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 1-11, 17-20, 22 and 23 are pending.
Claims 22 and 23, drawn to non-elected claims are not examined.
Claim 1 has been amended.
Claims 12-16 and 21 have been cancelled.
Claims 1-11 and 17-20 are examined on the merits with elected species (antigen components): all the components identified as (a)-(e), SEQ ID NO: 40.
Withdrawn Objection
Specification
3. The disclosure is no longer objected to because the embedded hyperlink and/or other form of browser-executable code has been deleted, see In the Specification, page 22, lines 10-16.
Withdrawn Grounds of Rejection
Claim Rejections - 35 USC § 112
4. The rejection of claim 21 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or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in light of the cancellation of the claim, see In the Claims, page 7.
Claim Interpretation
5. 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.
6. The claims 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.
7. This application includes one or more claim limitations that do not use the word “means,” but are nonetheless being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, because the claim limitation(s) uses a generic placeholder that is coupled with functional language without reciting sufficient structure to perform the recited function and the generic placeholder is not preceded by a structural modifier. Such claim limitation(s) is/are: "configured to” in claim 1 (lines 2 and 4). Applicant’s Remarks submitted June 30, 2026 does not set forth any response to the interpretation, see Remarks submitted June 30, 2026.
Because this/these claim limitation(s) is/are being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, it/they is/are being interpreted to cover the corresponding structure described in the specification as performing the claimed function, and equivalents thereof.
If applicant does not intend 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 avoid it/them being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph (e.g., by reciting sufficient structure to perform the claimed function); or (2) present a sufficient showing that the claim limitation(s) recite(s) sufficient structure to perform the claimed function so as to avoid it/them
being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph.
Maintained Grounds of Rejection
Claim Rejections - 35 USC § 112
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. The rejection of claims 1-11 and 17-20 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 is maintained. Claims 12-16 and 21 have been cancelled.
Applicant recites the tenets required to satisfy the written description requirement under the first paragraph of 35 U.S.C. 112, see Remarks submitted June 30, 2026, pages 8-10.
Applicant asserts with the amendment to “…claim 1 to recite specific sequences (SEQ ID NOs) which comprise each domain of the antigen component, providing the structural specificity required to demonstrate possession of the claimed invention.”, see Remarks submitted June 30, 2026, page 9, paragraphs (paras.) 1-3; and page 10, 1st full paragraph (para.).
Applicant points out Tables 1 and 2 spanning pages 70-74 within the Specification, as well as Examples 1-6 spanning pages 50-62 and Figures 4A-18, see Remarks, page 9, 2nd and 3rd paras; and para. spanning pages 9 and 10. Applicant asserts “[t]he Specification…demonstrates the structure-function relationship between the specific domain combinations and the ability to bind and deplete PLA2R-specific antibodies.”, see last sentence on page 9 of the Remarks.
Applicant’s arguments, points of view and noted passages and Figures have been carefully considered, but fail to persuade.
While Applicant has amended claim 1 to recite a host of sequences that read on domains within the antigen component of the macromolecule, there is no evidence the innumerable and possible parts, fragments and pieces of the antigen components comprised within the macromolecule are able to facilitate the function cited in claim 1. The claim reads on parts of each of the domain and no limitations on the amino acids that define a part of each domain. Accordingly, the rejection is maintained for the reasons cited herein.
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.
As stated previously, the claims read on a macromolecule that depletes phospholipase A2 receptor (PLA2R)-specific antibodies from an individual’s serum, said macromolecule comprises a targeting component that is configured to bind to an internalizing cell surface receptor or other internalized cell surface molecule, and an antigen component that is configured to bind to a PLA2R-specific antibody, wherein the antigen component comprises a. at least part of each domain, the cysteine rich (CysR), fibronectin (FN), C-type lectin domain 1 (CTLD1), C-type lectin domain 7 (CTLD7) and C-type lectin domain 8 (CTLD8) domain of PLA2R, or a sequence 90% identical thereto, as well as mutations within the Fc fragment.
The written description in this instant case does not set forth a plethora of macromolecules comprising undefined and uncharacterized targeting components that bind internalizing cell surface receptor(s)/molecule(s), as well as parts of antigen components that too are undefined and uncharacterized. This plethora of macromolecules have not been fully defined and characterized. While the claims cite the antigen component has five components and at least part of each of the five domains there is no evidence or showing of any of the macromolecules that comprise a targeting component and an antigen component or parts of the said components.
The written description is not commensurate in scope with the plethora of macromolecules comprising a targeting component and an antigen component configured to bind to a PLA2R-specific antibody. The instant application does not provide sufficient guidance as to the nexus or correlation between the structure and function of the targeting component and antigen component comprised within the macromolecule. The macromolecules of record seem to be solely characterized by art known structures. There are no be no identifying sequences in the independent claim that would evidence Applicant’s written descriptive support for the genus of macromolecules encompassed by the claims. The ability to make the macromolecules essential to the claimed products does not place the skilled artisan in possession of the relevant identifying characteristics of a genus of molecules commensurate in scope with the claimed invention.
The instant application does not provide sufficient guidance as to the nexus or correlation between the structure and function of the macromolecules that places the skilled artisan in possession of the genera of macromolecules in scope with the claimed invention.
In Abbvie v. Centocor (Fed. Cir. 2014), the Court held that a disclosure of many different antibodies (in that case neutralizing antibodies to IL-12 with a particular binding affinity) was not enough to support the genus of all IL-12 neutralizing antibodies because the disclosed antibodies were very closely related to each other in structure and were not representative of the full diversity of the genus. The Court further noted that functionally defined genus claims can be inherently vulnerable to invalidity challenge for lack of written description support especially in technology fields that are highly unpredictable where it is difficult to establish a correlation between structure and function for the whole genus or to predict what would be covered by the functionally claimed genus.
“A sufficient description of a genus . . . 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.” See AbbVie, 759 F.3d at 1297, reiterating Eli Lilly, 119 F.3d at 1568-69.
Vas-Cath Inc. V Mahurkar, 19 U5PQ2d 1111, clearly states that "applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the 'written description' inquiry, whatever is now claimed." (See page 1117). The specification does not "clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed." (See Vas-Cath at page 1116).
Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. 112 is severable from its enablement provision (see page 115).
The skilled artisan cannot envision the detailed structure of the broad class of macromolecules that are remiss of sequences, therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and a reference to a potential method of isolating it. The polypeptide itself is required. See Fiers v. Revel, 25 U5PQ 2d 1601 at 1606 (CAFC1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Lts. 18 U5PQ2d 1016.
Furthermore, In The Reagents of the University of California v. Eli Lilly (43 U5PQ2d 1398-1412), the court held that a generic statement which defines a genus of nucleic acids by only their functional activity does not provide an adequate written description of the genus. The court indicated that while Applicants are not required to disclose every species encompassed by a genus, the description of a genus is achieved by the recitation of a representative number of DNA molecules, usually defined by a nucleotide sequence, falling within the scope of the claimed genus. At section B(l), the court states that "An 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".
At the time the application was filed Applicants do not seem to be in possession of all the members of the genus of macromolecules. Applicant did not have possession of the breadth of these molecules.
The USPTO has released a Memo on the Clarification of Written Description Guidance For Claims Drawn to Antibodies and Status of 2008 Training Materials, 02/22/2018. See https://www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf.
There is insufficient written description of the required kind of structure-identifying information about the corresponding makeup of macromolecule essential to the claimed invention to demonstrate possession that fulfill the requirements of a structure-function relationships of written description. Also, see Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017).
The instant disclosure, including the claims fail to disclose a representative number of species falling with the scope of the genera and/or structural common to the members of the genera so the one of skill in the art can visualize or recognize the members of the genus of macromolecules.
Also, it is not enough for the specification to show how to make and use the invention, i.e., to enable it (see Amgen at page 1361).
An adequate written description must contain enough information about the actual makeup of the claimed products – “a precise definition, such as structure, formula, chemic name, physical properties of other properties, of species falling with the genus sufficient to distinguish the gene from other materials”, which may be present in “functional terminology when the art has established a correlation between structure and function” (Amgen page 1361).
A skilled artisan cannot, as one can do with a fully described genus, visualize or recognize the identity of the members of the genus that exhibit this functional property, i.e., bind different entities.
