||| |||||||||| Db 26 EFTFTDYYMTWVRQPPRKALEWLGFIRNRANGYTTEYNPSVKGRFTISRDNSQSIAYLQM 85 Qy 19 -------------ARVSNWAFDY 28 |||||||||| Db 86 NTLRTEDSATYYCARVSNWAFDY 108 RESULT 1 from 4 fus 5 fus 6 fus.aling450.rag database. BEW79488 (NOTE: this sequence has 1 duplicate in the database searched. See complete list at the end of this report) ID BEW79488 standard; protein; 112 AA. XX AC BEW79488; XX DT 08-MAR- 2018 ( first entry) XX DE Humanized anti-OAcGD2 antibody light chain variable region, SEQ 87. XX KW OAcGD2 protein; antibody therapy; cancer; cytostatic; diagnostic test; KW glioma; humanized antibody; light chain variable region; neuroblastoma; KW neuroprotective; ophthalmological; prophylactic to disease; KW retinoblastoma; therapeutic; tumor marker. XX OS Mus musculus. OS Synthetic. XX CC PN EP3269739-A1. XX CC PD 17-JAN-2018. XX CC PF 15-JUL-2016; 2016EP-00001564. XX PR 15-JUL-2016; 2016EP-00001564. XX CC PA ( OGDT-) OGD2 PHARMA. XX CC PI Terme M, Le Doussal J, Dorvillius M, Assouline B; XX DR WPI; 2018-04937Q/08. XX CC PT New humanized antibody against O-acetylated GD2 ganglioside (OAcGD2), CC PT useful for preventing and/or treating cancer expressing the OAcGD2 CC PT ganglioside, e.g. neuroblastoma, glioma, and retinoblastoma. XX CC PS Example; SEQ ID NO 87; 122pp; English. XX CC The present invention relates to a novel humanized antibody against O- CC acetylated GD2 ganglioside (OAcGD2) useful for preventing and/or treating CC cancer. The invention further relates to: (1) a method for diagnosing a CC cancer expressing the OAcGD2 ganglioside in a subject; and (2) a kit for CC diagnosing a cancer expressing the OAcGD2 ganglioside in a subject. The CC cancer chosen from neuroblastoma, glioma, retinoblastoma. The present CC sequence is a humanized anti-OAcGD2 antibody light chain variable region, CC used in the invention for preventing and/or treating cancer. XX SQ Sequence 112 AA; Query Match 79.5 %; Score 97.8; Length 112; Best Local Similarity 31.6%; Matches 24; Conservative 0; Mismatches 0; Indels 52; Gaps 2; Qy 1 QSLLKNNGNTFL----------------KVS----------------------------- 15 |||||||||||| ||| Db 27 QSLLKNNGNTFLSWYLQKSGQSPKLLIYKVSNRLSGVPDRFSGSGSGTYFTLKISRVEAE 86 Qy 16 -------SQSTHIPYT 24 ||||||||| Db 87 DLGVYFCSQSTHIPYT 102 RESULT 1 from 7.rag database. BEW79446 (NOTE: this sequence has 2 duplicates in the database searched. See complete list at the end of this report) ID BEW79446 standard; protein; 112 AA. XX AC BEW79446; XX DT 08-MAR- 2018 ( first entry) XX DE Humanized anti-OAcGD2 antibody light chain variable region, SEQ 45. XX KW OAcGD2 protein; antibody therapy; cancer; cytostatic; diagnostic test; KW glioma; humanized antibody; light chain variable region; neuroblastoma; KW neuroprotective; ophthalmological; prophylactic to disease; KW retinoblastoma; therapeutic; tumor marker. XX OS Mus musculus. OS Synthetic. XX CC PN EP3269739-A1. XX CC PD 17-JAN-2018. XX CC PF 15-JUL-2016; 2016EP-00001564. XX PR 15-JUL-2016; 2016EP-00001564. XX CC PA ( OGDT-) OGD2 PHARMA. XX CC PI Terme M, Le Doussal J, Dorvillius M, Assouline B; XX DR WPI; 2018-04937Q/08. XX CC PT New humanized antibody against O-acetylated GD2 ganglioside (OAcGD2), CC PT useful for preventing and/or treating cancer expressing the OAcGD2 CC PT ganglioside, e.g. neuroblastoma, glioma, and retinoblastoma. XX CC PS Claim 3; SEQ ID NO 45; 122pp; English. XX CC The present invention