Database for
Therapeutic Antibodies
Therapeutic Antibodies
| Entry ID | 937 |
| INN | None |
| Status | Clinical |
| Drug code(s) | LMN-201 |
| Brand name | None |
| mAb sequence source | mAb - source TBD |
| General Molecular Category | Mixture of 3 |
| Format, general category | Fragment |
| Format details | sdAb, VHH dimers |
| Isotype (Fc) | None |
| Light chain isotype | None |
| Linker | None |
| Ave. DAR | None |
| Conjugated/fused moiety | None |
| Discovery method/technology | Camelid-derived |
| Target(s) | C. difficile (exotoxin TcdB) |
| Indications of clinical studies | Clostridioides Difficile Infection |
| Primary therapeutic area | Infectious diseases |
| Most advanced stage of development (global) | Phase 2/3 |
| Status | Active |
| Start of clinical phase (IND filing or first Phase 1) | August 15, 2021 |
| Start of Phase 2 | |
| Start of Phase 3 | August 29, 2024 |
| Date BLA/NDA submitted to FDA | |
| Year of first approval (global) | None |
| Date of first US approval | |
| INN, US product name | None |
| US or EU approved indications | None |
| Company | Lumen Bioscience Inc. |
| Licensee/Partner | None |
| Comments about company or candidate | NCT05330182 Phase 2/3 study of Prevention of C. Difficile Infection Recurrence started in Aug 2024. May 17, 2023: Lumen Bioscience announced that the U.S. Food and Drug Administration (FDA) has granted Fast Track Designation for LMN-201, an investigational, orally delivered biologic drug to treat and prevent C. difficile infection (CDI). The FDA previously cleared a planned Phase 2/3 study of LMN-201, which will begin enrolling approximately 375 patients at sites across the United States later this year. |
| Full address of company | Seattle, WA 98103 North America United States of America https://www.lumen.bio/contact |
LMN-201 consists of orally delivered whole, dried, non-viable biomass of spirulina (Arthrospira platensis) grown from 4 separate strains, each of which has been engineered to express one of the following therapeutic proteins: 3 toxin-binding proteins that bind and inhibit C. difficile toxin B (TcdB), an essential virulence factor for C. difficile 1 lysozyme-like enzyme that selectively degrades the cell wall of C. difficile and causes rapid destruction of the organism. The cocktail is comprised of homodimeric versions of three toxin-binding proteins (5D, E3, and 7F) derived from camelid single-domain antibody fragments known as VHHs or nanobodies. Each protein was previously shown to inactivate TcdB. Binding of 5D to TcdB prevents its pH-driven conformational change that enables pore formation and transit into the cytoplasm from internalised endosomes. E3 binds to the glucosyltransferase domain (GTD) of TcdB, interfering with the autoproteolysis step necessary for enzyme activation. 7F also binds to the GTD, inhibiting catalytic glucosylation/inactivation of Rho-family GTPases by the mature N-terminal glucosyltransferase. The fourth cocktail component is a C. difficile-specific endolysin. (https://www.biorxiv.org/content/10.1101/2021.12.21.473715v1.full)
| Anticipated events | None |
| Factor(s) contributing to discontinuation | None |