The specification does not evidence the possession of all the macromolecules that are undefined and uncharacterized falling within the potentially large genus to establish possession. Consequently, Applicant was not in possession of the instant claimed invention. See University of California v. Eli Lilly and Co. 43 U5PQ2d 1398.
The full breadth of the claims does not meet the written description provision of 35 U.S.C. 112, first paragraph.
10. 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.
11. The rejection of claims 1-11 and 17-20 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 is maintained. Claims 12-16 and 21 have been cancelled.
a. Claims 1, 6-8 and 18-20 recites the antigen component of the macromolecule comprises an antigen component comprising “…at least a part of each of the CysR, FN, CTLD1, CTLD7 and CTLD8 domains of PLA2R”, see In the Claims submitted June 30, 2026, claim 1, lines 5 and 6.
Applicant argues claim 1 has been amended to recite “…specific [sequence identifying numbers] that define the structural boundaries of each domain.”, see Remarks submitted June 30, 2026, page 10, 3rd paragraph (para.).
Applicant’s argument has been reviewed and carefully considered, but fails to persuade.
While Applicant has further defined each domain of the antigen component of the macromolecule with a sequence identifying sequence, it remains unclear which amino acids, segment, piece or fragment of each of the domain is able to function and bind a PLA2R-specific antibody to facilitate depleting PLA2R-specific antibodies. Accordingly, the metes and bounds cannot be determined.
Claim Rejections - 35 USC § 103
12. 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.
13. The rejection of claim(s) 1-11 and 17-20 under 35 U.S.C. 103 as being unpatentable over Gutierrez et al., WO 2025/030003 A2 (effective filing date 01 August 2023/ Foreign Patent Documents, IDS reference #12 submitted August 15, 2025), and further in view of Payne et al., WO 2023/015239 A1 (published 09 February 2023/ U.S. Patent Application Publication, IDS reference #8 submitted August 15, 2025) is maintained. Claim 21 has been cancelled.
Applicant argues “…the claimed invention wound not have been obvious to one of ordinary skill in the art.”, see Remarks submitted June 30, 2026, page 11, 2nd paragraph (para.). Applicant follows with required conditions for making a proper case for obviousness and case law supporting these conditions, see pages 11 and 12 of the Remarks.
Applicant asserts claim 1 has been amended “…to recite specific sequences…which comprise each domain of the antigen component.”, see page 12, 3rd para.
In particular, “Applicant submits that, while Gutierrez teaches molecules comprising an autoantibody-binding domain and Fc domains, critically, Gutierrez provides no experimental data whatsoever demonstrating that any of its molecules actually bind to or deplete anti- PLA2R autoantibodies.”, see last full sentence on page 12 of the Remarks. Applicant continues to argue Gutierrez, the primary reference reads on prophetic in vivo examples and its teachings according to Applicant undercut the plausibility of applying their teachings as the skilled artisan would not have a reasonable expectation of success implementing the molecules of Gutierrez.
Applicant cites the teachings of Payne, the secondary reference stating “Payne teaches chimeric autoantibody receptors (CAARs) for cell therapy, not soluble macromolecules with targeting components as claimed. Payne's CAAR technology involves cell surface receptors expressed on engineered T cells for cellular immunotherapy, which is fundamentally different from the soluble macromolecules of the present invention that are administered to patients and function by binding to internalizing cell surface receptors on endogenous cells.
Moreover, the anti-PLA2R targeting molecules taught by Payne lack the specific combination of CysR, FN, CTLD1, CTLD7 and CTLD8 as recited in the present claims.”, see last two paragraphs (paras.) on page 13.
Applicant argues there is “…no motivation to combine Payne's CAAR technology with Gutierrez's soluble molecules”, as there are alleged “structural and functional differences between cell-based therapies and soluble protein therapeutics…”, see para. bridging pages 13 and 14.
Applicant concludes arguments asserting Applicant discovered “[t]he specific domain combination of CysR, FN, CTLD1, CTLD7, and CTLD8…” and macromolecules comprising such “…are more effective in depleting PLAR2R-specific antibodies than macromolecules comprising fewer domains” yielding unobvious and unexpected results., see page 14, 1st full para.
Applicant’s arguments and points of view have been carefully considered, but fail to persuade.
Applicant is reminded that a reference is presumed to be operable. See MPEP 2121.02. Prior art printed publications, like prior art patents are presumptively enabled barring any contrary showing by applicant or patentee and burden shifts to applicant to submit rebuttal evidence of nonenablement. See In re Antor Media Corp., 103 USPQ2d 1555 (Fed. Cir. 2012). A reference is presumed operable until applicant provides facts rebutting the presumption of operability. In re Sasse, 207 USPQ 107 (CCPA 1980). See MPEP 2121, 2121.02.
Applicant is also reminded the claimed invention reads on a product and not a method. Hence, desired method endpoints, desired outcomes and parameters in Applicant's Remarks are moot. Notwithstanding, elected species, SEQ ID NO: 40 is taught by both prior art references, see alignments at close of rejection. The alignments reveal at least part of each domain. Accordingly, the antigen component with at least part of each domain comprised within the macromolecule will bind PLA2R-specific antibodies and deplete PLA2R-specific antibodies. For the reasons of record and herein, the rejection is maintained.
Gutierrez teaches “…a molecule that selectively targets and neutralizes and/or depletes pathogenic autoantibodies in a subject. Molecules described herein comprise a first polypeptide and a second polypeptide, wherein the first polypeptide comprises an autoantibody-binding domain and a first Fc domain and the second polypeptide comprises a second Fc domain.”, see page 1, sections 0003 and 0004. “For example, a PLA2R autoantigen domain (or a fragment or variant thereof) may be used in a molecule in order to target anti-PLA2R, wherein the “…autoantigen domain includes a PLA2R, or a fragment or variant thereof. PLA2R protein includes a cysteine-rich (CysR) domain, a fibronectin type II (FnII) domain, 8 sequential C- type lectin domains (CTLDs), and an intracellular C-terminal tail.”
“Challenges exist in producing heterodimerized Fc domains of two different polypeptides from a single composition, particularly because the random pairing of different polypeptides can yield undesired species…One approach to solve the problem of mispaired byproducts is known as “knob-into-holes technology” (KIH), which aims to force the pairing of two different polypeptides containing Fc domains by ntroducing mutations into the CH3 regions of the Fc domains to modify the contact interface.”, see page 109, section 0282. “As described herein, a first and/or second Fc domain in a molecule described herein may comprise certain mutations that utilize KIH technology that include, but are not limited to, a CH3 modification. In some embodiments, a molecule comprises first and second Fc domains that form a heterodimer using knobs-in-holes (KIH) modifications… In some embodiments, a KIH mutation comprises T366W, S354C, T366S, L368A, Y407V, and Y349C, according to the EU numbering scheme. In some embodiments, the first Fc domain comprises the T366W and S354C mutations and the second Fc domain comprises the T366S, L368A, Y407V, and Y349C mutations. In some embodiments, the first Fc domain comprises the T366S, L368A, Y407V, and Y349C mutations and the second Fc domain comprises the T366W and S354C mutations.”, see page 110, section 0284.
“In some embodiments, the autoantibody-binding domain is covalently linked to the first Fc domain through a linker. In some embodiments, the linker comprises the amino acid sequence of SEQ ID NO: 150 (GGGGS),”, see page 8, section 0035.
Gutierrez does not the macromolecule has a targeting component and the PLA2R autoantigen has a fibronectin domain (FN) and a CTLD8 domain. Gutierrez does not teach the macromolecule, wherein at least part of the CysR, FN and CTLD1 domains are linked to at least part of the CTLD7 and CTLD8 by a Ser-Gly (SG) linker peptide.
However, Payne teaches a chimeric autoantibody receptor (CAAR) specific comprising PLA2R autoantigen comprising an extended cysteine rich (eCysR) domain further comprising a fibronectin type II (FNII) domain, a C-type lectin domain (CTLD1), a C-type lectin domain 7 (CTLD7) and a C-type lectin domain 8 (CTLD8) in a N-terminal to C-terminal orientation, see page 4. “In some embodiments, the extracellular domain of the CAAR further comprises a C-terminal glycine-serine (GS) linker.”, see paragraph (para.) bridging pages 27 and 28.