relates to a novel humanized antibody against O- CC acetylated GD2 ganglioside (OAcGD2) useful for preventing and/or treating CC cancer. The invention further relates to: (1) a method for diagnosing a CC cancer expressing the OAcGD2 ganglioside in a subject; and (2) a kit for CC diagnosing a cancer expressing the OAcGD2 ganglioside in a subject. The CC cancer chosen from neuroblastoma, glioma, retinoblastoma. The present CC sequence is a humanized anti-OAcGD2 antibody light chain variable region, CC used in the invention for preventing and/or treating cancer. XX SQ Sequence 112 AA; Query Match 88.5 %; Score 269; Length 112; Best Local Similarity 50.9%; Matches 56; Conservative 0; Mismatches 54; Indels 0; Gaps 0; Qy 3 VMTQSPXXLXXXXGXXXXXXCRXSQSXXKXXXXXXLXWXXQXPGXXPXXLIYXXSXRXXG 62 |||||| | | || ||| | | | | || | ||| | | | Db 3 VMTQSPATLSLSPGERATLSCRSSQSLVKNQANTYLHWYQQKPGQAPRLLIYKVSNRLTG 62 Qy 63 XPXRFSGSGSGTXFTLXIXXXXXEDXXXYXCXQXXXXXYTFGXGTKVEIK 112 | ||||||||| ||| | || | | | |||| ||||||| Db 63 IPARFSGSGSGTDFTLTISSLQAEDFAVYYCSQSTHIPYTFGGGTKVEIK 112 RESULT 1 from 8.rag database. BEW79443 (NOTE: this sequence has 2 duplicates in the database searched. See complete list at the end of this report) ID BEW79443 standard; protein; 119 AA. XX AC BEW79443; XX DT 08-MAR- 2018 ( first entry) XX DE Humanized anti-OAcGD2 antibody heavy chain variable region, SEQ 42. XX KW OAcGD2 protein; antibody therapy; cancer; cytostatic; diagnostic test; KW glioma; heavy chain variable region; humanized antibody; neuroblastoma; KW neuroprotective; ophthalmological; prophylactic to disease; KW retinoblastoma; therapeutic; tumor marker. XX OS Mus musculus. XX CC PN EP3269739-A1. XX CC PD 17-JAN-2018. XX CC PF 15-JUL-2016; 2016EP-00001564. XX PR 15-JUL-2016; 2016EP-00001564. XX CC PA ( OGDT-) OGD2 PHARMA. XX CC PI Terme M, Le Doussal J, Dorvillius M, Assouline B; XX DR WPI; 2018-04937Q/08. XX CC PT New humanized antibody against O-acetylated GD2 ganglioside (OAcGD2), CC PT useful for preventing and/or treating cancer expressing the OAcGD2 CC PT ganglioside, e.g. neuroblastoma, glioma, and retinoblastoma. XX CC PS Claim 4; SEQ ID NO 42; 122pp; English. XX CC The present invention relates to a novel humanized antibody against O- CC acetylated GD2 ganglioside (OAcGD2) useful for preventing and/or treating CC cancer. The invention further relates to: (1) a method for diagnosing a CC cancer expressing the OAcGD2 ganglioside in a subject; and (2) a kit for CC diagnosing a cancer expressing the OAcGD2 ganglioside in a subject. The CC cancer chosen from neuroblastoma, glioma, retinoblastoma. The present CC sequence is a humanized anti-OAcGD2 antibody heavy chain variable region, CC used in the invention for preventing and/or treating cancer. XX SQ Sequence 119 AA; Query Match 95.4 %; Score 432; Length 119; Best Local Similarity 69.5%; Matches 82; Conservative 0; Mismatches 36; Indels 0; Gaps 0; Qy 2 VQLXESGGGLVXPGXSLRLSCXXSXFTFXDXYMXWXRQAPGKGLEWXXXXRNXXXXXXXX 61 ||| ||||||| || |||||| | ||| | || | |||||||||| || Db 2 VQLVESGGGLVQPGRSLRLSCTASEFTFTDYYMTWVRQAPGKGLEWLGFIRNRANAYTTE 61 Qy 62 YXXSVKGRFTISRDXXKXXXYLQMNSLXXEDTAXYYCXRVSNWXFDYWGQGTXXTVSS 119 | ||||||||||| | ||||||| |||| ||| ||||| |||||||| |||| Db 62 YAASVKGRFTISRDNSKSILYLQMNSLKTEDTAVYYCARVSNWAFDYWGQGTLVTVSS 119 RESULT 1 from 9.rag database. BEW79405 (NOTE: this sequence has 4 duplicates in the database searched. See complete list