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Assignees
Member
VLP TherapeuticsVLP Therapeutics is a Maryland-based biotechnology company established in 2012, focused on developing preventative and therapeutic vaccines as well as targeted antibody agents for cancer, infectious diseases, autoimmune conditions, and neurological diseases. The company utilizes next-generation virus-like particle platforms, gene delivery systems, and structure-based antigen design to address unmet global medical needs. Its research pipeline includes vaccine candidates for malaria, dengue, COVID-19, and cancer immunotherapies. The organization is driven by a team with experience in vaccine R&D, clinical development, and collaborative partnerships with prominent academic and government institutions.
VLP Therapeutics is a Maryland-based biotechnology company established in 2012, focused on developing preventative and therapeutic vaccines as well as targeted antibody agents for cancer, infectious diseases, autoimmune conditions, and neurological diseases. The company utilizes next-generation virus-like particle platforms, gene delivery systems, and structure-based antigen design to address unmet global medical needs. Its research pipeline includes vaccine candidates for malaria, dengue, COVID-19, and cancer immunotherapies. The organization is driven by a team with experience in vaccine R&D, clinical development, and collaborative partnerships with prominent academic and government institutions.
Publication Number
US-9249191-B2
Publication Date
2016-02-02
Expiration Date
Abstract
The present invention provides a particle comprising a polypeptide and at least one antigen, and a composition comprising thereof.
Core Innovation
A Chikungunya virus (CHIKV) or Venezuelan equine encephalitis virus (VEEV) virus-like particle is provided in which the virus-like particle contains at least one antigen inserted into an E2 envelope protein to form a fusion protein. The fusion protein includes an antigen inserted into a CHIKV E2 envelope protein within a region that corresponds in position to residues 509-512, residues 519-520, or residues 529-533 of SEQ ID NO: 1 or 2, or the antigen inserted into a VEEV E2 envelope protein within a region that corresponds in position to residues 515-520, or residues 536-539 of SEQ ID NO: 3.
The at least one antigen may include a polypeptide derived from TNF-α, CD20, or CTLA4. The antigen may be arranged in the fusion protein with optional linker configurations, including one or two linkers positioned between the antigen N-terminal residue and/or the antigen C-terminal residue and the envelope protein.
The fusion proteins of the virus-like particles are also defined by sequence-identity constraints, including that the fusion protein includes an amino acid sequence with at least 90% sequence identity to one of SEQ ID NOs: 4, 5, 6, 7, or 8.
Claims Coverage
The provided claim set contains one independent claim directed to CHIKV- or VEEV-derived E2 virus-like particles with antigen insertion at specified E2 residue regions, with additional dependent refinements. The independent claim includes placement-specific insertion criteria and defines fusion protein formation through E2 integration.
Antigen insertion into CHIKV or VEEV E2 to form a fusion protein
A CHIKV or VEEV virus-like particle wherein the virus-like particle contains at least one antigen inserted into an E2 envelope protein to form a fusion protein.
Position-specific E2 insertion regions for CHIKV and VEEV
The at least one antigen is inserted within a CHIKV E2 envelope protein within a region that corresponds in position to residues 509-512, residues 519-520, or residues 529-533 of SEQ ID NO: 1 or 2; or within a VEEV E2 envelope protein within a region that corresponds in position to residues 515-520, or residues 536-539 of SEQ ID NO: 3.
Coverage centers on virus-like particles built from CHIKV or VEEV E2 envelope proteins with antigen fused via insertion at specified residue regions, optionally configured with linker placement, optionally restricted to specific antigen polypeptides (TNF-α, CD20, CTLA4), and optionally constrained by sequence identity to defined fusion protein sequences.
Stated Advantages
Documented Applications
No documented applications found
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