It would not be outside the scope of the skilled artisan to substitute the fibronectin type I with the fibronectin type II domain. It is obvious to those skilled in the art to substitute one known equivalent for another. See In re Omeprazole Patent Litigation, 483 F.3d 1364, 1374 (Fed. Cir. 2007) (“[T]his court finds no . . . error in [the] conclusion that it would have been obvious to one skilled in the art to substitute one ARC [alkaline reactive compound] for another.”).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to implement CTLD8 domain and the GS linker in the antigen component.
One of ordinary skill in the art would have been motivated to do so with a reasonable expectation of success by teachings in all the references and in particular, Payne.
It also would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine the teachings of the references to effectively assemble the molecule in the manner set forth in the claims given they are easily manufactured, see all references in their entireties.
RESULT 1 from 40.rag database.
BQU95509
ID BQU95509 standard; protein; 835 AA.
AC BQU95509;
DT 03-APR-2025 (first entry)
XX
DE human PLA2R-hIgG1 Fc knob protein construct, SEQ 269.
XX
KW Immunoglobulin G1; Immunoglobulin gamma 1; PLA2R protein;
KW antiinflammatory; autoimmune disease; fusion protein; immunosuppressive;
KW membranous glomerulonephritis; mutein; nephrotropic;
KW phospholipase A2 receptor; protein production; protein therapy;
KW therapeutic; uropathic.
XX
OS Homo sapiens.
OS Synthetic.
XX
CC PN WO2025030003-A2.
XX
CC PD 06-FEB-2025.
XX
CC PF 01-AUG-2024; 2024WO-US040519.
XX
PR 01-AUG-2023; 2023US-0517104P.
XX
CC PA (MERI-) MERIDA BIOSCI INC.
XX
CC PI Gutierrez DA, Logtenberg MEW, Capili AD;
XX
DR WPI; 2025-13587A/020.
XX
CC PT New molecule comprising polypeptides having first Fc domain and second Fc
CC PT domain forming homodimer or heterodimer of first polypeptide and second
CC PT polypeptide, used to treat autoimmune disease e.g. membranous
CC PT nephropathy.
XX
CC PS Claim 107; SEQ ID NO 269; 349pp; English.
XX
CC The present invention relates to a novel molecule, useful for treating
CC autoimmune disease. The molecule comprises: (a) a first polypeptide
CC containing a first Fc domain and an autoantibody-binding domain that
CC binds to anti-PLA2R (phospholipase A2 receptor) autoantibodies; and (b) a
CC second polypeptide containing a second Fc domain, where the first Fc
CC domain and the second Fc domain form a homodimer or heterodimer of the
CC first polypeptide and the second polypeptide. The invention further
CC claims: (1) a nucleic acid comprising a nucleotide sequence encoding the
CC molecule; (2) a host cell containing the nucleic acid; (3) a vector
CC comprising the nucleic acid; (4) a pharmaceutical composition comprising
CC the molecule; (5) a method for making the molecule; (6) a method for
CC treating a subject suffering from or susceptible to an autoimmune disease
CC ; (7) a method for selectively depleting anti-PLA2R autoantibodies in the
CC subject; (8) a method for treating a human subject suffering from or
CC susceptible to membranous nephropathy; (9) a composition for decreasing
CC the titer of the anti-PLA2R autoantibodies in the blood serum of the
CC subject; and (10) an immune complex comprising the anti-PLA2R
CC autoantibody. The molecule is useful for controlling autoimmune response
CC and treating a subject suffering from or susceptible to autoimmune
CC disease, preferably membranous nephropathy (MN).
XX
SQ Sequence 835 AA;
Query Match 69.2%; Score 3320; Length 835;
Best Local Similarity 96.1%;
Matches 596; Conservative 5; Mismatches 9; Indels 10; Gaps 2;
Qy 251 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 310
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 60
Qy 311 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 370
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 120
Qy 371 ICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWG 430
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 ICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWG 180
Qy 431 FCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 490
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 FCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 240
Qy 491 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 550
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 300
Qy 551 PSAWRSRDCESTLPYICKKYLN-------SGNTSDMYPMPNTLEYGNRTYKIINANMTWY 603
|||||||||||||||||||||| |||||||||||||||||||||||||||||
Db 301 PSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDMYPMPNTLEYGNRTYKIINANMTWY 360
Qy 604 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 663
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 420
Qy 664 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 723
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 480
Qy 724 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 783
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 540
Qy 784 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 843
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 600
Qy 844 CKMNUCLEOTIDESEQUENC 863
||| :: |:: : |
Db 601 CKME---PKSSDKTHTCPPC 617
RESULT 2 from 40.rag database.
BQU79881
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
ID BQU79881 standard; protein; 854 AA.
AC BQU79881;
DT 03-APR-2025 (first entry)
XX
DE Human PLA2R-human IgG1 Fc knob mutant construct, SEQ 181.
XX
KW IgG1; Immunoglobulin G1; Immunoglobulin gamma 1;
KW M-type phospholipase A2 receptor; PLA2R protein; antibody neutralization;
KW autoimmune disease; fusion protein; immunosuppressive; mutein;
KW protein production; protein therapy; therapeutic.
XX
OS Homo sapiens.
OS Chimeric.
OS Synthetic.
OS Unidentified.
XX
CC PN WO2025030009-A1.
XX
CC PD 06-FEB-2025.
XX
CC PF 01-AUG-2024; 2024WO-US040527.
XX
PR 01-AUG-2023; 2023US-0517101P.
PR 01-AUG-2023; 2023US-0517104P.
XX
CC PA (MERI-) MERIDA BIOSCI INC.
XX
CC PI Gutierrez DA, Logtenberg MEW, Capili AD;
XX
DR WPI; 2025-13496A/017.
XX
CC PT New molecule comprising first polypeptide having first Fc domain and
CC PT binding domain that binds specifically to target antibody, and second
CC PT polypeptide having second Fc domain, used to treat autoimmune disease.
XX
CC PS Example 2; SEQ ID NO 181; 267pp; English.
XX
CC The present invention relates to a novel molecule, useful for treating
CC autoimmune disease. The molecule comprises: a first polypeptide
CC comprising a first Fc domain and a binding domain that binds specifically
CC to a target antibody; and a second polypeptide comprising a second Fc
CC domain; where the first Fc domain and the second Fc domain form a
CC homodimer or heterodimer of the first polypeptide and the second
CC polypeptide, and where the first and/or second Fc domain comprises one or
CC more mutated amino acid residues and has increased binding affinity to Fc
CC gamma RIIB relative to a corresponding wild-type Fc domain; and where
CC upon binding of two molecules to the target antibody, an immune complex
CC is formed that has enhanced binding kinetics with Fc gamma RIIB relative
CC to an immune complex that comprises the target antibody bound to two
CC corresponding molecules with wild-type Fc domains. The invention also
CC provides: a nucleic acid comprising a nucleotide sequence encoding the
CC molecule; a host cell containing the nucleic acid; a vector comprising
CC the nucleic acid; an immune complex comprising (i) a target antibody, and
CC (ii) two molecules; a method for making a molecule; a method for reducing
CC antibody titer of a circulating target antibody in a subject diagnosed
CC with an autoimmune disease; a method for treating a subject suffering
CC from or susceptible to an autoimmune disease; and a method for decreasing
CC the titer of a target antibody in the blood serum of a subject in need
CC the composition. The autoimmune disease is Graves' Disease, type 1
CC diabetes, rheumatoid arthritis, systemic lupus erythematosus,
CC inflammatory bowel disease, pre-eclampsia, multiple sclerosis, and
CC vasculitis; and controlling immune response. The molecule: bounds to a
CC target autoantibody may target ASGPR on hepatocytes and binding to ASGPR
CC will cause internalization of the complex (that is removal of target
CC autoantibodies); and shows improved efficacy in treating autoimmune
CC disease. The method and composition that allow for selective depletion
CC and/or neutralization of pathogenic antibodies.
