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Human leukocyte antigen Bw4 and Bw6 epitopes recognized by antibodies and natural killer cells

Lutz, Charles T.

Current Opinion in Organ Transplantation: August 2014 - Volume 19 - Issue 4 - p 436–441
doi: 10.1097/MOT.0000000000000103
HISTOCOMPATIBILITY: Edited by RenÉ J. Duquesnoy

Purpose of review To describe the structural basis of human leukocyte antigen (HLA) Bw4 and Bw6 epitopes that are recognized by antibodies and the KIR3DL1 natural killer cell receptor.

Recent findings Molecular modeling and X-ray crystallography have refined our understanding of Bw4 and Bw6. These epitopes had been defined by comparison of HLA allele sequences and by site-directed mutagenesis. Anti-Bw4 and anti-Bw6 antibodies and KIR3DL1 receptors recognize HLA α-1 α-helix residues 77–83 in combination with other HLA regions. The variability of HLA sequences within the 77–83 region and at other sites indicates that the Bw4 epitope is complex. Adding complexity, HLA-bound peptides influence Bw4 and Bw6 epitopes. These structures are recognized by diverse antibodies and KIR3DL1 allotypes. This diversity allowed a Bw4+ patient to produce anti-Bw4 antibody without breaking self-tolerance.

Summary Bw4 and Bw6 epitopes are best regarded as families of related structures that are recognized by a diverse array of antibodies and KIR3DL1 allotypes.

Department of Pathology and Laboratory Medicine and Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, Kentucky, USA

Correspondence to Charles T. Lutz, MD, PhD, Department of Pathology and Laboratory Medicine, University of Kentucky, 800 Rose Street, MS 117, Lexington, KY 40536-0298, USA. Tel: +1 859 323 0356; fax: +1 859 323 2094; e-mail:

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