The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.
The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.
Patent No.:
Date of Patent:
Nov. 09, 2010
Filed:
Apr. 25, 2006
Florian Werther, Innsbruck, AT;
Clemens Achmüller, Innsbruck, AT;
Philipp Wechner, Innsbruck, AT;
Bernhard Auer, Innsbruck, AT;
Silvio Podmirseg, Innsbruck, AT;
Florian Werther, Innsbruck, AT;
Clemens Achmüller, Innsbruck, AT;
Philipp Wechner, Innsbruck, AT;
Bernhard Auer, Innsbruck, AT;
Silvio Podmirseg, Innsbruck, AT;
Sandoz AG, Basel, CH;
Boehringer Ingelheim RCV GmbH & Co KG, Vienna, AT;
Abstract
The invention relates to a process for the recombinant production of a heterologous polypeptide of interest by cultivating a bacterial host cell transformed with an expression vector comprising a nucleic acid molecule encoding a fusion polypeptide wherein (a) the amino-proximal fusion partner is an autoprotease Ncomprising the replacement(s) by glutamic acid of one or more cysteines at positions corresponding to the positions 112, 134, and 138 of the autoprotease Nof classical swine fever virus and (b) the carboxyl-proximal fusion partner is an heterologous polypeptide of interest fused to the autoprotease Nso that it is capable of being cleaved from the fusion polypeptide by autoprotease Nautoproteolytic activity, said process comprising (i) cultivating the transformed host cell under conditions permitting the expression of the fusion polypeptide and the formation of corresponding cytoplasmic inclusion bodies, (ii) isolating the inclusion bodies from the host cell, (iii) solubilizing the isolated inclusion bodies, (iv) inducing autoproteolytic cleavage of the heterologous polypeptide of interest from the fusion polypeptide, and (v) isolating the cleaved heterologous polypeptide of interest.