XX
SQ Sequence 854 AA;
Query Match 69.2%; Score 3320; Length 854;
Best Local Similarity 96.1%;
Matches 596; Conservative 5; Mismatches 9; Indels 10; Gaps 2;
Qy 251 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 310
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 20 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 79
Qy 311 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 370
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 80 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 139
Qy 371 ICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWG 430
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 140 ICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWG 199
Qy 431 FCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 490
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 200 FCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 259
Qy 491 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 550
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 260 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 319
Qy 551 PSAWRSRDCESTLPYICKKYLN-------SGNTSDMYPMPNTLEYGNRTYKIINANMTWY 603
|||||||||||||||||||||| |||||||||||||||||||||||||||||
Db 320 PSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDMYPMPNTLEYGNRTYKIINANMTWY 379
Qy 604 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 663
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 380 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 439
Qy 664 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 723
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 440 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 499
Qy 724 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 783
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 500 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 559
Qy 784 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 843
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 560 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 619
Qy 844 CKMNUCLEOTIDESEQUENC 863
||| :: |:: : |
Db 620 CKME---PKSSDKTHTCPPC 636
RESULT 3 from 40.rag database.
BQU79797
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
ID BQU79797 standard; protein; 603 AA.
XX
AC BQU79797;
XX
DT 03-APR-2025 (first entry)
XX
DE Human PLA2R protein mutant, SEQ 23.
XX
KW M-type phospholipase A2 receptor; PLA2R protein; antibody neutralization;
KW antigen; autoimmune disease; immunosuppressive; mutein;
KW protein production; protein therapy; therapeutic.
XX
OS Homo sapiens.
XX
CC PN WO2025030009-A1.
XX
CC PD 06-FEB-2025.
XX
CC PF 01-AUG-2024; 2024WO-US040527.
XX
PR 01-AUG-2023; 2023US-0517101P.
PR 01-AUG-2023; 2023US-0517104P.
XX
CC PA (MERI-) MERIDA BIOSCI INC.
XX
CC PI Gutierrez DA, Logtenberg MEW, Capili AD;
XX
DR WPI; 2025-13496A/017.
XX
CC PT New molecule comprising first polypeptide having first Fc domain and
CC PT binding domain that binds specifically to target antibody, and second
CC PT polypeptide having second Fc domain, used to treat autoimmune disease.
XX
CC PS Example 2; SEQ ID NO 23; 267pp; English.
XX
CC The present invention relates to a novel molecule, useful for treating
CC autoimmune disease. The molecule comprises: a first polypeptide
CC comprising a first Fc domain and a binding domain that binds specifically
CC to a target antibody; and a second polypeptide comprising a second Fc
CC domain; where the first Fc domain and the second Fc domain form a
CC homodimer or heterodimer of the first polypeptide and the second
CC polypeptide, and where the first and/or second Fc domain comprises one or
CC more mutated amino acid residues and has increased binding affinity to Fc
CC gamma RIIB relative to a corresponding wild-type Fc domain; and where
CC upon binding of two molecules to the target antibody, an immune complex
CC is formed that has enhanced binding kinetics with Fc gamma RIIB relative
CC to an immune complex that comprises the target antibody bound to two
CC corresponding molecules with wild-type Fc domains. The invention also
CC provides: a nucleic acid comprising a nucleotide sequence encoding the
CC molecule; a host cell containing the nucleic acid; a vector comprising
CC the nucleic acid; an immune complex comprising (i) a target antibody, and
CC (ii) two molecules; a method for making a molecule; a method for reducing
CC antibody titer of a circulating target antibody in a subject diagnosed
CC with an autoimmune disease; a method for treating a subject suffering
CC from or susceptible to an autoimmune disease; and a method for decreasing
CC the titer of a target antibody in the blood serum of a subject in need
CC the composition. The autoimmune disease is Graves' Disease, type 1
CC diabetes, rheumatoid arthritis, systemic lupus erythematosus,
CC inflammatory bowel disease, pre-eclampsia, multiple sclerosis, and
CC vasculitis; and controlling immune response. The molecule: bounds to a
CC target autoantibody may target ASGPR on hepatocytes and binding to ASGPR
CC will cause internalization of the complex (that is removal of target
CC autoantibodies); and shows improved efficacy in treating autoimmune
CC disease. The method and composition that allow for selective depletion
CC and/or neutralization of pathogenic antibodies.
XX
SQ Sequence 603 AA;
Query Match 68.9%; Score 3308.5; Length 603;
Best Local Similarity 98.5%;
Matches 594; Conservative 0; Mismatches 2; Indels 7; Gaps 1;
Qy 251 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 310
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 60
Qy 311 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 370
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 120
Qy 371 ICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWG 430
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 ICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWG 180
Qy 431 FCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 490
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 FCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 240
Qy 491 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 550
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 300
Qy 551 PSAWRSRDCESTLPYICKKYLN-------SGNTSDMYPMPNTLEYGNRTYKIINANMTWY 603
|||||||||||||||||||||| |||||||||||||||||||||||||||||
Db 301 PSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDMYPMPNTLEYGNRTYKIINANMTWY 360
Qy 604 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 663
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 420
Qy 664 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 723
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 480
Qy 724 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 783
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 540
Qy 784 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 843
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 600
Qy 844 CKM 846
|||
Db 601 CKM 603
RESULT 31 from 40.rag database.
BQU95510
ID BQU95510 standard; protein; 782 AA.
DT 03-APR-2025 (first entry)
XX
DE human PLA2R-hIgG1 Fc knob protein construct, SEQ 270.
XX
KW Immunoglobulin G1; Immunoglobulin gamma 1; PLA2R protein;
KW antiinflammatory; autoimmune disease; fusion protein; immunosuppressive;
KW membranous glomerulonephritis; mutein; nephrotropic;
KW phospholipase A2 receptor; protein production; protein therapy;
KW therapeutic; uropathic.
XX
OS Homo sapiens.
OS Synthetic.
XX
CC PN WO2025030003-A2.
XX
CC PD 06-FEB-2025.
XX
CC PF 01-AUG-2024; 2024WO-US040519.
XX
PR 01-AUG-2023; 2023US-0517104P.
XX
CC PA (MERI-) MERIDA BIOSCI INC.
XX
CC PI Gutierrez DA, Logtenberg MEW, Capili AD;
XX
DR WPI; 2025-13587A/020.
XX
CC PT New molecule comprising polypeptides having first Fc domain and second Fc
CC PT domain forming homodimer or heterodimer of first polypeptide and second
CC PT polypeptide, used to treat autoimmune disease e.g. membranous
CC PT nephropathy.
XX
CC PS Claim 107; SEQ ID NO 270; 349pp; English.
XX
CC The present invention relates to a novel molecule, useful for treating
CC autoimmune disease. The molecule comprises: (a) a first polypeptide
CC containing a first Fc domain and an autoantibody-binding domain that
CC binds to anti-PLA2R (phospholipase A2 receptor) autoantibodies; and (b) a
CC second polypeptide containing a second Fc domain, where the first Fc
CC domain and the second Fc domain form a homodimer or heterodimer of the
CC first polypeptide and the second polypeptide. The invention further
CC claims: (1) a nucleic acid comprising a nucleotide sequence encoding the
CC molecule; (2) a host cell containing the nucleic acid; (3) a vector
CC comprising the nucleic acid; (4) a pharmaceutical composition comprising
CC the molecule; (5) a method for making the molecule; (6) a method for
CC treating a subject suffering from or susceptible to an autoimmune disease
CC ; (7) a method for selectively depleting anti-PLA2R autoantibodies in the
CC subject; (8) a method for treating a human subject suffering from or
CC susceptible to membranous nephropathy; (9) a composition for decreasing
CC the titer of the anti-PLA2R autoantibodies in the blood serum of the
CC subject; and (10) an immune complex comprising the anti-PLA2R
CC autoantibody. The molecule is useful for controlling autoimmune response
CC and treating a subject suffering from or susceptible to autoimmune
CC disease, preferably membranous nephropathy (MN).
XX
SQ Sequence 782 AA;
Query Match 61.5%; Score 2951.5; Length 782;
Best Local Similarity 87.6%;
Matches 543; Conservative 5; Mismatches 9; Indels 63; Gaps 3;
Qy 251 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 310
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 60
Qy 311 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 370
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 120
Qy 371 ICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWG 430
||||||||||||
Db 121 ICEYLHKDLHTI------------------------------------------------ 132
Qy 431 FCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 490
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 133 -----TSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 187
Qy 491 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 550
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 188 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 247
Qy 551 PSAWRSRDCESTLPYICKKYLN-------SGNTSDMYPMPNTLEYGNRTYKIINANMTWY 603
|||||||||||||||||||||| |||||||||||||||||||||||||||||
Db 248 PSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDMYPMPNTLEYGNRTYKIINANMTWY 307
Qy 604 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 663
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 308 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 367
Qy 664 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 723
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 368 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 427
Qy 724 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 783
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 428 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 487
Qy 784 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 843
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 488 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 547
Qy 844 CKMNUCLEOTIDESEQUENC 863
||| :: |:: : |
Db 548 CKME---PKSSDKTHTCPPC 564
RESULT 32 from 40.ragdatabase.
