Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...
Reexamination Certificate
2007-01-30
2007-01-30
Smith, Lynette R. F. (Department: 1645)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Blood proteins or globulins, e.g., proteoglycans, platelet...
C530S388100, C530S388200, C424S192100, C424S243100, C435S069700, C536S023700, C536S023500
Reexamination Certificate
active
10323903
ABSTRACT:
The present invention encompasses protective monoclonal antibodies that bind to peptidoglycan of Gram-positive bacteria. The antibodies also bind to whole bacteria and enhance phagocytosis and killing of the bacteria in vitro and block nasal colonization by Gram-positive bacteria in vivo. The invention also provides human, humanized and chimeric antibodies. The invention also sets forth the heavy chain and light chain variable regions of an antibody within the invention.
REFERENCES:
patent: 4596769 (1986-06-01), Shockman et al.
patent: 5571511 (1996-11-01), Fischer
patent: 5624904 (1997-04-01), Krieger et al.
patent: 5955074 (1999-09-01), Fischer
patent: 6610293 (2003-08-01), Fischer et al.
Proc Natl Acad Sci USA 1982 vol. 79 p. 1979.
Proc Natl Acad Sci USA 1988 vol. 85 3080-3084.
Amit et el Science vol. 233 747-753 1986.
Merkel, G.J. et al., “Characterization of a Monoclonal Antibody That Binds to an Epitope on Soluble Bacterial Peptidoglycan Fragments,”Clinical and Diagnostic Laboratory Immunology, vol. 8, No. 3, pp. 647-651 (2001).
Wergeland et al., “Antibodies to Various Bacterial Cell Wall Peptidoglycans in Human and Rabbit Sera,”Journal of Clinical Microbiology, 25(3):540-545 (1987).
Wergeland et al., “Antibodies to Staphylococcal Peptidoglycan and its Peptide Epitopes, Teichoic Acid, and Lipoteichoic Acid in Sera from Blood Donors and Patients with Staphylococcal infections,”Journal of Clinical Microbiology, 27(6): 1286-1291 (1989).
U.S. Appl. No. 10/323,904, filed Dec. 20, 2002, Kokai-kun et al.
U.S. Appl. No. 09/097,055, filed Jun. 15, 1998, Fischer et al.
U.S. Appl. No. 60/341,806, filed Dec. 21, 2001, Kokai-kun et al.
Atrih et al., “Analysis of Peptidoglycan Structure from Vegetative Cells ofBacillus subtilis168 and Role PBP 5 in Peptidoglycan Maturation,”Journal of Bacteriology, 181:3956-3966 (1999).
Bartal et al., “Current Methods in Hybridoma Formation,” (ed.)Methods of Hybridoma Formation, Humana Press, Clifton, New Jersey (1987).
Devereux et al., “A Comprehensive Set Of Sequence Analysis Programs For The VAX,”Nucl. Acids Res., 12:387-395 (1984).
Espersen et al., “Cross-Reactions BetweenStaphylococcusEpidermis and 23 Other Bacterial Species,”Acta Path. Microbial. Scand., Sect. B. 89: 253-260 (1981).
Fleer et al., “Septicemia Due to Coagulase-Negative Staphylococci In a Neonatal Intensive Care Unit: Clinical And Bacteriological Features And Contaminated Parenteral Fluids As A Source Of Sepsis,”Pediatr. Infect. Dis., 2: 426-431 (1983).
Foster, “Analysis of the Autolysins ofBacillus subtilis168 during Vegetative Growth and Differentiation by Using Renaturin Polyacrylamide Gel Electrophoresis,”Journal of Bacteriology, 174: 464-470 (1992).
Foster, “Molecular Analysis Of Three Major Wall-Associated Proteins OfBacillus subtilis168: Evidence For The Processing The Product Of A Gene Encoding A 258 kDa Precursor Two-Domain Ligand-Binding Protein,”Molecular Microbiology, 8:299-310 (1993).
Fournier, “Staphylococcu aureus,” Vaccines and Immunotherapy, Ch. 13, 166-177 (1991).
Green et al., “Antigen-Specific Human Monoclonal Antibodies From Mice Engineered With Human Ig Heavy And Light Chain YACs,”Nat Genet, 7(1): 13-21 (1994).
Gribskov et al., “Sigma Factors FromE. coli, B. subtilis, phage SP01, and phage T4 are Homologous Proteins,”Nucleic Acids Res., 14:6745-6763 (1986).
Hancock, “Bacterial Cell Surface Carbohydrates: Structure and Assembly,”Biochem. Soc. Trans., 25:183-187 (1997).
Jendeberg et al., “Engineering of Fc1and Fc3from Human Immunoglobulin G to Analyse Subclass Specificity for Staphyiococcal Protein A,”J. Immunol. Methods, 201:25-34(1997).
Kantor et al, “Development Of The Antibody Repertoire As Revealed By Single-Cell PCR of FACS-sorted B-cell Subsets,”Ann N Y Acad Sci, 764:224-227 (1995).
