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Ramifications Of The Hla-I Allelic Reactivity Of Anti-Hla-E*01:01 And Anti-Hla-E*01:03 Heavy Chain Monoclonal Antibodies In Comparison With Anti-Hla-I Igg Reactivity In Non-Alloimmunized Males, Melanoma-Vaccine Recipients, And End-Stage Renal Disease Patients, Mepur H Ravindranath, Narendranath M Ravindranath, Fatiha El Hilali, Senthamil R Selvan, Edward J Filippone
Ramifications Of The Hla-I Allelic Reactivity Of Anti-Hla-E*01:01 And Anti-Hla-E*01:03 Heavy Chain Monoclonal Antibodies In Comparison With Anti-Hla-I Igg Reactivity In Non-Alloimmunized Males, Melanoma-Vaccine Recipients, And End-Stage Renal Disease Patients, Mepur H Ravindranath, Narendranath M Ravindranath, Fatiha El Hilali, Senthamil R Selvan, Edward J Filippone
Department of Medicine Faculty Papers
Serum anti-HLA-I IgG are present in non-alloimmunized males, cancer patients, and transplant recipients. Anti-HLA-I antibodies are also present in intravenous immunoglobulin (IVIg), prepared from the plasma of thousands of healthy donors. However, the HLA-Ia reactivity of IVIg diminishes markedly after passing through HLA-E HC-affinity columns, suggesting that the HLA-I reactivity is due to antibodies formed against HLA-E. Hence, we examined whether anti-HLA-E antibodies can react to HLA-I alleles. Monoclonal IgG antibodies (mAbs) against HCs of two HLA-E alleles were generated in Balb/C mice. The antibodies were analyzed using multiplex bead assays on a Luminex platform for HLA-I reactivity. Beads coated …
Four Faces Of Cell-Surface Hla Class-I: Their Antigenic And Immunogenic Divergence Generating Novel Targets For Vaccines, Mepur H Ravindranath, Narendranath M Ravindranath, Senthamil R Selvan, Edward J Filippone, Carly J Amato-Menker, Fatiha El Hilali
Four Faces Of Cell-Surface Hla Class-I: Their Antigenic And Immunogenic Divergence Generating Novel Targets For Vaccines, Mepur H Ravindranath, Narendranath M Ravindranath, Senthamil R Selvan, Edward J Filippone, Carly J Amato-Menker, Fatiha El Hilali
Department of Medicine Faculty Papers
Leukocyte cell-surface HLA-I molecules, involved in antigen presentation of peptides to CD8+ T-cells, consist of a heavy chain (HC) non-covalently linked to β2-microglobulin (β2m) (Face-1). The HC amino acid composition varies across all six isoforms of HLA-I, while that of β2m remains the same. Each HLA-allele differs in one or more amino acid sequences on the HC α1 and α2 helices, while several sequences among the three helices are conserved. HCs without β2m (Face-2) are also observed on human cells activated by malignancy, viral transformation, and cytokine or chemokine-mediated inflammation. In the absence of β2m, the monomeric Face-2 exposes immunogenic …