Expression of recombinant human proteins in Tetrahymena

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S069100, C435S007100, C435S252300, C435S320100, C435S233000, C530S350000, C530S300000, C536S023100, C514S002600

Reexamination Certificate

active

06962800

ABSTRACT:
The present invention concerns a method for production of recombinant human proteins, in whichTetrahymenacells are transformed with recombinant DNA containing at least one functional gene that codes for a human protein, the recombinantTetrahymenacells are cultured, in which the gene that codes for a human protein is expressed and the proteins are then isolated. The present invention also concerns a corresponding method, in which the gene that codes for a human protein contains a human leader sequence that leads to secretion of the expressed protein.

REFERENCES:
patent: WO 00/46381 (2000-08-01), None
patent: WO 00/58483 (2000-10-01), None
Gaertig et al., Nature Biotechnology, vol. 17, pp. 462-465, May 1999.
Glick, et al, “Microbial Production of Therapeutic Agents,” Molecular Biotechnology, Chapter 10, ASM Press (Washington, DC), p. 227-252, (1998).
Ashford, et al, “Protein glycosylation,” Post-translational Process—A Practical Approach, Chapter 4, Oxford University Press, p. 135-174.
Glick, et al, “Recombinant Protein Production in Eukaryotic Cells,” Molecular Biotechnoloby, Chapter 7, ASM Press (Washington, DC), p. 145-169.
Castillo, “Organism Selection,” Biopress Technology, Chapter 2, XOMA Corporation (Berkeley, CA), p. 13-45.
Geisse, et al, “Eukaryotic Expression Systems: A Comparison,” Protein Expression and Purification 8, Academic Press Inc., p. 271-282, (1996).
Verma, et al, “Antibody engineering: Comparison of bacterial, yeast, insect and mammalian expression systems,” J. Immunological Methods, Elsevier, p. 165-181, (1998).
Moremen, et al, “Glycosidases of the asparagine-linked oligosaccharide processing pathway,” Glycobiology, vol. 4, Oxford University Press, p 113-125, (1994).
Tuite, et al, “Expressing cloned genes in the yeastsSaccharomyces cerevisiaeandPichia pastoris,” Protein Expression-A Practical Approach, Oxford University Press, Chap. 3, (1999).
Jenkins, et al, “Getting th glycosylation right: Implications for the biotechnology industry,” Nature Biotechnology, vol. 14, p. 175-981, (1996).
Henderson's Dictionary of Biological Terms, 10th Edition, Longman Scientific & Technical (Essex, England), p. 438, (1989).
Handbook of Protoctista, An Introduction to Physology, Cambridge University Press, (1995).
Kiy, et al, “Continuous high-cell-density fermentation of the ciliated protozoon Tetrahymena in a perfused bioreactor,” Applied Microbiology and Biotechnology, p. 141-146, (1992).
Taniguchi, et al, “Carbohydrates of Lysosomal Enzymes Secreted byTetrahymena pyriformis*, ” Journal of BIological Chemistry, vol. 260, p. 13941-13946, (1985).
Bruns, et al, “Biolistic Transformation of Macro- and Micronuclei,” Methods in Cell Biology, vol. 62, Chapter 27, Academic Press, p. 501-512, (1999).
Gaertig, et al, “Methods in Cell Biology,” vol. 62, Academic Press, p. 486-500, (1999).
Hai, et al, Methods in Cell Biology, vol. 62, Academic Press, p. 514-531, (1999).
Gaertig, et al, “Surface display of a parasite antigen in the ciliateTetrahymena thermophila,” Nature Biotecyhnology, vol. 17, p. 462-465, (May 1999).
Cassidy-Hanley, et al, “Germline and Somatic Transformation of MatingTetrahymena thermophila,” Genetics 146, p. 135-147, (1997).
Yao, et al, “Transformation of Tetrahymena to Cycloheximide resistance with a ribosomal protein gene through sequence replacement,” Proc. Natl. Acad. Sci., vol. 88, p. 9493-9497, (1991).
Kahn, et al, “Transformation ofTetrahymena thermophilaby microinjection of a foreign gene,” Proc. Natl. Acad. Sci., vol. 90, p. 9295-9299, (Oct. 1993).
Gaertig, et al, “Electroporation-mediated replacdement of a positively and negatively selectable B-tubulin gene inTetrahymena thermophila,” Proc. Natl. Acad. Sci., vol. 91, p. 4549-4553, (May 1994).
Boileau, et al, “Transformation ofParamecium tetraureliaby Electroporation or Particle Bombardment,” J. Euk. Microbiol, p. 56-65, (1999).
Kelly, “Genetic Transformation of Parasitic Protozoa,” Advances In Parasitology, vol. 39, Academic Press, p. 227-270, (1997).
Manstein, et al, “Cloning vectors for the production of proteins inDictyostelium discoideum,” Gene. 162, p. 129-134, (1995).
Jung, et al, “The production of recombinant glycoproteins with special reference to simple eukaryotes includingDictyostelium discoideum,” Biotechnol. Appl. Biochem 25, p. 3-8, (1997).
Hall, et al, Expression of a foreign gene inCHlamydomonas reinhardtii, Gene. 124, p. 75-81, (1993).
Schiedlmeier, et al, “Nuclear transformation of Volvox carteri,” Proc. Natl. Acad. Sci., vol. 91, p. 5080-5084, (May 1994).
ten Lohuis, et al, “Genetic transformation of dinoflagellates (Amphidinium and Symbiodinium): expression of GUS in microlagae using heterologous promoter constructs,” Plant Journal, p. 427-435, (1998).
Dunahay, et al, “Genetic Transformation Of The DiatomsCyclotella CrypticaAndNavicula Saprophila,” J. Phycol. 31, p. 1004-1012, (1995).
Benson, et al, “GenBank,” Nucleic Acids Research, vol. 28, No. 1, Oxford University Press, p. 15-18, (2000).
Wuitschick, et al, “Analysis of Genomic G+C Content, Condon Usage, Initiator Condon Context and Translation Termination Sites inTetrahymena thermophila,” J. Eukaryot. Microbiol., p. 239-247, (1999).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Expression of recombinant human proteins in Tetrahymena does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Expression of recombinant human proteins in Tetrahymena, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Expression of recombinant human proteins in Tetrahymena will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3507280

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.