US 8,956,847 B2Granted

Fusion proteins

AssigneeSyntaxin Limited

InventorsKeith Alan Foster, John Chaddock, Philip Marks, Patrick Stancombe, Lyndsey Durose

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Abstract

The invention provides a single chain, polypeptide fusion protein, comprising: a non-cytotoxic protease, or a fragment thereof, which protease or protease fragment is capable of cleaving a protein of the exocytic fusion apparatus of a target cell; a Targeting Moiety that is capable of binding to a Binding Site on the target cell, which Binding Site is capable of undergoing endocytosis to be incorporated into an endocome within the target cell; a protease cleaving site at which site the fusion protein is cleavable by the protease, wherein the protease cleavage site is located between the non-cytotoxic protease or fragment thereof and the Targeting Moiety; and the translocation domain that is capable of translocating the protease or protease fragment from within an endosome, across the endosomal membrane and into the cytosol of the target cell.

Claims25

Dependent claims

A single chain, polypeptide fusion protein, comprising:

a) a non-cytotoxic protease that cleaves a protein of the exocytic fusion apparatus of a target cell;
b) a Targeting Moiety that binds to a Binding Site on the target cell, which Binding Site undergoes endocytosis to be incorporated into an endosome within the target cell;
c) a protease cleavage site at which site the fusion protein is cleavable by a protease, wherein the protease cleavage site is located between the non-cytotoxic protease and the Targeting Moiety;
and
d) a translocation domain that translocates the non-cytotoxic protease from within an endosome, across the endosomal membrane and into the cytosol of the target cell;
wherein the Targeting Moiety is located between the protease cleavage site and the translocation domain;
and
wherein the non-cytotoxic protease forms a disulphide bond with the translocation domain of the fusion protein, wherein the amino acid residue of the non-cytotoxic protease that forms the first part of the disulphide bond is located within the last 20 C-terminal amino acid residues of the non-cytotoxic protease, and the amino acid residue of the translocation domain that forms the second part of the disulphide bond is located within the first 20 N-terminal amino acid residues of the translocation domain.

5 more elements

Dependencies are inferred from the claim text.

Facts

Application: 13/738,235Filed 10 Jan 2013 · continuation
Priority: GB 0426397.61 Dec 2004
Published: US 2013/0115682 A19 May 2013
Granted: 17 Feb 2015
Term ends: Not estimatedThe source records don’t support an estimate.

Classification45 codes

C12N 9/52
Proteinases , e.g. Endopeptidases: derived from bacteria or Archaea
A61P 1/00
Drugs for disorders of the alimentary tract or the digestive system
A61P 1/04
Drugs for disorders of the alimentary tract or the digestive system: for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of…
A61P 1/16
Drugs for disorders of the alimentary tract or the digestive system: for liver or gallbladder disorders, e.g. hepatoprotective agents,…

Family

PCT/GB2005/004606Parent of this continuation · filed 1 Dec 2005
Application13/354,787Parent of this continuation · filed 20 Jan 2012
US 8,124,074 B2Parent of this continuation · filed 28 Feb 2012
US 2013/0115682 A1Pre-grant publication · published 9 May 2013
US 8,372,615 B2Parent of this continuation
Application11/792,076Parent of this continuation
US 2009/0004174 A1Published application
US 2012/0149084 A1Published application
US 8,956,847 B2This patent

From the US filing history. Foreign family members aren’t listed.