Drug – bio-affecting and body treating compositions – Immunoglobulin – antiserum – antibody – or antibody fragment,... – Structurally-modified antibody – immunoglobulin – or fragment...
Reexamination Certificate
2005-08-04
2011-12-20
Ogunbiyi, Oluwatosin (Department: 1645)
Drug, bio-affecting and body treating compositions
Immunoglobulin, antiserum, antibody, or antibody fragment,...
Structurally-modified antibody, immunoglobulin, or fragment...
C424S130100, C424S131100, C530S350000, C530S387100, C530S387200, C530S388200, C530S388400
Reexamination Certificate
active
08080245
ABSTRACT:
Chimeric molecules that include a pathogen recognition module derived from a pathogen binding domain of a pathogen recognition protein, e.g., a toll-like receptor (TLR), CD14, BPI, MD-2, scavenger receptors (SRs), surfactant proteins (SP), C-reactive protein (CRP), Mannan-binding lectin (MBL), or complement Clq globular binding domain, an optional linker, and an Fc portion of an antibody are described and are useful for, e.g., drug discovery and treatment of conditions related to TLR signaling.
REFERENCES:
patent: 4438114 (1984-03-01), Boberg et al.
patent: 5578572 (1996-11-01), Horwitz et al.
patent: 5643570 (1997-07-01), Theofan et al.
patent: 6107076 (2000-08-01), Tang et al.
patent: 6462254 (2002-10-01), Vernachio et al.
patent: 6569112 (2003-05-01), Strahilevitz
patent: 6660843 (2003-12-01), Feige et al.
patent: 7157418 (2007-01-01), McDonald et al.
patent: 2003/0032090 (2003-02-01), Hardiman et al.
patent: 2003/0049648 (2003-03-01), Choi
patent: WO 2004/103294 (2004-12-01), None
patent: WO 2006/025995 (2006-03-01), None
Bassler et al. Current Opinion in Microbiology 1999, 2:582-587.
Paul. Fundamental Immunology, 5th edition. 2003 Chapter 3 (p. 56-58): The Immunoglobulin Hinge.
Chmura et al. Chest 2003; 124,379-382.
Abrahamson et al., “Biochemical characterization of recombinant fusions of lipopolysaccharide binding protein and bactericidal/permeability-increasing protein. Implications in biological activity,” Journal of Biological Chemistry, 272:2149-2155 (1997).
Ashkenazi et al., “Immunoadhesins as research tolls and therapeutic agents,” Curr. Opin. Immunol., 9(2):195-200 (1997).
Bazil and Strominger, “Shedding as a mechanism of down-modulation of CD14 on stimulated human monocytes,” J. Immunol., 147:1567-1574 (1991).
Bazil et al., “Biochemical characterization of a soluble form of the 53-kDa monocyte surface antigen,” Eur. J. Immunol., 16:1583-1589 (1986).
Beamer et al., “The BPI/LBP family of proteins: a structural analysis of conserved regions,” Protein Science, 7:906-914 (1998).
Bell et al., “The molecular structure of the Toll-like receptor 3 ligand-binding domain,” Proc. Natl. Acad. Sci. USA, 102(31):10976-10980 (2005).
Bell et al., “Leucine-rich repeats and pathogen recognition in Toll-like receptors,” TRENDS Immunology, 24(10):528-533 (2003).
Bufler et al., “Soluble lipopolysaccharide receptor (CD14) is released via two different mechanisms from human monocytes and CD14 transfectants,” Eur. J. Immunol., 25:604-610 (1995).
Chamow et al., “Immunoadhesins: principles and applications,” Trends Biotechnol., 14(2):52-60 (1996).
Froidevaux et al., “Anti-Toll-Like Receptor 4 (TLR4) Antibodies Protect from Lethal Endotoxemia but Not from Gram-Negative Septice Shock,” Gateway to the National Library of Medicine, [printed from http://gateway.nlm.nih.gov/MeetingAbstracts/102265282.html on Jan. 25, 2008].
Gioannini et al., “Isolation of an endotoxin-MD-2 complex that produces Toll-like receptor 4-dependent cell activation at picomolar concentrations,” Proc. Natl. Acad. Sci. USA, 101:4186-4191 (2004).
Goldbach-Mansky and Lipsky, “New Concepts in the Treatment of Rheumatoid Arthritis,” Annu. Rev. Med., 55:197-216 (2003).
Haziot et al., “The monocyte differentiation antigen, CD14, is anchored to the cell membrane by a phosphatidylinositol linkage,” J. Immunol., 141:547-552 (1988).
Haziot et al., “Neutrophil CD14: biochemical properties and role in the secretion of tumor necrosis factor-alpha in response to lipopolysaccharide,” J. Immunol., 150:5556-5565 (1998).
