Abstract:
Provided are isolated complexes comprising a major histocompatibility complex (MHC) class II and a type I diabetes-associated GAD autoantigenic peptide, the isolated complex having a structural conformation which enables isolation of a high affinity entity which comprises an antigen binding domain capable of specifically binding to a native conformation of a complex composed of the MHC class II and the type I diabetes-associated GAD autoantigenic peptide; and isolated high affinity entities comprising an antigen binding domain capable of specifically binding the complex, wherein the isolated high affinity entity does not bind to the MHC class II in an absence of the diabetes-associated GAD autoantigenic peptide, wherein the isolated high affinity entity does not bind to the diabetes-associated GAD autoantigenic peptide in an absence of the MHC class II; and methods and kits using same for diagnostic and therapeutic purposes.
Abstract:
Provided are isolated high affinity entities which comprise an antigen binding domain which specifically binds a soluble T-cell receptor ligand comprising a two-domain beta1-alpha1 of a major histocompatibility complex (MHC) class II, wherein said antigen binding domain does not bind a complex comprising a four-domain alpha1-beta1/alpha2-beta2 MHC class II. Also provided are methods and kits using same for detecting and sequestering soluble two-domain T cell receptor ligands in a sample.
Abstract:
Provided are isolated complexes comprising a major histocompatibility complex (MHC) class II and a type I diabetes-associated autoantigenic peptide, the isolated complex having a structural conformation which enables isolation of a high affinity entity which comprises an antigen binding domain capable of specifically binding to a native conformation of a complex composed of the MHC class II and the type I diabetes-associated autoantigenic peptide; and isolated high affinity entities comprising an antigen binding domain capable of specifically binding the complex, wherein the isolated high affinity entity does not bind to the MHC class II in an absence of the diabetes-associated autoantigenic peptide, wherein the isolated high affinity entity does not bind to the diabetes-associated autoantigenic peptide in an absence of the MHC class II; and methods and kits using same for diagnostic and therapeutic purposes.
Abstract:
An immuno-molecule which comprises a soluble human MHC class I effector domain; and an antibody targeting domain which is linked to the soluble human MHC class I effector domain, methods of making same and uses thereof.
Abstract:
Provided are antibodies comprising an antigen recognition domain capable of binding an MHC molecule being complexed with a human immunodeficiency virus (HIV) peptide, wherein the antibody does not bind the MHC molecule in an absence of the complexed peptide, and wherein the antibody does not bind the peptide in an absence of the MHC molecule. Also provided are methods of using same for diagnosing HIV infection and treating AIDS.
Abstract:
Disclosed are protein ligands comprising an immunoglobulin heavy chain variable (VH) domain and an immunoglobulin light chain variable (VL) domain, wherein the proteins bind a complex comprising an MHC and a peptide, do not substantially bind the MHC in the absence of the bound peptide, and do not substantially bind the peptide in the absence of the MHC, and the peptide is a peptide fragment of gp100, MUC1, TAX, or hTERT. Also disclosed are methods of using and identifying such ligands.
Abstract:
Provided are methods of generating a functional mammalian single chain MHC class I complex in prokaryotic expression systems and a host cell transformed with expression construct(s) capable of expressing a functional human single chain MHC class I complex capable of presenting specific antigenic peptides restricted to specific CTL clones.
Abstract:
An artificial receptor comprises a non-biological surface having unique surface electrical properties that vary over its extent, the electrical properties being such as to configure an electrical field about the surface to provide specific binding for a target moiety such as a biological moiety.
Abstract:
Disclosed are protein ligands comprising an immunoglobulin heavy chain variable (VH) domain and an immunoglobulin light chain variable (VL) domain, wherein the proteins bind a complex comprising an MHC and a peptide, do not substantially bind the MHC in the absence of the bound peptide, and do not substantially bind the peptide in the absence of the MHC, and the peptide is a peptide fragment of gp100, MUC1, TAX, or hTERT. Also disclosed are methods of using and identifying such ligands.
Abstract:
A method of determining responsiveness to cancer treatment is disclosed. The method comprises analyzing a frequency of tumor infiltrating lymphocytes (TILs) having a CD8+CD28−CD152− signature in a sample of the subject, wherein a frequency of TILs having the CD8+CD28−CD152− signature above a predetermined level is indicative of a positive responsiveness to cancer treatment. Other signatures reflecting responsiveness to cancer treatment are also disclosed. In addition, methods of treating cancer based on these signatures are also disclosed.