Chemistry: molecular biology and microbiology – Micro-organism – per se ; compositions thereof; proces of... – Fungi
Reexamination Certificate
2007-03-20
2007-03-20
Wax, Robert A. (Department: 1656)
Chemistry: molecular biology and microbiology
Micro-organism, per se ; compositions thereof; proces of...
Fungi
C435S183000, C435S320100, C530S350000, C536S023740
Reexamination Certificate
active
10474431
ABSTRACT:
A plasmid is constructed so as to express a fused protein of a sugar chain-binding protein domain with a desired protein. Then this plasmid is transferred into cells and thus the protein is expressed in the cell surface layer. This method is particularly adequate in case of expressing a protein having an activity in the C-terminal portion in cell surface layer.
REFERENCES:
patent: 6027910 (2000-02-01), Klis et al.
patent: 11-290078 (1999-10-01), None
patent: 11-290078 (1999-10-01), None
patent: 8-506484 (2001-05-01), None
patent: WO 94/18330 (1994-08-01), None
patent: WO 00/66755 (2000-11-01), None
Murai, et al., “Construction of a Starch-Utilizing Yeast by Cell Surface Engineering,”Applied and Environmental Microbiology, Apr. 1997, pp. 1362-1366.
Watari, et al., “Breeding of Flocculent IndustrialSaccharomyces cerevisiaeStrains by Introducing the Flocculation Gene FLOI,”Agric. Biol. Chem., 55 (6), 1991, pp. 1547-1552.
Stewart, et al., “The Identification, Characterization, and Mapping of a Gene for Flocculation inSaccharomycessp.,”Can. J. Microbiol, vol. 23, 1977, pp. 441-447.
Russell, et al., “Revised Nomenclature of Genes that Control Yeast Flocculation,”J. Inst. Brew., May-Jun. 1980., vol. 86, pp. 120-121.
Lewis, et al., “The Genetics of Yeast Flocculation,”J. Inst. Brew., May-Jun. 1976, vol. 82, pp. 158-160.
Russell, et al., “Spheroplast Fusion of Brewer's Yeast Strains,”J. Inst. Brew., Mar.-Apr., 1979, vol. 85, pp. 95-98.
Yamashita, et al., “Isolation of Glucoamylase-non-producing Mutants in the YeastSaccharomyces diastaticus,” Agric. Biol. Chem., 48 (1), 1984, pp. 131-135.
Beer, et al., “Cloning, Expression, Characterization and Role of the Leader Sequence of a Lipase fromRhizopus oryzae,” Biochimica et Biophysics Acta1399 (1998), pp. 173-180.
Kaieda, et al., “Biodiesel Fuel Production from Plant Oil Catalyzed byRhizopus oryzaeLipase in a Water-Contaning System without an Organic Solvent,”Journal of Bioscience and Bioengineering, vol. 88, No. 6, 1999, pp. 627-631.
Smit, et al., “Flocculence ofSaccharomyces cerevisiaeCells Is Induced by Nutrient Limitation, with Cell Surface Hydrophobizity as a Major Determinant,”Applied and Environmental Microbiology, Nov. 1992, pp. 3709-3714.
Kondo, et. al., “Development of Cell Display Systems and Their Utilization,”Applied and Environmental Microbiology, vol. 5, No. 2, 2001, pp. 121-126. (Partial Translation).
Lipke, et al, “AGal is the Structural Gene for theSaccharomyces cerevisiaeα-Agglutinin, a Cell-Surface Glycoprotein Involved in Cell-Cell Interactions during Mating,”Molecular&Cellular Biology, Aug. 1989. p. 3155-3165, American Society for Microbiology.
Bony, et al, “Localization and Cell Surface Anchoring of theSaccharomyces cerevisiaeFlocculation Protein Flo1p,”Journal of Bacteriology, Aug. 1997, p. 4929-4936, American Society for Microbiology.
Schreuder, et al, “Immobilizing proteins on the surface of yeast cells,”TIBTECH, Apr. 1996, vol. 14, Elsevier Science Ltd.
Matsumoto, et al., “Construction of Yeast Strains with High Cell Surface Lipase Activity by Using Novel Display Systems Based on the Flo1p Flocculation Functional Domain,”Applied&Environmental Microbiology, Sep. 2002, vol. 68, No. 9, p. 417-4522. American Society for Microbiology.
Kondo, et al., “Yeast cell-surface display—applications of molecular display,”Appl. Microbiol. Biotechnical, 2004, 64: p. 28-40, published online: Jan. 10, 2004, Spring-Verlag 2004.
Supplementary European Search Report, Sep. 29, 2004.
Kondo, et al., “Yeast Cell Surface Display Applications of Molecular Display,”Gene and Medicine, (2004) 64: 28-40.
Steen, et al., “AcmA of Lactococcur lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning,”FEBS Journal272 (2005) 2854-2868.
Steen, et al., “Cell Wall Attachment of a Widely Distributed Peptidoglycan Binding Domain Is Hindered by Cell Wall Constituents,”The Journal of Biological Chemistry, vol. 278, No. 26, Issue of Jun. 27, p. 23874-23881, 2003, USA.
Raha, et al., “Cell Surface Display System forLactococcus lactis: A Novel Development for Oral Vaccine,”Applied Genetics and Molecular Biotechnology, (2005) 68: 75-81.
Fukuda Hideki
Kondo Akihiko
Matsumoto Takeshi
Noda Hideo
Jagtiani & Guttag
Kansai Chemical Engineering, Co.
Wax Robert A.
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