Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or...
Reexamination Certificate
2003-06-27
2009-06-02
Navarro, Mark (Department: 1645)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
C435S041000, C435S440000
Reexamination Certificate
active
07541139
ABSTRACT:
A method is disclosed for producing a polypeptide with a modified activity or stability, by replacing an arginine residue capable of being ADP-ribosylated with a tryptophan or a phenylalanine. In one embodiment, compositions are provided that include polypeptides, such as alpha defensin, with arginine-to-tryptophan or arginine-to-phenylalanine substitutions, where the arginine residue is capable of being ADP-ribosylated. In another embodiment, methods are disclosed for modifying an immune response in a subject.
REFERENCES:
patent: 5386021 (1995-01-01), Moss et al.
patent: 5514600 (1996-05-01), Moss et al.
patent: 5716816 (1998-02-01), Moss et al.
patent: 5834310 (1998-11-01), Moss et al.
patent: 6015668 (2000-01-01), Hughes et al.
patent: 2003/0148936 (2003-08-01), Svendsen et al.
Rudinger, Characteristics of the amino acids as components of a peptide hormone sequence, 1976, University Park Press, Peptide Hormones Biol Council, pp. 1-7.
Higazi et al, Defensin stimulates the binding of lipoprotein (a) to human vascular endothelial and smooth muscle cells, 1997, Blood, vol. 89, pp. 4290-8.
Balducci et al.,Am J Respir Cell Mol Biol21(3), 337-346, 1999.
Bortel et al.,Autoimmunity33(3), 199-211, 2001, abstract only.
Han et al.,Biochem J318(Pt 3), 903-908, 1996.
Lesma et al.,J Immunol161(3), 1212-1219, 1998.
Takada et al.,J Biol Chem269(13), 9420-9423, 1994.
Weng et al.,J Biol Chem274(45), 31797-31803, 1999.
Yamada et al.,Arch Biochem Biophys308(1), 31-36, 1994, abstract only.
Balducci et al., “Selective Expression of RT6 Superfamily in Human Bronchial Epithelial Cells,”Am. J. Respir. Cell Mol. Biol. 21:337-346, 1999.
Bortel et al., “Levels of Art2+ cells but not soluble Art2 protein correlate with expression of autoimmune diabetes in the BB rat,”Automimmunity33(3):199-211, 2001, abstract only.
Bortell et al., “Nicotinamide adenine dinucleotide (NAD) and its metabolites inhibit T lymphocyte proliferation: role of cell surface NAD glycohydrolase and pyrophosphatase activities,”J. Immunol. 167(4):2049-2059, 2001, abstract only.
Bourgeois et al., “Identification of Regulatory Domains in ADP-ribosyltransferase-1 That Determine Transferase and NAD Glycohydrolase Activities,” 278(29):26351-26355, 2003.
Bredehorst et al., “Using secondary structure predictions and site-directed mutagenesis to identify and probe the role of potential active site motifs in the RT6 mono(ADP-ribosyl)transferase,”Adv Exp Med Biol419:185-189, 1997, abstract only.
Domenighini et al., “Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages,”Mol. Microbiol. 21(4):667-674, 1996, abstract only.
Greiner et al., Absence of the RT-6 T cell subset in diabetes-prone BB/W rats,J. Immunol. 136(1):148-151, 1986, abstract only.
Haag et al., “Premature stop codons inactivate the RT6 genes of the human and chimpanzee species,”J. Mol. Biol. 243(3):537-546, 1994, abstract only.
Han et al., “Regulation of NAD+ glycohydrolase activity by NAD+ -dependent auto-ADP-ribosylation,”Biochem. J. 318:903-908, 1996.
Hara et al., “Glutamic Acid 207 in Rodent T-cell RT-6 Antigens Is Essential for Arginine-specific ADP-ribosylation,”J. Biol. Chem., 271(47):29552-09555, 1996.
Hara et al., “Mouse Rt6.1 is a thiol-dependent arginine-specific ADP-ribodyltransferase,”Eur. J. Biochem. 259:289-294, 1999.
Karsten et al., “Expression and comparative analysis of recombinant rat and mouse RT6 T cell mono(ADP-ribosyl)transferase inE. coli,” Adv. Exp. Med. Biol. 419:175-180, 1997, abstract only.
Koch et al., “The rat T-cell differentiation marker RT6.1 is more polymorphic than its alloantigenic counterpart RT6.2,”Immunology65(2):259-265, 1988, abstract only.
Koch-Nolte et al., “Mouse T Cell Membrane Proteins Rt6-1 and Rt6-2 Are Arginine/Protein Mono(ADPribosyl)transferases and Share Seocndary Structure Motifs with ADP-ribosylating Bacterial Toxins,”J. Biol. Chem. 271(13):7686-7693, 1996.
