Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2006-04-25
2010-11-09
Nashed, Nashaat T (Department: 1656)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C435S069100, C435S069700, C435S252300, C435S252330, C435S320100, C536S023200, C536S023400
Reexamination Certificate
active
07829319
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 Nprocomprising the replacement(s) by glutamic acid of one or more cysteines at positions corresponding to the positions 112, 134, and 138 of the autoprotease Nproof classical swine fever virus and (b) the carboxyl-proximal fusion partner is an heterologous polypeptide of interest fused to the autoprotease Nproso that it is capable of being cleaved from the fusion polypeptide by autoprotease Nproautoproteolytic 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.
REFERENCES:
patent: 6936455 (2005-08-01), Stempfer et al.
patent: 7378512 (2008-05-01), Rumenapf et al.
patent: 2009/0203069 (2009-08-01), Jungbauer et al.
patent: 2009/0306343 (2009-12-01), Jungbauer et al.
patent: WO-01/11056 (2001-02-01), None
patent: WO-01/11057 (2001-02-01), None
Stark, R., et al., 1993, “Processing of pestivirus polyprotein: Cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus”, Journal of Virology, vol. 67, No. 12, pp. 7088-7095.
Mishra, N., et al., 2006, “Genetic analysis of Indian bovine viral diarrhea virus 1 isolates in Npro and entire region coding structural proteins”, Acta Virologica, vol. 50, No. 1, pp. 39-44.
Gil, L. H. V. G., et al., 2006, “The amino-terminal domain of bovine viral diarrhea virus Npro protein is necessary for alpha/beta interferon antagonism”, Journal of Virology, vol. 80, No. 2, pp. 900-911.
Szymanski, M. R., et al., 2009, “Zinc binding in pestivirus Npro is required for interferon regulatory factor 3 interaction and degradation”, Journal of Molecular Biology, vol. 391, No. 2, pp. 438-449.
Hartl, Marcus et al., “JAC, a direct target of oncogenic transcription factor Jun, is involved in cell transformation and tumorigenesis”, PNAS, Nov. 20, 2001, vol. 98, No. 24, pp. 13601-13606.
Ruemenapf Tillmann et al., “N-Terminal Protease of Pestiviruses: Identification of Putative Catalytic Residues by Site-Directed Mutagenesis”, Journal of Virology, The American Society for Microbiology, vol. 72, No. 3, Mar. 1998, pp. 2544-2547.
Achmüller Clemens
Auer Bernhard
Podmirseg Silvio
Wechner Philipp
Werther Florian
Birch & Stewart Kolasch & Birch, LLP
Boehringer Ingelheim RCV GmbH & Co KG
Moore William W
Nashed Nashaat T
Sandoz AG
LandOfFree
Glutamic acid-modified classical swine fever virus... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Glutamic acid-modified classical swine fever virus..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Glutamic acid-modified classical swine fever virus... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4186288