at the end of this report) ID BEW79405 standard; protein; 119 AA. XX AC BEW79405; XX DT 08-MAR- 2018 ( first entry) XX DE Humanized anti-OAcGD2 antibody heavy chain variable region, SEQ 4. XX KW OAcGD2 protein; antibody therapy; cancer; cytostatic; diagnostic test; KW glioma; heavy chain variable region; humanized antibody; neuroblastoma; KW neuroprotective; ophthalmological; prophylactic to disease; KW retinoblastoma; therapeutic; tumor marker. XX OS Mus musculus. OS Synthetic. XX CC PN EP3269739-A1. XX CC PD 17-JAN-2018. XX CC PF 15-JUL-2016; 2016EP-00001564. XX PR 15-JUL-2016; 2016EP-00001564. XX CC PA ( OGDT-) OGD2 PHARMA. XX CC PI Terme M, Le Doussal J, Dorvillius M, Assouline B; XX DR WPI; 2018-04937Q/08. XX CC PT New humanized antibody against O-acetylated GD2 ganglioside (OAcGD2), CC PT useful for preventing and/or treating cancer expressing the OAcGD2 CC PT ganglioside, e.g. neuroblastoma, glioma, and retinoblastoma. XX CC PS Example; SEQ ID NO 4; 122pp; English. XX CC The present invention relates to a novel humanized antibody against O- CC acetylated GD2 ganglioside (OAcGD2) useful for preventing and/or treating CC cancer. The invention further relates to: (1) a method for diagnosing a CC cancer expressing the OAcGD2 ganglioside in a subject; and (2) a kit for CC diagnosing a cancer expressing the OAcGD2 ganglioside in a subject. The CC cancer chosen from neuroblastoma, glioma, retinoblastoma. The present CC sequence is a humanized anti-OAcGD2 antibody heavy chain variable region, CC used in the invention for preventing and/or treating cancer. XX SQ Sequence 119 AA; Query Match 100.0 %; Score 636; Length 119; Best Local Similarity 100.0%; Matches 119 ; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 EVQLVESGGGLVQPGRSLRLSCTTSEFTFTDYYMTWVRQAPGKGLEWLGFIRNRANGYTT 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 EVQLVESGGGLVQPGRSLRLSCTTSEFTFTDYYMTWVRQAPGKGLEWLGFIRNRANGYTT 60 Qy 61 EYNPSVKGRFTISRDNSKSILYLQMNSLKTEDTAVYYCARVSNWAFDYWGQGTLVTVSS 119 ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 EYNPSVKGRFTISRDNSKSILYLQMNSLKTEDTAVYYCARVSNWAFDYWGQGTLVTVSS 119 Conclusion 9 . Any inquiry concerning this communication or earlier communications from the E xaminer should be directed to FILLIN "Examiner name" \* MERGEFORMAT ALANA HARRIS DENT whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-0831 . The E xaminer works a flexible schedule, however can generally be reached between 8AM-8PM, Monday through Friday . 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 E xaminer by telephone are unsuccessful, the E xaminer’s supervisor, FILLIN "SPE Name?" \* MERGEFORMAT Julie Wu can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT 571-272-5205 . 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. FILLIN "Examiner Stamp" \* MERGEFORMAT ALANA HARRIS DENT Primary Examiner Art Unit 1643 24 March 2026
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Prosecution Timeline

Oct 12, 2023
Application Filed
Mar 26, 2026
Non-Final Rejection — §102, §103, §112 (current)

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Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

1-2
Expected OA Rounds
44%
Grant Probability
77%
With Interview (+32.6%)
3y 11m
Median Time to Grant
Low
PTA Risk
Based on 730 resolved cases by this examiner. Grant probability derived from career allow rate.

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