IGM Biosciences has filed a patent for modified recombinant J-chain polypeptides and binding molecules, including antibodies, and their uses. The patent claim specifically covers antibodies with a modified J-chain that includes an extraneous binding moiety. GlobalData’s report on IGM Biosciences gives a 360-degree view of the company including its patenting strategy. Buy the report here.

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According to GlobalData’s company profile on IGM Biosciences, Personalized cancer vaccines was a key innovation area identified from patents. IGM Biosciences's grant share as of September 2023 was 25%. Grant share is based on the ratio of number of grants to total number of patents.

Modified j-chain antibodies with extraneous binding moiety

Source: United States Patent and Trademark Office (USPTO). Credit: IGM Biosciences Inc

A recently filed patent (Publication Number: US20230279111A1) describes a modified antibody that includes a modified J-chain. The modified J-chain contains an extraneous binding moiety, which is a molecule that can bind to a specific target. The antibody can be an IgM, IgA, IgG/IgM, or IgG/IgA antibody, or an antigen-binding fragment of these antibodies.

The patent claims specify various aspects of the modified antibody. Claim 2 states that the native sequence J-chain is the native human J-chain sequence of SEQ ID NO: 1, or a functional fragment thereof. Claim 4 mentions that the extraneous binding moiety is introduced into the native human J-chain sequence by direct or indirect fusion. Claim 5 further specifies that the binding moiety can be introduced by indirect fusion through a peptide linker, which is a short sequence of amino acids that connects the J-chain and the binding moiety. Claim 7 states that the extraneous binding moiety is introduced at or around the C-terminus of the native human J-chain sequence, and claim 9 mentions that it can also be introduced at or around the N-terminus.

The patent claims also provide details about the specific locations where the extraneous binding moiety can be introduced. Claim 11 specifies that it can be introduced between cysteine residues 92 and 101 of the native human J-chain sequence. Claim 12 mentions that it can be introduced at or near a glycosylation site, which is a location where sugar molecules can attach to the J-chain.

Additionally, the patent claims describe the use of a peptide linker of about 10 to 20 amino acids in length (claim 13), with claim 15 specifying that the peptide linker is 15 amino acids long. The claims also mention the introduction of the extraneous binding moiety through chemical or chemo-enzymatic derivatization (claim 16), with claim 17 specifying the use of a chemical linker. Claim 18 mentions that the chemical linker can be cleavable or non-cleavable, and claim 19 provides examples of cleavable linkers such as chemically labile or enzyme-labile linkers. Finally, claim 20 lists various specific linkers that can be used, including N-succinimidyl-3-(2-pyridyldithio) propionate (SPDP), succinimidyl-4-(N-maleimidomethyl) cyclohexane-1-carboxylate (SMCC), and others.

Overall, the patent claims describe a modified antibody with a modified J-chain that includes an extraneous binding moiety. The claims provide specific details about the sequence, location, and methods of introducing the binding moiety, as well as the use of a peptide linker and chemical linkers. These modifications can potentially enhance the binding specificity and effectiveness of the antibody for various applications in the field of immunology and therapeutics.

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GlobalData, the leading provider of industry intelligence, provided the underlying data, research, and analysis used to produce this article.

GlobalData Patent Analytics tracks bibliographic data, legal events data, point in time patent ownerships, and backward and forward citations from global patenting offices. Textual analysis and official patent classifications are used to group patents into key thematic areas and link them to specific companies