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  • Serologic
  • Serologic and immunochemical assays have shown that the two MoAbs recognize the same (or spatially close) determinant expressed by HLA-B7,B27,Bw42,Bw54,Bw55,Bw56,Bw67, and Bw73 alloantigens. (semanticscholar.org)
  • Epitopes
  • We observed that C-clade-infected individuals with HLA-B*07:02 target a broader range of Gag epitopes, and to higher magnitudes, than do individuals infected with B-clade infection. (ox.ac.uk)
  • specificity
  • The unique binding specificity of LILRB5 for HLA-class I heavy chains probably results from differences in the D1 and D2 immunoglobulin-like binding domains which are distinct from other LILR which bind to β2m-associated HLA-class I. (ox.ac.uk)
  • The monoclonal antibodies (MoAbs) KS3 and KS4 are secreted by hybridomas constructed with splenocytes from a BALB/c mouse sequentially immunized with the cultured lymphoid cells JKu and LG-2 which share only the HLA-B27 specificity. (semanticscholar.org)
  • Binding
  • We screened for LILR binding to HLA-class I by tetramer staining of 293T cells transfected with LILRA1, A4, A5 A6 and LILRB2 and LILRB5. (ox.ac.uk)
  • We also studied HLA class I tetramer binding to LILRB5 on peripheral monocyte cells. (ox.ac.uk)
  • LILRB5 binding to HLA-class I heavy chains was confirmed by co-immunoprecipitation. (ox.ac.uk)
  • Binding to B27 appeared to be slightly stronger than to B7 and stronger than to B22 in an indirect binding assay, but no difference in B7 and B27 binding could be detected by Scatchard analysis. (semanticscholar.org)
  • heavy chains
  • HLA-B7 and B27 heavy chains co-immunoprecipitated with LILRB5 in transduced B and rat basophil RBL cell lines. (ox.ac.uk)
  • versus
  • Although this epitope was also targeted in B-clade infection, the escape mutant S357S is present at higher frequency in B-clade infection than in C-clade infection (70% versus 43% in HLA-B*07:02-negative subjects). (ox.ac.uk)