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AssigneesMicrobiological Research Authority, The Speywood Laboratory Ltd.
InventorsClifford Charles Shone, Conrad Padraig Quinn, Keith Alan Foster
Estimating the term…
A polypeptide has first and second domains which enable the polypeptide to be translocated into a target cell or which increase the solubility of the polypeptide, or both, and further enable the polypeptide to cleave one or more vesicle or plasma-membrane associated proteins essential to exocytosis. The polypeptide thus combines useful properties of a clostridial toxin, such as a botulinum or tetanus toxin, without the toxicity associated with the natural molecule. The polypeptide can also contain a third domain that targets it to a specific cell, rendering the polypeptide useful in inhibition of exocytosis in target cells. Fusion proteins comprising the polypeptide, nucleic acids encoding the polypeptide and methods of making the polypeptide are also provided. Controlled activation of the polypeptide is possible and the polypeptide can be incorporated into vaccines and toxin assays.
A non-toxic polypeptide comprising first, second and third domains, wherein
A non-toxin polypeptide comprising first, second and third domains, wherein
A non-toxin polypeptide comprising first and second domains, wherein
A non-toxin polypeptide comprising first and second domains, wherein
A non-toxin polypeptide comprising first and second domains, wherein
A polypeptide comprising a botulinum toxin light chain and a botulinum toxin heavy chain lacking a C-terminal part of the botulinum toxin heavy chain designated Hc wherein said botulinum toxin heavy chain is not capable of binding to cell surface receptors.
A polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO. 2, 4, 6, 10, 12, 14, 16, 18, 20, 22, 24, and 26.
Dependencies are inferred from the claim text.