THE CLINICAL IMPORTANCE OF VARIATION WITHIN THE HLA-Bw4 COMPLEX

Abstract

This report identifies an antibody to a sub-group of the Bw4 public specificity and also confirms the need for sequence-level analysis in the tissue-typing laboratory to determine future unacceptable mismatches.

High-resolution, three-dimensional modeling of human leukocyte antigen class I structure and surface electrostatic potential reveals the molecular basis for alloantibody binding epitopes

“…The majority of HLA alleles that express the Bw4 epitope incorporate the motifs T-A-L-R, I-A-L-R, and T-L-L-R at positions 80 -83, and asparagine, serine, or aspartic acid at position 77 [30]. Differences in Bw4 specific alloantibody binding patterns are well documented among HLA specificities that express the Bw4 epitope [31,32]. The structural and physiochemical characteristics of the Bw4 epitope expressed on the common HLA-B alleles was modeled to determine whether the observed heterogeneity in Bw4 specific antibody binding patterns can be explained by differences in topography and surface electrostatic potential.…”