Chimeric invasin system
AssigneeSiVEC Biotechnologies LLC
InventorsAshley B. Williams, Lyndsey M. Linke, Darcy Mora, Melissa Vivian
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AssigneeSiVEC Biotechnologies LLC
InventorsAshley B. Williams, Lyndsey M. Linke, Darcy Mora, Melissa Vivian
Estimating the term…
A transkingdom platform for the delivery of therapeutics to target cells. The system maintains the export and uptake functions of Inv while modifying its targeting away from β1 integrin to other proteins expressed on the surface of target eukaryotic cells (i.e., a cell surface protein) or chemical moieties (i.e., a cell surface chemical moiety) expressed on the surface of a target eukaryotic cell by replacing D4 and D5 of Inv with a binding domain from a heterologous protein via genetic engineering. These heterologous proteins could be derived from bacterial, fungal, animal, or viral genomes. This engineering would result in the construction of a chimeric Inv protein in which D1-D3 (i.e., the non-binding domains) are fused in frame to an alternative binding domain derived from a heterologous protein. The alternative binding domain would interact with a different cell surface protein or chemical moiety, which can in some instances be referred to as a receptor, on the surface on the surface of a eukaryotic cell, thereby allowing specific targeting to cells independent of Inv's intrinsic β1 integrin binding.
An expression cassette for the production of a chimeric invasin (Inv) polypeptide comprising a prokaryotic promoter and a nucleic acid sequence encoding an Inv polypeptide fused to a linker polypeptide at the carboxy terminus of the Inv polypeptide and wherein expression of the nucleic acid encoding the chimeric invasin polypeptide is controlled by the prokaryotic promoter.
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A chimeric invasin polypeptide comprising an Inv polypeptide and a linker polypeptide, wherein the linker polypeptide has a first end (N-terminus) and a second end (C-terminus), wherein the first end (N-terminus) of the linker polypeptide is attached to the C-terminus of the Inv polypeptide.
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A chimeric invasin polypeptide comprising the D1-D3 domains of the Inv polypeptide attached to the binding domain of a heterologous protein or a synthetic binding domain.
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Dependencies are inferred from the claim text.