BQU79882
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
ID BQU79882 standard; protein; 801 AA.
DT 03-APR-2025 (first entry)
XX
DE Human PLA2R-human IgG1 Fc knob mutant construct, SEQ 182.
XX
KW IgG1; Immunoglobulin G1; Immunoglobulin gamma 1;
KW M-type phospholipase A2 receptor; PLA2R protein; antibody neutralization;
KW autoimmune disease; fusion protein; immunosuppressive; mutein;
KW protein production; protein therapy; therapeutic.
XX
OS Homo sapiens.
OS Chimeric.
OS Synthetic.
OS Unidentified.
XX
CC PN WO2025030009-A1.
XX
CC PD 06-FEB-2025.
XX
CC PF 01-AUG-2024; 2024WO-US040527.
XX
PR 01-AUG-2023; 2023US-0517101P.
PR 01-AUG-2023; 2023US-0517104P.
XX
CC PA (MERI-) MERIDA BIOSCI INC.
XX
CC PI Gutierrez DA, Logtenberg MEW, Capili AD;
XX
DR WPI; 2025-13496A/017.
XX
CC PT New molecule comprising first polypeptide having first Fc domain and
CC PT binding domain that binds specifically to target antibody, and second
CC PT polypeptide having second Fc domain, used to treat autoimmune disease.
XX
CC PS Example 2; SEQ ID NO 182; 267pp; English.
XX
CC The present invention relates to a novel molecule, useful for treating
CC autoimmune disease. The molecule comprises: a first polypeptide
CC comprising a first Fc domain and a binding domain that binds specifically
CC to a target antibody; and a second polypeptide comprising a second Fc
CC domain; where the first Fc domain and the second Fc domain form a
CC homodimer or heterodimer of the first polypeptide and the second
CC polypeptide, and where the first and/or second Fc domain comprises one or
CC more mutated amino acid residues and has increased binding affinity to Fc
CC gamma RIIB relative to a corresponding wild-type Fc domain; and where
CC upon binding of two molecules to the target antibody, an immune complex
CC is formed that has enhanced binding kinetics with Fc gamma RIIB relative
CC to an immune complex that comprises the target antibody bound to two
CC corresponding molecules with wild-type Fc domains. The invention also
CC provides: a nucleic acid comprising a nucleotide sequence encoding the
CC molecule; a host cell containing the nucleic acid; a vector comprising
CC the nucleic acid; an immune complex comprising (i) a target antibody, and
CC (ii) two molecules; a method for making a molecule; a method for reducing
CC antibody titer of a circulating target antibody in a subject diagnosed
CC with an autoimmune disease; a method for treating a subject suffering
CC from or susceptible to an autoimmune disease; and a method for decreasing
CC the titer of a target antibody in the blood serum of a subject in need
CC the composition. The autoimmune disease is Graves' Disease, type 1
CC diabetes, rheumatoid arthritis, systemic lupus erythematosus,
CC inflammatory bowel disease, pre-eclampsia, multiple sclerosis, and
CC vasculitis; and controlling immune response. The molecule: bounds to a
CC target autoantibody may target ASGPR on hepatocytes and binding to ASGPR
CC will cause internalization of the complex (that is removal of target
CC autoantibodies); and shows improved efficacy in treating autoimmune
CC disease. The method and composition that allow for selective depletion
CC and/or neutralization of pathogenic antibodies.
XX
SQ Sequence 801 AA;
Query Match 61.5%; Score 2951.5; Length 801;
Best Local Similarity 87.6%;
Matches 543; Conservative 5; Mismatches 9; Indels 63; Gaps 3;
Qy 251 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 310
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 20 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 79
Qy 311 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 370
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 80 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 139
Qy 371 ICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWG 430
||||||||||||
Db 140 ICEYLHKDLHTI------------------------------------------------ 151
Qy 431 FCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 490
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 152 -----TSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 206
Qy 491 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 550
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 207 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 266
Qy 551 PSAWRSRDCESTLPYICKKYLN-------SGNTSDMYPMPNTLEYGNRTYKIINANMTWY 603
|||||||||||||||||||||| |||||||||||||||||||||||||||||
Db 267 PSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDMYPMPNTLEYGNRTYKIINANMTWY 326
Qy 604 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 663
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 327 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 386
Qy 664 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 723
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 387 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 446
Qy 724 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 783
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 447 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 506
Qy 784 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 843
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 507 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 566
Qy 844 CKMNUCLEOTIDESEQUENC 863
||| :: |:: : |
Db 567 CKME---PKSSDKTHTCPPC 583
RESULT 34 from 40.rag database.
BQU79799
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
ID BQU79799 standard; protein; 550 AA.
AC BQU79799;
DT 03-APR-2025 (first entry)
XX
DE Human PLA2R protein mutant, SEQ 25.
XX
KW M-type phospholipase A2 receptor; PLA2R protein; antibody neutralization;
KW antigen; autoimmune disease; immunosuppressive; mutein;
KW protein production; protein therapy; therapeutic.
XX
OS Homo sapiens.
XX
CC PN WO2025030009-A1.
XX
CC PD 06-FEB-2025.
XX
CC PF 01-AUG-2024; 2024WO-US040527.
XX
PR 01-AUG-2023; 2023US-0517101P.
PR 01-AUG-2023; 2023US-0517104P.
XX
CC PA (MERI-) MERIDA BIOSCI INC.
XX
CC PI Gutierrez DA, Logtenberg MEW, Capili AD;
XX
DR WPI; 2025-13496A/017.
XX
CC PT New molecule comprising first polypeptide having first Fc domain and
CC PT binding domain that binds specifically to target antibody, and second
CC PT polypeptide having second Fc domain, used to treat autoimmune disease.
XX
CC PS Example 2; SEQ ID NO 25; 267pp; English.
XX
CC The present invention relates to a novel molecule, useful for treating
CC autoimmune disease. The molecule comprises: a first polypeptide
CC comprising a first Fc domain and a binding domain that binds specifically
CC to a target antibody; and a second polypeptide comprising a second Fc
CC domain; where the first Fc domain and the second Fc domain form a
CC homodimer or heterodimer of the first polypeptide and the second
CC polypeptide, and where the first and/or second Fc domain comprises one or
CC more mutated amino acid residues and has increased binding affinity to Fc
CC gamma RIIB relative to a corresponding wild-type Fc domain; and where
CC upon binding of two molecules to the target antibody, an immune complex
CC is formed that has enhanced binding kinetics with Fc gamma RIIB relative
CC to an immune complex that comprises the target antibody bound to two
CC corresponding molecules with wild-type Fc domains. The invention also
CC provides: a nucleic acid comprising a nucleotide sequence encoding the
CC molecule; a host cell containing the nucleic acid; a vector comprising
CC the nucleic acid; an immune complex comprising (i) a target antibody, and
CC (ii) two molecules; a method for making a molecule; a method for reducing
CC antibody titer of a circulating target antibody in a subject diagnosed
CC with an autoimmune disease; a method for treating a subject suffering
CC from or susceptible to an autoimmune disease; and a method for decreasing
CC the titer of a target antibody in the blood serum of a subject in need
CC the composition. The autoimmune disease is Graves' Disease, type 1
CC diabetes, rheumatoid arthritis, systemic lupus erythematosus,
CC inflammatory bowel disease, pre-eclampsia, multiple sclerosis, and
CC vasculitis; and controlling immune response. The molecule: bounds to a
CC target autoantibody may target ASGPR on hepatocytes and binding to ASGPR
CC will cause internalization of the complex (that is removal of target
CC autoantibodies); and shows improved efficacy in treating autoimmune
CC disease. The method and composition that allow for selective depletion
CC and/or neutralization of pathogenic antibodies.
