Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Glycoprotein – e.g. – mucins – proteoglycans – etc.
Reexamination Certificate
2005-12-27
2005-12-27
Landsman, Robert S. (Department: 1647)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Glycoprotein, e.g., mucins, proteoglycans, etc.
C530S350000
Reexamination Certificate
active
06979727
ABSTRACT:
A recombinant conglutinin which contains a collagen region consisting of six amino acids containing two amino acid sequences Gly-Xaa-Xaa (SEQ ID NO:3, wherein Xaa stands for a protein-constituting amino acid), the neck region of natural conglutinin and the sugar chain recognition region of natural conglutinin, has an antiviral activity (virus neutralizing activity), and is expected to be applicable to drugs; and a process for detecting anti-influenza A virus activity of a mannose-binding protein (MBP) or a human mannose-binding protein (hMBP) involving the step of treating influenza A virus-infected cells with the MBP or hMBP and measuring the level of the suppression of the budding of the virus in the virus-infected cells. An MBP and an hMBP having an anti-influenza A virus activity are disclosed.
REFERENCES:
patent: 6110708 (2000-08-01), Wakamiya
patent: WO 91/07189 (1991-05-01), None
patent: WO 95/16697 (1995-06-01), None
Kawasaki N, et al. J Biochem (Tokyo). Sep. 1983;94(3):937-47.
Anders, E.M. et al., “Bovine and Mouse Serum β Inhibitors of Influenza A Viruses Are Mannose-Binding Lectins,”Proc. Natl. Acad. Sci. USA,87(12):4485-4489 (Jun., 1990).
Eda, S. et al., Report No. 2002, “Expression of Recombinant Conglutinin inE. coli,” Seikagaku,67(7):732 (Jul., 1995) (Japanese with English Translation).
Hartley, C.A. et al., “Two Distinct Serum Mannose-Binding Lectins Function as β Inhibitors of Influenza Virus: Identification of Bovine Serum β Inhibitor as Conglutinin,”J. Virology,66(7):4358-4363 (Jul., 1992).
Hoppe, H-J et al., “A Parallel Three Stranded α-helical Bundle at the Nucleation Site of Collagen Triple-Helix Formation,”FEBS Letters,344:191-195 (1994).
Kase, T. et al., Report No. 2006, “Study on Infection Inhibition Activities by Recombinant Conglutinin Against Influenza Viruses,”Seikagaku,67(7):732 (Jul., 1995).(Japanese With English Translation).
Kawasaki, N. et al., “Differentiation of Conglutination Activity and Sugar-Binding Activity of Conglutinin After Removal of NH2-Terminal 54 Amino Acid Residues by Endogenous Serine Protease(s),”Archives of Biochemistry and Biophysics,305(2):533-540 (Sep., 1993).
Kawasaki, N. et al., “Gene Organization and 5′-Flanking Region Sequence of Conglutinin: A C-Type Mammalian Lectin Containing A Collagen-Like Domain,”Biochemical Biophysical Research Communications,198(2):597-604 (Jan. 28, 1994).
Lee, Y-M et al., “Primary Structure of Bovine Conglutinin, a Member of the C-type Animal Lectin Family,”J. Biological Chemistry,266(5):2715-2723 (Feb. 15, 1991).
Lim, B-L et al., “Expression of the Carbohydrate Recognition Domain of Bovine Conglutinin and Demonstration of Its Binding to iC3b and Yeast Mannan,”Biochemical Biophysical Research Communications,218(1):260-266 (1996).
Liou, L.S. et al., “Bovine Conglutinin (BC) mRNA Expressed in Liver: Cloning and Characterization of the BC cDNA Reveals Strong Homology to Surfactant Protein-D,”Gene,141(2):277-281 (1994).
Lu, J. et al., “Purification, Characterization and cDNA Cloning of Human Lung Surfactant Protein D,”Biochem. J.,284:795-802 (1992).
Malhotra, R. et al., “Binding of Human Collectins (SP-A and MBP) to Influenza Virus,”Biochem. J.,304(2):455-461 (1994).
Malhotra, R. et al., “Interaction of C1q Receptor With Lung Surfactant Protein A,”Eur. J. Immunol.,22:1437-1445 (1992).
Nikkei Biotechnology, Article No. 4, p. 9 “Stable Expression of Recombinant Bkg Had Been Succeeded and Viral Inhibition Activities Had Also Been Confirmed,” (Sep. 25, 1995) (Japanese With English Translation).
Okuno, Y. et al., “Rapid Focus Reduction Neutralization Test of Influenza A and B Viruses in Microtiter System,”J. Clinical Microbiology,28(6):1308-1313 (Jun. 1990).
Reading, P.C. et al., “A Serum Mannose-Binding Lectin Mediates Complement-Dependent Lysis of Influenza Virus-Infected Cells,”Biochemical and Biophysical Research Communications,217(3):1128-1136 (Dec. 26, 1995).
Reading, P.C. et al., “A Serum Mannose-Binding Lectin Mediates Complement-Dependent Lysis of Influenza Virus-Infected Cells,”J. Leukocyte Biology, 0(Suppl.): 45(1993) (Abstract No. 72).
Sakamoto, T. et al., Report No. 2005, “Expression of Recombinant Human MBP inE. coli,” Seikagaku,67(7):732 (Jul., 1995).(Japanese With English Translation).
Sheriff, S. et al., “Human Mannose-Binding Protein Carbohydrate Recognition Domain Trimerizes Through a Triple α-helical Coiled-Coil.,”Structural Biology,1(11):789-794 (Nov., 1994).
Strang, C.J. et al., “Ultrastructure and Composition of Bovine Conglutinin,”Biochem. J.,234:381-389 (1986).
Sumiya, M. et al., “Molecular Basis of Opsonic Defect in Immunodeficient Children,”Lancet,337:1569-1570 (Jun. 29, 1991).
Super, M. et al., “Association of Low Levels of Mannan-Binding Protein With a Common Defect of Opsonisation,”Lancet,2(8674):1236-1239 (Nov. 25, 1989).
Suzuki, Y. et al., “Cloning and Sequencing of a cDNA Coding for Bovine Conglutinin,”Biochemical Biophysical Research Communications,191(2):335-342 (Mar. 15, 1993).
Taylor, M.E. et al., “Structure and Evolutionary Origin of the Gene Encoding a Human Serum Amnose-Binding Protein,”Biochem. J.262:763-771 (1989).
Wakamiya, N. et al., “Isolation and Characterization of Conglutinin as an Influenza A Virus Inhibitor,”Biochemical Biophysical Research Communications,187(3):1270-1278 (Sep. 30, 1992).
Wakamiya et al., “The Mannose Binding Protein and Conglutinin in Bovine Serum Have a Antiviral Activity Against Influenza Virus,”Glycoconjugate J.,8:235 (1991) (No. 12.27).
Wakamiya, N. et al., Report No. 1P1-16, “Preparation of Recombinant Animal Serum Lectin and Its Role on Early Defense Against Viral Infection,”Proc. of the Genl. Mtg. of the Japanese S. for Immun,25:113 (Oct. 28, 1995) (Japanese With English Translation).
Wang, J-Y et al., “A Recombinant Polypeptide, Composed of the α-helical Neck Region and the Carbohydrate Recognition Domain of Conglutinin, Self-Associates to Give a Functionally Intact Homotrimer,”FEBS Letters:376:6-10 (1995).
Fuso Pharmaceutical Industries Ltd.
Landsman Robert S.
Marshall & Gerstein & Borun LLP
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