Comparative ligand mapping from MHC positive cells

Details Comparative ligand mapping from MHC positive cells Comparative ligand mapping from MHC positive cells

2001-10-10

2009-06-02

Saunders, David A. (Department: 1644)

Chemistry: natural resins or derivatives; peptides or proteins;

Peptides of 3 to 100 amino acid residues

11 to 14 amino acid residues in defined sequence

C530S328000, C530S329000

Reexamination Certificate

active

07541429

ABSTRACT:
The present invention relates generally to a methodology for the isolation, purification and identification of peptide ligands presented by MHC positive cells. In particular, the methodology of the present invention relates to the isolation, purification and identification of these peptide ligands from soluble class I and class II MHC molecules which may be uninfected, infected, or tumorgenic. The methodology of the present invention broadly allows for these peptide ligands and their comcomittant source proteins thereof to be identified and used as markers for infected versus uninfected cells and/or tumorgenic versus nontumorgenic cells with said identification being useful for marking or targeting a cell for therapeutic treatment or priming the immune response against infected cells.

REFERENCES:
patent: 4683202 (1987-07-01), Mullis
patent: 5256541 (1993-10-01), Pouletty et al.
patent: 5270169 (1993-12-01), Chang et al.
patent: 5292641 (1994-03-01), Pouletty
patent: 5482841 (1996-01-01), Buelow
patent: 5710248 (1998-01-01), Grose
patent: 5750367 (1998-05-01), Chan
patent: 5776746 (1998-07-01), Denney, Jr.
patent: 5798209 (1998-08-01), Chan
patent: 5830995 (1998-11-01), Shoyab et al.
patent: 5846827 (1998-12-01), Celis et al.
patent: 6001365 (1999-12-01), Peterson et al.
patent: 6232445 (2001-05-01), Rhode et al.
patent: 6255073 (2001-07-01), Cai et al.
patent: 2002/0131960 (2002-09-01), Sadelain et al.
patent: WO 95/11702 (1995-05-01), None
patent: WO 97/46256 (1997-12-01), None
patent: WO 98/06749 (1998-02-01), None
patent: WO 00/23053 (2000-04-01), None
“Molecular Cloning A Laboratory Manual”, Maniatis et al., Selected Text “RNA-Dependent DNA Polymerase” p. 129, “Isolation of mRNA from Mammalian Cells” pp. 191-193, Cold Harbor Spring Laboratory (1982).
“Large Scale Production of Murine Monoclonal Antibodies Using Hollow Fiber Bioreactors”, Evans et al., BioTechniques, 6(8):763-767 (1988).
“HIV-1 Reverse Transcriptase is a Target for Cytotoxic T Lymphocytes in Infected Individuals”, Walker et al., Science, 240(4848):64-66 (1988).
“Assembly of MHC Class 1 Molecules Analyzed in Vitro”, Townsend et al., Cell, 62(6):285-295 (1990).
“Allele-Specific Motifs Revealed by Sequencing of Self-Peptides Eluted from MHC Molecules”, Falk et al., Nature, 351(6324):290-296, (1991).
“Characterization of Peptides Bound to the Class 1 MHC Molecule HLA-A2.1 by Mass Spectrometry”, Hunt et al., Science, 255(5049):1261-1263 (1992).
“Peptide Binding to HLA-A2 and HLA-827 Isolated fromEscherichia coli”, Parker et al., The Journal of Biological Chemistry, 267(8):5451-5459 (1992).
“Endogenous Peptides of Soluble Major Histocompatibility Complex Class I Molecule, H-2Lds: Sequence Motif, Quantitative Binding, and Molecular Modeling of the Complex”, Corr et al., J. Exp. Med., 176(6):1681-1692 (1992).
“The Specificity and Efficiency of Endogenous Peptides in the Induction of HLA Class I Alpha Chain Refolding”, Tanigaki, Eur J. Immunol., 22(8):2177-2180 (1992).
“Can One Predict Antigenic Peptides for MHC Class I-Restricted Cytotoxic T Lymphocytes Useful for Vaccination?”, Calin-Laurens et al., Vaccine, 11(9): 974-978 (1993).
“Direct Identification of an Endogenous Peptide Recognized by Multiple HLA-A2.1-Specific Cytotoxic T Cells”, Henderson et al., Proc. Natl. Acad. Sci. USA, 90:10275-10279 (1993).
“Characterization of Endogenous Peptides Eluted from the Class I MHC Molecule HLA-B7 Determined by Mass Spectrometry and Computer Modeling”, Huczko et al., J. Immunol., 151 (5):2572-2587 (1993).
“Flow-Cytometric Determination of Peptide-Class I Complex Formation Identification of p53 Peptides that Bind to HLA-A2”, Zeh et al., Human Immunology, 39:79-86 (1994).