XX
SQ Sequence 550 AA;
Query Match 61.3%; Score 2940; Length 550;
Best Local Similarity 89.7%;
Matches 541; Conservative 0; Mismatches 2; Indels 60; Gaps 2;
Qy 251 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 310
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAP 60
Qy 311 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 370
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 EQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVASRKYIHKWISYGSGGGD 120
Qy 371 ICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWG 430
||||||||||||
Db 121 ICEYLHKDLHTI------------------------------------------------ 132
Qy 431 FCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 490
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 133 -----TSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETEEN 187
Qy 491 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 550
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 188 FIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDHCGTFSSFM 247
Qy 551 PSAWRSRDCESTLPYICKKYLN-------SGNTSDMYPMPNTLEYGNRTYKIINANMTWY 603
|||||||||||||||||||||| |||||||||||||||||||||||||||||
Db 248 PSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDMYPMPNTLEYGNRTYKIINANMTWY 307
Qy 604 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 663
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 308 AAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFT 367
Qy 664 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 723
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 368 FWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETRQSEHPELCSETSIPWIK 427
Qy 724 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 783
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 428 FKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLN 487
Qy 784 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 843
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 488 AQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFI 547
Qy 844 CKM 846
|||
Db 548 CKM 550
RESULT 22 from 40.rag database.
BMJ56852
ID BMJ56852 standard; protein; 798 AA.
AC BMJ56852;
XX
DT 09-MAR-2023 (first entry)
XX
DE IgG-PLA2R eC178-CD8 alpha-4-1BB-CD3 zeta CAAR protein, SEQ ID 17.
XX
KW 4-1BB protein; CD3 zeta protein; CD8 alpha protein; CDw137;
KW Immunoglobulin G; PLA2R protein; Phospholipase A2 receptor;
KW T-cell CD3 glycoprotein zeta chain; T-cell surface CD8 alpha chain;
KW chimeric antibody; chimeric autoantibody receptor; chimeric protein;
KW glomerular disease; immunotherapy; nephrotropic; prophylactic to disease;
KW renal disease; therapeutic.
XX
OS Homo sapiens.
OS Chimeric.
OS Synthetic.
OS Unidentified.
XX
CC PN WO2023015239-A1.
XX
CC PD 09-FEB-2023.
XX
CC PF 04-AUG-2022; 2022WO-US074516.
XX
PR 05-AUG-2021; 2021US-0229875P.
XX
CC PA (UPEN ) UNIV PENNSYLVANIA.
XX
CC PI Payne AS, Wang B;
XX
DR WPI; 2023-176625/018.
DR N-PSDB; BMJ56855.
XX
CC PT New polynucleotide encoding a chimeric autoantibody receptor comprising
CC PT an extracellular domain and an intracellular domain useful for treating
CC PT an autoantibody-mediated kidney disease and reducing glomerulus damage in
CC PT a subject.
XX
CC PS Claim 20; SEQ ID NO 17; 107pp; English.
XX
CC The present invention relates a polynucleotide encoding a chimeric
CC autoantibody receptor (CAAR), useful for treating an autoantibody-
CC mediated kidney disease and reducing glomerulus damage in a subject. The
CC polynucleotide comprises an extracellular domain comprising a
CC phospholipase A2 receptor (PLA2R) autoantigen, a transmembrane domain,
CC and an intracellular domain comprising an intracellular signaling domain
CC of a costimulatory molecule and/or a CD3 zeta intracellular signaling
CC domain, where the PLA2R autoantigen comprises (a) an extended cysteine
CC rich (eCysR) domain comprising a PLA2R N- terminal peptide and a cysteine
CC rich (CysR) domain, and (b) a C-type lectin domain 1 (CTLD1), C-type
CC lectin domain 7 (CTLD7), C-type lectin domain 8 (CTLD8), and fibronectin
CC type II (FNII) domain. The invention also includes: (1) a vector
CC comprising the polynucleotide; (2) a chimeric autoantibody receptor
CC comprising an extracellular domain comprising a phospholipase A2 receptor
CC autoantigen, a transmembrane domain, and an intracellular domain
CC comprising an intracellular signaling domain of a costimulatory molecule
CC and/or a CD3 zeta intracellular signaling domain, where the PLA2R
CC autoantigen comprises (a) an extended cysteine rich domain comprising a
CC PLA2R N-terminal peptide and a cysteine rich domain, and (b) CTLD7; (3) a
CC genetically modified cell comprising the PLA2R CAAR, the polynucleotide,
CC and/or the vector; (4) a composition comprising the polynucleotide, the
CC CAAR, and/or the cell, and a excipient; (5) a method for treating an
CC autoantibody-mediated kidney disease in a subject; and (6) a method for
CC preventing or reducing glomerulus damage in a subject at risk of or
CC suffering from an autoantibody-mediated kidney disease. The
CC polynucleotide of the invention is useful for treating an autoantibody-
CC mediated kidney disease; preventing or reducing glomerulus damage in a
CC subject at risk of or suffering from an autoantibody-mediated kidney
CC disease.
XX
SQ Sequence 798 AA;
Query Match 62.6%; Score 3004; Length 798;
Best Local Similarity 88.8%;
Matches 557; Conservative 2; Mismatches 6; Indels 62; Gaps 3;
Qy 227 KGGGGSAEGVAAALTPERLLEWQDKGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLW 286
|| :|||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 15 KGVQCGSEGVAAALTPERLLEWQDKGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLW 74
Qy 287 KWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVA 346
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 75 KWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVA 134
Qy 347 HDNTVVASRKYIHKWISYGSGGGDICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECT 406
||||||||||||||||||||||||||||||||||||
Db 135 HDNTVVASRKYIHKWISYGSGGGDICEYLHKDLHTI------------------------ 170
Qy 407 REGREDDLLWCATTSRYERDEKWGFCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSW 466
|||||||||||||||||||||||||||||||
Db 171 -----------------------------TSAEVGCDTIWEKDLNSHICYQFNLLSSLSW 201
Qy 467 SEAHSSCQMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNY 526
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 202 SEAHSSCQMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNY 261
Qy 527 LNWSPEVNFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKKYLN-------SGNTSDM 579
|||||||||||||||||||||||||||||||||||||||||||||| |||||
Db 262 LNWSPEVNFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDM 321
Qy 580 YPMPNTLEYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAH 639
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 322 YPMPNTLEYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAH 381
Qy 640 WIGLFTTDNGLNFDWSDGTKSSFTFWKDEESSLLGDCVFADSNGRWHSTACESFLQGAIC 699
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 382 WIGLFTTDNGLNFDWSDGTKSSFTFWKDEESSLLGDCVFADSNGRWHSTACESFLQGAIC 441
Qy 700 HVPPETRQSEHPELCSETSIPWIKFKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKD 759
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 442 HVPPETRQSEHPELCSETSIPWIKFKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKD 501
Qy 760 EAENAFLLEELFAFGSSVQMVWLNAQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPH 819
|||||||||||||||||||||||||||| :|||||||||||||||||||||||||||||
Db 502 EAENAFLLEELFAFGSSVQMVWLNAQFD--DETIKWFDGTPTDQSNWGIRKPDTDYFKPH 559
Qy 820 HCVALRIPEGLWQLSPCQEKKGFICKM 846
|||||||||||||||||||||||||||
Db 560 HCVALRIPEGLWQLSPCQEKKGFICKM 586
RESULT 24 from 40.rag database.
BMJ56844
ID BMJ56844 standard; protein; 585 AA.
XX
AC BMJ56844;
XX
DT 09-MAR-2023 (first entry)
XX
DE PLA2R eCysR-CTLD1-CTLD7-CTLD8 eC178 construct protein, SEQ ID 9.
XX
KW PLA2R protein; Phospholipase A2 receptor; chimeric antibody;
KW chimeric autoantibody receptor; fusion protein; glomerular disease;
KW immunotherapy; nephrotropic; prophylactic to disease; renal disease;
KW therapeutic.
XX
OS Homo sapiens.
OS Synthetic.
XX
CC PN WO2023015239-A1.
XX
CC PD 09-FEB-2023.
XX
CC PF 04-AUG-2022; 2022WO-US074516.
XX
PR 05-AUG-2021; 2021US-0229875P.
XX
CC PA (UPEN ) UNIV PENNSYLVANIA.
XX
CC PI Payne AS, Wang B;
XX
DR WPI; 2023-176625/018.
XX
CC PT New polynucleotide encoding a chimeric autoantibody receptor comprising
CC PT an extracellular domain and an intracellular domain useful for treating
CC PT an autoantibody-mediated kidney disease and reducing glomerulus damage in
CC PT a subject.