Kengatharan et al., “Mechanism of Gram-Positve Shock: Identification of Peptidoglycan And Lipoteichoic Acid Moieties Essential In the Induction Of Nitric Oxide Synthase, Shock and Multiple Organ Failure,”Journal of Experimental Medicine, 188: 305-315 (1998).
Kiser et al., “Development and Characterization of aStaphylococcus aureusNasal Colonization Model in Mice,”Infection and Immunity, 67: 5001-5006 (1999).
Lee, “The Prospects For Developing A Vaccine AgainstStaphylococcus aureus,”Trends in Micro., 4:162-66 (1996).
LoBuglio et al., “Mouse/Human Chimeric Monoclonal Antibody In Man: Kinetics And Immune Response,”P.N.A.S., 86:4220-4224 (1989).
Low et al, “Mimicking Somatic Hypermutation: Affinity Maturation of Antibodies Displayed on Bacteriophage Using a Bacterial Mutator Strain,”J Mol Biol, 260(3):359-68 (1996).
Merkus, “Cyclodextrin in nasal drug delivery,”Advan. Drug Deliv. Rev, 36:41-57 (1999).
Nakamura et al., “Uptake and Release of Budesonide from Mucoadhesive, pH-sensitive Copolymers and Their Application to Nasal Delivery,”J. Control. Release61:329-335. (1999).
Natsume, “Screening of Cationic Compounds as an Absorption Enhancer for Nasal Drug Delivery,”Int. J. Pharma, 185:1-12 (1999).
Navarre et al., “Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope,”Microbiology and Molecular Biology Reviews, 63:174-229 (1999).
Needleman et al., A General Method Applicable to the Search for Similarities in the Amino Acid Sequence of Two Proteins,J. Mol. Biol., 48;443-453 (1970).
Peterson et al., “Effect of Protein A on Staphylococcal Opsonization,”Infection and Immunity. 15:760-764 (1977).
Peterson et al., “Influence of Encapsulation on Staphylococcal Opsonization and Phagocytosis by Human Polymorphonuclear Leukocytes,”Infection and Immunity, 19:943-949 (1978).
Peterson et al., “The Key Role of Peptidoglycan in the Opsonization ofStaphylococcus aureus,”The Journal of Clinical Investigation, 61:597-609 (1978).
Quie et al., “Defective Phagocytosis of Staphylococci,”Annals New York Academy of Sciences, 236:233-243 (1974).
Ramkissoon-Ganorkar et al., “Modulating Insulin-Release Profile From pH/thermosensivite Polymeric Beads Through Polymer Molecular Weight,”J. Contr. Release, 59:287-298 (1999).
Romero-Vivas et al., Mortality Associated With Nosocomial Bacteremia Due To Methiciilin-ResistantStaphylococcus aureus, Clin. Infect. Dis., 21:1417-23 (1995).
Salton, “The Bacterial Cell Envelope—A Historical Perspective, in J.-M. Ghuyson and R. Hakenbeck (ed.),”Bacterial Cell Wall, Elsevier Science BV, Amsterdam, 1-22 (1994).
Schwab et al. “Increased Adherence OfStaphylococcus aureusFrom Cystic Fibrosis Lungs To Airway Epithelial Cells,”Am. Rev. Respir. Dis., 148:365-369 (1993).
Schwartz et al., “Matrices For Detecting Distant Relationships,”Atlas of Protein Sequence and Structure National Biomedical Research Foundation, 5 (suppl. 3):353-358 (1979).
Shulman et al., “A Better Cell Line for Making Hybridomas Secreting Specific Antibodies,”Nature, 276:269-270 (1978).
Smith et al., “Comparison Of Biosequences,”Adv. Appl. Math, 2:482-489 (1981).
Soto et al., “Bacitracin Versus Mupirocin ForStaphylococcus aureusNasal Colonization,”Infect. Cont. Hosp. Epidem, 20: 351-353 (1999).
Suzuki et al., “Mucosal Drug Delivery Using Cellulose Derivative As A Functional Polymer,”J. Control. Release, 62:101-107 (1999).
Timmerman et al., “Characterisation and Functional Aspects of Monoclonal Antibodies Specific for Surface Proteins of Coagulase-Negative Staphylococci,”J. Med. Micro., 35:65-71 (1991).
Tomasz, “The Staphylococcal Cell Wall, in V.A. Fischetti et al. (ed.),”Gram-Positive Pathogens, Ch. 36, 351-360 (2000).
Verbrugh et al., “Antibodies to Cell Wall Peptidoglycan ofStaphylococcus aureusin Patients with Se
Fischer Gerald Walter
Foster Simon J.
Kokai-Kun John Fitzgerald
Schuman Richard F.
Stinson Jeffrey R.
Baskar Padma
Biosynexus Incorporated
Lahive & Cockfield LLP
Mandragouras Esq. Amy E.
Smith Lynette R. F.
LandOfFree
Multifunctional monoclonal antibodies directed to... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Multifunctional monoclonal antibodies directed to..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Multifunctional monoclonal antibodies directed to... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3739824