Hyakushima et al., “Interaction of soluble form of recombinant extracellular TLR4 domain with MD-2 enables lipopolysaccharide binding and attenuates TLR4-mediated signaling,” J. Immunol., 173(11):6949-6954 (2004).
Jit et al., “TNF-alpha neutralization in cytokine-driven diseases: a mathematical model to account for therapeutic success in rheumatoid arthritis but therapeutic failure in systemic inflammatory response syndrome,” Rheumatology, 44:323-331 (2005).
Juan et al., “Soluble CD14 truncated at amino acid 152 binds lipopolysaccharide (LPS) and enables cellular response to LPS,” J. Biol. Chem., 270:1382-1387 (1995).
Kennedy et al., “A complex of soluble MD-2 and lipopolysaccharide serves as an activating ligand for Toll-like receptor 4,” J. Biol. Chem., 279:34698-34704 (2004).
LaBeta et al., “Release from a human monocyte-like cell line of two different soluble forms of the lipopolysaccharide receptor, CD14,” Eur. J. Immunol , 23:2144-2151 (1993).
Landmann et al., “Increased circulating soluble CD14 is associated with high mortality in gram-negative septic shock,” J. Infect. Dis., 171:639-644 (1995).
Latz et al., “TLR9 signals after translocating from the ER to CpG DNA in the lysosome,” Nat. Immunol , 5(2):190-198 (2004).
Lawson et al., “Treatment of murine lupus with cDNA encoding IFN-γR/Fc,” J. Clin. Invest., 106:207-215 (2000).
LeBouder et al., “Soluble forms of Toll-like receptor (TLR)2 capable of modulating TLR2 signaling are present in human plasma and breast milk,” J. Immunol., 171(12):6680-6689 (2003).
Meng et al., “Antagonistic antibody prevents toll-like receptor 2-driven lethal shock-like syndromes,” J. Clin. Invest., 113(10):1473-1481 (2004).
Navia et al., “Crystal structure of galactan-binding mouse immunoglobulin J539 Fab at 4.5-A resolution,” Proc. Natl. Acad. Sci. USA, 76:4071-4074 (1979).
Pugin et al., “Soluble MD-2 activity in plasma from patients with severe sepsis and septic shock,” Blood, 104(13):4071-4079 (2004).
R&D Systems, “Recombinant Mouse CD14/Fc Chimera,” Catalog No. 982-CD (2001).
Ram et al., “C4bp binding to porin mediates stable serum resistance ofNeisseria gonorrhoeae,” Int. Immunopharmacol., 1:423-432 (2001).
Ram et al., “Binding of C4b-binding protein to porin: a molecular mechanism of serum resistance ofNeisseria gonorrhoeae,” J. Exp. Med., 193:281 (2001).
Robinson et al., “Optimizing the stability of single-chain proteins by linker length and composition mutagenesis,” Proc. Natl. Acad. Sci. USA, 95:5929-5934 (1998).
Rothenfusser et al., “Recent advances in immunostimulatory CpG oligonucleotides,” Curr. Opin. Mol. Ther., 5(2):98-106 (2003).
Shimazu et al., “MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4,” J. Exp. Med., 189(11):1777-1782 (1999).
Takeuchi et al., “Discrimination of bacterial lipoproteins by Toll-like receptor 6,” Int. Immunol., 13:933-940 (2001).
Takeuchi et al., “Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins,” J. Immunol , 169:10-14 (2002).
Viriyakosol and Kirkland, “The N-terminal half of membrane CD14 is a functional cellular lipopolysaccharide receptor,” Infect. Immun , 64(2):653-656 (1996).
Visintin et al., “Lysines 128 and 132 enable lipopolysaccharide binding to MD-2, leading to Toll-like receptor-4 aggregation and signal transduction,” J. Biol. Chem., 278(48):48313-48320 (2003).
Froidevaux, R.T. et al., “Anti-Toll-Like Receptor 4 (TLR4) Antibodies Protect from Lethal Endotoxemia but Not from Gram-Negative Septic Shock,” Abst Intersci Conf Antimicrob Agents Chemother Intersci Conf antimicro angents Chemother, Sep. 14-17, 2003 (Lusanee, Switzerland), abstract No. B-1506.
Akashi et al., “Lipopolysaccharide interaction with cell surface Toll-like receptor 4-MD 2: higher affinity than that with MD 2 or CD14,”J. Exp. Med., 198:1035 (2003).
Beutler, “Inferences, questions and possibilities in Toll-like receptor signalling,”Nature, 430:257 (2004).
Fitzgerald et al., “LPS-TLR4 signaling to IRF-3/7 and NR-kappaB involves the
Golenbock Douglas T.
Visintin Alberto
Fish & Richardson P.C.
Ogunbiyi Oluwatosin
University of Massachusetts
LandOfFree
Anti-pathogen immunoadhesins does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Anti-pathogen immunoadhesins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Anti-pathogen immunoadhesins will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4267545