“Peptide Binding to the Most Frequent HLA-A Class I Alleles Measured by Quantitative Molecular Binding Assays”, Sette et al., Molecular Immunology, 31(11): 813-822 (1994).
“Binding of a Peptide Antigen to Multiple HLA Alleles Allows Definition of an A2-Like Supertype”, del Guercio et al., J Immunol., 154(2):685-693 (1995).
“An HLA Class I Peptide-Binding Assay Based on Competition for Binding to Class I Molecules on Intact Human B Cells Identification of Conserved HIV-I Polymerase Peptides Binding to HLA-A0301”, van der Burg et al., Human Immunology, 44:189-198 (1995).
“Measuring Interactions of MHC Class I Molecules using Surface Plasmon Resonance”, Khilko et al., J. Immunol. Methods, 183(1):77-94 (1995).
“Peptide Motifs of HLA-B58, B60, B61 and B62 Molecules”, Falk et al., Immunogenetics, 41(2-3):165-168 (1995).
“An Empirical Method for the Prediction of T-Cell Epitopes”, Davenport et al., Immunogenetics, 42(5):392-397 (1995).
“Peptide Motifs of HLA-838 and 839 Molecules”, Falk et al., Immunogenetics, 41(2-3):162-164, (1995).
“Detailed Motifs for Peptide Binding to HLA-A0201 Derived from Large Random Sets of Peptides Using Cellular Binding Assay”, Drifthout et al., Human Immunology, 43(1):1-12, (1995).
“Analysis of the Structure of Naturally Processed Peptides Bound by Class I and Class II Major Histocompatibility Complex Molecules”, Appella et al., EXS., 73:105-119 (1995).
“Mapping and Ranking of Potential Cytotoxic T Epitopes in the p53 Protein: Effect of Mutations and Polymorphism on Peptide Binding to Purified and Refolded HLA Molecules”, Gnjatic et al., Eur. J. Immunol., 25(6):1638-1642 (1995).
“Simplified High-Sensitivity Sequencing of a Major Histocompatibility Complex Class I-Associated Immunoreactive Peptide Using Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry”, Woods et al., 226(1):15-25 (1995).
“Probing HLA-B7 Conformational Shifts Induced by Peptide-Binding Groove Mutations and Bound Peptide with Anti-HLA Monoclonal Antibodies”, Smith et al., 157(6):2470-2478 (1996).
“Mass Spectrometry. Ionization Methods and Instrumentation”, Chapman, Method Mol Biol., 61:9-28 (1996).
“HLA Allele Selection for Designing Peptide Vaccines”, Kamalakar et al, Genetic Analysis: Biomolecular Engineering, 13:81-86 (1996).
“Class I-Restricted Presentation of an HIV-I gp41 Epitope Containing an N-Linked Glycosylation Site. Implications for the Mechanism of Processing of Viral Envelope Proteins”, Ferris et al., J Immunol., 156(2):834-840 (1996).
“Evaluation of Hollow Fiber Bioreactors as an Alternative to Murine Ascites Production for Small Scale Monoclonal Antibody Production”, Jackson et al., J. Immunol. Methods, 189(2):217-231 (1996).
“T-Cell Epitope Determination”, Walden, Curr Opin Immunol., 8(1):68-74 (1996).
“Large-Scale Production of Class I Bound Peptides: Assigning a Signature to HLA-B1501”, Prilliman et al., Immunogentics, 45(6):379-385 (1997).
“HLA Class I Binding Motifs Derived from Random Peptide Libraries Differ at the Cooh Terminus from Those of Eluted Peptides”, Davenport et al., J. Exp. Med., 185(2): 367-371 (1997).
“Stability of Empty and Peptide-Loaded Class II Major Histocompatibility Complex Molecules at Neutral and Endosomal pH: Comparison to Class I Proteins”, Reich et al., Proc. Natl. Acad. Sci. USA, 94:2495-2500 (1997).
“Human Peptide Transporter Deficiency: Importance of HLA-B in the Presentation of Tap-Independent EBV Antigens”, de la Salle et al., J. Immunol., 158(10):4555-4563 (1997).
“A Novel, Highly Efficient Peptide-HLA Class I Binding Assay Using Unfolded Heavy Chain Molecules: Identification of HIV-1 Derived Peptides That Bind to HLA-A0201 HLA-A0301”, Tan et al., J. Immunol. Methods, 205(2): 201-209 (1997).
“Large-Scale Production of Class I Bound Peptides: Assigning a Signature to HLA-B1501”, Prilliman et al., Immunogenetics, 45(6):379-385 (1997).
“Synthetic Peptides Based on Chlamydia tra

Affiliated with

Also associated with

Rating

Comparative ligand mapping from MHC positive cells does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Comparative ligand mapping from MHC positive cells, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Comparative ligand mapping from MHC positive cells will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4063064