XX
CC PS Claim 10; SEQ ID NO 9; 107pp; English.
XX
CC The present invention relates a polynucleotide encoding a chimeric
CC autoantibody receptor (CAAR), useful for treating an autoantibody-
CC mediated kidney disease and reducing glomerulus damage in a subject. The
CC polynucleotide comprises an extracellular domain comprising a
CC phospholipase A2 receptor (PLA2R) autoantigen, a transmembrane domain,
CC and an intracellular domain comprising an intracellular signaling domain
CC of a costimulatory molecule and/or a CD3 zeta intracellular signaling
CC domain, where the PLA2R autoantigen comprises (a) an extended cysteine
CC rich (eCysR) domain comprising a PLA2R N- terminal peptide and a cysteine
CC rich (CysR) domain, and (b) a C-type lectin domain 1 (CTLD1), C-type
CC lectin domain 7 (CTLD7), C-type lectin domain 8 (CTLD8), and fibronectin
CC type II (FNII) domain. The invention also includes: (1) a vector
CC comprising the polynucleotide; (2) a chimeric autoantibody receptor
CC comprising an extracellular domain comprising a phospholipase A2 receptor
CC autoantigen, a transmembrane domain, and an intracellular domain
CC comprising an intracellular signaling domain of a costimulatory molecule
CC and/or a CD3 zeta intracellular signaling domain, where the PLA2R
CC autoantigen comprises (a) an extended cysteine rich domain comprising a
CC PLA2R N-terminal peptide and a cysteine rich domain, and (b) CTLD7; (3) a
CC genetically modified cell comprising the PLA2R CAAR, the polynucleotide,
CC and/or the vector; (4) a composition comprising the polynucleotide, the
CC CAAR, and/or the cell, and a excipient; (5) a method for treating an
CC autoantibody-mediated kidney disease in a subject; and (6) a method for
CC preventing or reducing glomerulus damage in a subject at risk of or
CC suffering from an autoantibody-mediated kidney disease. The
CC polynucleotide of the invention is useful for treating an autoantibody-
CC mediated kidney disease; preventing or reducing glomerulus damage in a
CC subject at risk of or suffering from an autoantibody-mediated kidney
CC disease.
XX
SQ Sequence 585 AA;
Query Match 62.5%; Score 3000; Length 585;
Best Local Similarity 89.5%;
Matches 555; Conservative 1; Mismatches 2; Indels 62; Gaps 3;
Qy 234 EGVAAALTPERLLEWQDKGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHG 293
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EGVAAALTPERLLEWQDKGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHG 60
Qy 294 LFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVA 353
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 LFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVA 120
Qy 354 SRKYIHKWISYGSGGGDICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDD 413
|||||||||||||||||||||||||||||
Db 121 SRKYIHKWISYGSGGGDICEYLHKDLHTI------------------------------- 149
Qy 414 LLWCATTSRYERDEKWGFCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSC 473
||||||||||||||||||||||||||||||||||||||
Db 150 ----------------------TSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSC 187
Qy 474 QMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEV 533
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 188 QMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEV 247
Qy 534 NFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKKYLN-------SGNTSDMYPMPNTL 586
||||||||||||||||||||||||||||||||||||||| ||||||||||||
Db 248 NFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDMYPMPNTL 307
Qy 587 EYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTT 646
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 308 EYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTT 367
Qy 647 DNGLNFDWSDGTKSSFTFWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETR 706
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 368 DNGLNFDWSDGTKSSFTFWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETR 427
Qy 707 QSEHPELCSETSIPWIKFKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFL 766
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 428 QSEHPELCSETSIPWIKFKSNCYSFSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFL 487
Qy 767 LEELFAFGSSVQMVWLNAQFDGNNETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRI 826
||||||||||||||||||||| :||||||||||||||||||||||||||||||||||||
Db 488 LEELFAFGSSVQMVWLNAQFD--DETIKWFDGTPTDQSNWGIRKPDTDYFKPHHCVALRI 545
Qy 827 PEGLWQLSPCQEKKGFICKM 846
||||||||||||||||||||
Db 546 PEGLWQLSPCQEKKGFICKM 565
RESULT 42 from rag.database.
BMJ56853
ID BMJ56853 standard; protein; 700 AA.
XX
AC BMJ56853;
XX
DT 09-MAR-2023 (first entry)
XX
DE IgG-PLA2R eCF17-CD8 alpha-4-1BB-CD3 zeta CAAR protein, SEQ ID 18.
XX
KW 4-1BB protein; CD3 zeta protein; CD8 alpha protein; CDw137;
KW Immunoglobulin G; PLA2R protein; Phospholipase A2 receptor;
KW T-cell CD3 glycoprotein zeta chain; T-cell surface CD8 alpha chain;
KW chimeric antibody; chimeric autoantibody receptor; chimeric protein;
KW glomerular disease; immunotherapy; nephrotropic; prophylactic to disease;
KW renal disease; therapeutic.
XX
OS Homo sapiens.
OS Chimeric.
OS Synthetic.
OS Unidentified.
XX
CC PN WO2023015239-A1.
XX
CC PD 09-FEB-2023.
XX
CC PF 04-AUG-2022; 2022WO-US074516.
XX
PR 05-AUG-2021; 2021US-0229875P.
XX
CC PA (UPEN ) UNIV PENNSYLVANIA.
XX
CC PI Payne AS, Wang B;
XX
DR WPI; 2023-176625/018.
DR N-PSDB; BMJ56856.
XX
CC PT New polynucleotide encoding a chimeric autoantibody receptor comprising
CC PT an extracellular domain and an intracellular domain useful for treating
CC PT an autoantibody-mediated kidney disease and reducing glomerulus damage in
CC PT a subject.
XX
CC PS Claim 20; SEQ ID NO 18; 107pp; English.
XX
CC The present invention relates a polynucleotide encoding a chimeric
CC autoantibody receptor (CAAR), useful for treating an autoantibody-
CC mediated kidney disease and reducing glomerulus damage in a subject. The
CC polynucleotide comprises an extracellular domain comprising a
CC phospholipase A2 receptor (PLA2R) autoantigen, a transmembrane domain,
CC and an intracellular domain comprising an intracellular signaling domain
CC of a costimulatory molecule and/or a CD3 zeta intracellular signaling
CC domain, where the PLA2R autoantigen comprises (a) an extended cysteine
CC rich (eCysR) domain comprising a PLA2R N- terminal peptide and a cysteine
CC rich (CysR) domain, and (b) a C-type lectin domain 1 (CTLD1), C-type
CC lectin domain 7 (CTLD7), C-type lectin domain 8 (CTLD8), and fibronectin
CC type II (FNII) domain. The invention also includes: (1) a vector
CC comprising the polynucleotide; (2) a chimeric autoantibody receptor
CC comprising an extracellular domain comprising a phospholipase A2 receptor
CC autoantigen, a transmembrane domain, and an intracellular domain
CC comprising an intracellular signaling domain of a costimulatory molecule
CC and/or a CD3 zeta intracellular signaling domain, where the PLA2R
CC autoantigen comprises (a) an extended cysteine rich domain comprising a
CC PLA2R N-terminal peptide and a cysteine rich domain, and (b) CTLD7; (3) a
CC genetically modified cell comprising the PLA2R CAAR, the polynucleotide,
CC and/or the vector; (4) a composition comprising the polynucleotide, the
CC CAAR, and/or the cell, and a excipient; (5) a method for treating an
CC autoantibody-mediated kidney disease in a subject; and (6) a method for
CC preventing or reducing glomerulus damage in a subject at risk of or
CC suffering from an autoantibody-mediated kidney disease. The
CC polynucleotide of the invention is useful for treating an autoantibody-
CC mediated kidney disease; preventing or reducing glomerulus damage in a
CC subject at risk of or suffering from an autoantibody-mediated kidney
CC disease.