Lesma et al., “Characterization of High Density Lipoprotein-Bound and Soluble RT6 Released Following Administration of Anti-RT6.1 Monoclonal Antibody,”J. Immunol. 161:1212-1219, 1998.
Maehama et al., “NAD+-dependent ADP-ribosylation of T Lymphocyte Alloantigen RT6.1 Reversibly Proceeding in Intact Rat Lymphocytes,”J. Biol. Chem. 270(39):22747-22751, 1995.
Maehama et al., “Increase in ADP-ribosyltransferase activity of rat T lymphocyte alloantigen RT6.1 by a single amino acid mutation,”FEBS Lett388(2-3):189-191, 1996, abstract only.
Maehama et al., “Molecular characterization of rat T lymphocyte alloantigen RT6.1 as an ADP-ribosyltransferase,”Adv Exp Med Biol419:181-183, 1997, abstract only.
Mojcik et al., “Characterization of RT6-bearing rat lymphocytes. II. Developmental relationships of RT6- RT6+ T cells,”Dev Immunol. 1(3):191-201, 1991, abstract only.
Moss et al., “ADP-ribosylarginie hydrolases and ADP-ribosyltransferases. Partners in ADP-ribosylation cycles,”Adv. Exp. Med. Biol. 419:25-33, 1997, abstract only.
Moss et al., “Characterization of Mouse Rt6.1 NAD:Arginine ADP-ribosyltransferase,”J. Biol. Chem. 272(7):4342-4346, 1997.
Moss et al., “Characterization of NAD:arginine ADP-ribosyltransferases,”Mol Cell Biochem193(1-2):109-113, 1999, abstract only.
Nemoto et al., “Cell surface ADP-ribosyltransferase regulates lymphocyte function-associated molecule-1 (LFA-1) function in T cells,”J. Immunol. 157(8):3341-3349, 1996, abstract only.
Okazaki et al., “Glycosylphosphatidylinositol-anchored and Secretory Isoforms of Mono-ADP-ribosyltransferases,”J. Biol. Chem. 273(37):23617-23620, 1998.
Paone et al., “ADP ribosylation of human neutrophil peptide-1 regulates its biological properties,”PNAS99(12);8231-8235, 2002.
Rigby et al., “Rat RT6.2 and mouse Rt6 locus 1 are NAD+: arginine ADP ribosyltransferases with auto-DP ribosylation activity,”J Immunol156(11):4259-4265, 1996, abstract only.
Stevens et al., “Regulatory Role of Arginine 204 in the Catalytic Activity of Rat Alloantigens ART2a and ARTb,”J. Biol. Chem. 278(22)19591-19596, 2003.
Takada et al., “Expression of NAD Glycohydrolase Activity by Rat Mammary Adenocarcinoma Cells Transformed with Rat T Cell Alloantigen RT6.2,”J. Biol. Chem. 269(13):9420-9423, 1994.
Thiele et al., “Biochemical characterization of the T-cell alloantigen RT-6.2,”Immunology59(2):195-201, 1986, abstract only.
Waite et al., “The RT6 rat lymphocyte alloantigen circulates in soluble form,”Cell Immunol, 152(1):82-95, 1993, abstract only.
Weng et al., “Modification of the ADP-ribosyltransferase and NAD Glycohydrolase Activities of a Mammalian Transferase (ADP-ribosyltransferase 5) by Auto-ADP-ribosylation,”J. Biol. Chem. 274(45):31797-31803, 1999.
Yamada et al., “Automodification of arginine-specific ADP-ribosyltransferase purified from chicken peripheral heterophils and alteration of the transferase activity,”Arch Biochem Biophys308(1):31-36, 1994, abstract only.
Zolkiewska et al., “Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle,”Proc. Natl. Acad. Sci. USA89:11352-11356, 1992.
Zolkiewska et al., “Integrin α7 as Substrate for a Glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the Surface of Skeletal Muscle Cells,”J. Biol. Chem. 268(34):25273-25276, 1993.
GenBank Accession No. NP—001916, Oct. 26, 2004.
GenBank Accession No. NP—001917, Oct. 26, 2004.
GenBank Accession No. NP—066290, Oct. 26, 2004.
GenBank Accession No. P11479, Sep. 15, 2003.
Yang et al., “Mammalian defensins in immunity: more than just microbicidal,”Trends in Immunology, 23(6):291-296, 2002.
Supplementary Partial European Search Report
Bortell Rita
Bourgeois Christelle
Moss Joel
Stevens Linda
Klarquist Sparkman LLP.
Navarro Mark
The United States of America as represented by the Department of
University of Massachusetts
LandOfFree
Tryptophan as a functional replacement for... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Tryptophan as a functional replacement for..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Tryptophan as a functional replacement for... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4082644