XX
SQ Sequence 700 AA;
Query Match 55.6%; Score 2668.5; Length 700;
Best Local Similarity 97.0%;
Matches 481; Conservative 1; Mismatches 7; Indels 7; Gaps 1;
Qy 227 KGGGGSAEGVAAALTPERLLEWQDKGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLW 286
|| :|||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 15 KGVQCGSEGVAAALTPERLLEWQDKGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLW 74
Qy 287 KWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVA 346
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 75 KWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVA 134
Qy 347 HDNTVVASRKYIHKWISYGSGGGDICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECT 406
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 135 HDNTVVASRKYIHKWISYGSGGGDICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECT 194
Qy 407 REGREDDLLWCATTSRYERDEKWGFCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSW 466
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 195 REGREDDLLWCATTSRYERDEKWGFCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSW 254
Qy 467 SEAHSSCQMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNY 526
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 255 SEAHSSCQMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNY 314
Qy 527 LNWSPEVNFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKKYLN-------SGNTSDM 579
|||||||||||||||||||||||||||||||||||||||||||||| |||||
Db 315 LNWSPEVNFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDM 374
Qy 580 YPMPNTLEYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAH 639
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 375 YPMPNTLEYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAH 434
Qy 640 WIGLFTTDNGLNFDWSDGTKSSFTFWKDEESSLLGDCVFADSNGRWHSTACESFLQGAIC 699
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 435 WIGLFTTDNGLNFDWSDGTKSSFTFWKDEESSLLGDCVFADSNGRWHSTACESFLQGAIC 494
Qy 700 HVPPETRQSEHPELCS 715
|||||||||||||| |
Db 495 HVPPETRQSEHPELAS 510
RESULT 43 from 40.rag database.
BMJ56845
ID BMJ56845 standard; protein; 487 AA.
AC BMJ56845;
DT 09-MAR-2023 (first entry)
DE PLA2R eCysR-FNII-CTLD1-CTLD7 eCF17 construct protein, SEQ ID 10.
XX
KW PLA2R protein; Phospholipase A2 receptor; chimeric antibody;
KW chimeric autoantibody receptor; fusion protein; glomerular disease;
KW immunotherapy; nephrotropic; prophylactic to disease; renal disease;
KW therapeutic.
XX
OS Homo sapiens.
OS Synthetic.
XX
CC PN WO2023015239-A1.
XX
CC PD 09-FEB-2023.
XX
CC PF 04-AUG-2022; 2022WO-US074516.
XX
PR 05-AUG-2021; 2021US-0229875P.
XX
CC PA (UPEN ) UNIV PENNSYLVANIA.
XX
CC PI Payne AS, Wang B;
XX
DR WPI; 2023-176625/018.
XX
CC PT New polynucleotide encoding a chimeric autoantibody receptor comprising
CC PT an extracellular domain and an intracellular domain useful for treating
CC PT an autoantibody-mediated kidney disease and reducing glomerulus damage in
CC PT a subject.
XX
CC PS Claim 10; SEQ ID NO 10; 107pp; English.
XX
CC The present invention relates a polynucleotide encoding a chimeric
CC autoantibody receptor (CAAR), useful for treating an autoantibody-
CC mediated kidney disease and reducing glomerulus damage in a subject. The
CC polynucleotide comprises an extracellular domain comprising a
CC phospholipase A2 receptor (PLA2R) autoantigen, a transmembrane domain,
CC and an intracellular domain comprising an intracellular signaling domain
CC of a costimulatory molecule and/or a CD3 zeta intracellular signaling
CC domain, where the PLA2R autoantigen comprises (a) an extended cysteine
CC rich (eCysR) domain comprising a PLA2R N- terminal peptide and a cysteine
CC rich (CysR) domain, and (b) a C-type lectin domain 1 (CTLD1), C-type
CC lectin domain 7 (CTLD7), C-type lectin domain 8 (CTLD8), and fibronectin
CC type II (FNII) domain. The invention also includes: (1) a vector
CC comprising the polynucleotide; (2) a chimeric autoantibody receptor
CC comprising an extracellular domain comprising a phospholipase A2 receptor
CC autoantigen, a transmembrane domain, and an intracellular domain
CC comprising an intracellular signaling domain of a costimulatory molecule
CC and/or a CD3 zeta intracellular signaling domain, where the PLA2R
CC autoantigen comprises (a) an extended cysteine rich domain comprising a
CC PLA2R N-terminal peptide and a cysteine rich domain, and (b) CTLD7; (3) a
CC genetically modified cell comprising the PLA2R CAAR, the polynucleotide,
CC and/or the vector; (4) a composition comprising the polynucleotide, the
CC CAAR, and/or the cell, and a excipient; (5) a method for treating an
CC autoantibody-mediated kidney disease in a subject; and (6) a method for
CC preventing or reducing glomerulus damage in a subject at risk of or
CC suffering from an autoantibody-mediated kidney disease. The
CC polynucleotide of the invention is useful for treating an autoantibody-
CC mediated kidney disease; preventing or reducing glomerulus damage in a
CC subject at risk of or suffering from an autoantibody-mediated kidney
CC disease.
XX
SQ Sequence 487 AA;
Query Match 55.4%; Score 2660.5; Length 487;
Best Local Similarity 98.2%;
Matches 478; Conservative 0; Mismatches 2; Indels 7; Gaps 1;
Qy 234 EGVAAALTPERLLEWQDKGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHG 293
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EGVAAALTPERLLEWQDKGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHG 60
Qy 294 LFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVA 353
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 LFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCNRKMITGPLQYSVQVAHDNTVVA 120
Qy 354 SRKYIHKWISYGSGGGDICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDD 413
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SRKYIHKWISYGSGGGDICEYLHKDLHTIKGNTHGMPCMFPFQYNHQWHHECTREGREDD 180
Qy 414 LLWCATTSRYERDEKWGFCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSC 473
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 LLWCATTSRYERDEKWGFCPDPTSAEVGCDTIWEKDLNSHICYQFNLLSSLSWSEAHSSC 240
Qy 474 QMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEV 533
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 QMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEV 300
Qy 534 NFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKKYLN-------SGNTSDMYPMPNTL 586
||||||||||||||||||||||||||||||||||||||| ||||||||||||
Db 301 NFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKKYLNHIDHEIVEVNTSDMYPMPNTL 360
Qy 587 EYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTT 646
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 EYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTT 420
Qy 647 DNGLNFDWSDGTKSSFTFWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETR 706
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 DNGLNFDWSDGTKSSFTFWKDEESSLLGDCVFADSNGRWHSTACESFLQGAICHVPPETR 480
Qy 707 QSEHPEL 713
|||||||
Db 481 QSEHPEL 487
Double Patenting
14. A rejection based on double patenting of the “same invention” type finds its support in the language of 35 U.S.C. 101 which states that “whoever invents or discovers any new and useful process... may obtain a patent therefor...” (Emphasis added). Thus, the term “same invention,” in this context, means an invention drawn to identical subject matter. See Miller v. Eagle Mfg. Co., 151 U.S. 186 (1894); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Ockert, 245 F.2d 467, 114 USPQ 330 (CCPA 1957).
A statutory type (35 U.S.C. 101) double patenting rejection can be overcome by canceling or amending the claims that are directed to the same invention so they are no longer coextensive in scope. The filing of a terminal disclaimer cannot overcome a double patenting rejection based upon 35 U.S.C. 101.
15. The provisional rejection of claims 1-11 and 17-20 under 35 U.S.C. 101 as claiming the same invention as that of claims 1-21 of copending Application No. 19/237,700 (filed June 13, 2025) is maintained. Claims 12-16 and 21 have been cancelled.
This is a provisional statutory double patenting rejection since the claims directed to the same invention have not in fact been patented.
”Applicant respectfully requests that this rejection be held in abeyance until allowable subject matter is identified in the present application.”, see Remarks submitted June 30, 2026, page 14, Double Patenting segment.
Applicant’s point of view has been carefully considered, but found unpersuasive.
At this point in prosecution the claimed invention has not been found allowable, nor has a terminal disclaimer been filed. Hence, the rejection is maintained.
Conclusion
16. Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
17. Any inquiry concerning this communication or earlier communications from the Examiner should be directed to ALANA HARRIS DENT whose telephone number is (571)272-0831. The Examiner works a flexible schedule, however can normally 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 Examiner by telephone are unsuccessful, the Examiner’s supervisor, Julie Wu can be reached on 571-272-0859. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
ALANA HARRIS DENT
Primary Examiner
Art Unit 1643
Alana Harris Dent
13 July 2026
/Alana Harris Dent/Primary Examiner, Art Unit 1643
Prosecution Insights