Abstract
KIR3DL1 is among the most interesting receptors studied, within the killer immunoglobulin receptor (KIR) family. Human leukocyte antigen (HLA) class I Bw4 epitope inhibits strongly Natural Killer (NK) cell's activity through interaction with KIR3DL1 receptor, while Bw6 generally does not. This interaction has been indicated to play an important role in the immune control of different viral infectious diseases. However, the structural interaction between the KIR3DL1 receptor and different HLA-B alleles has been scarcely studied. To understand the complexity of KIR3DL1-HLA-B interaction, HLA-B alleles carrying Bw4/Bw6 epitope and KIR3DL1∗001 allele in presence of different peptides has been evaluated by using a structural immunoinformatic approach. Different energy minimization force fields (ff) have been tested and NOVA ff enables the successful prediction of ligand-receptor interaction. HLA-B alleles carrying Bw4 epitope present the highest capability of interaction with KIR3DL1∗001 compared to the HLA-B alleles presenting Bw6. The presence of the epitope Bw4 determines a conformational change which leads to a stronger interaction between nonpolymorphic arginine at position 79 of HLA-B and KIR3DL1∗001 136–142 loop. The data shed new light on the modalities of KIR3DL1 interaction with HLA-B alleles essential for the modulation of NK immune-mediated response.
Highlights
Killer immunoglobulin receptor (KIR)3DL1 is among the most interesting receptors studied within the killer immunoglobulin receptor (KIR) family
The relative positions 7 and 8 of the peptide bound to Human leukocyte antigen (HLA) class I are critical for the recognition since they directly interact with amino acids from HLA-B at positions 77, 80, 81, 82, and 83 which form Bw4/Bw6 epitope [7, 8]
To assess the complexity of KIR3DL1-HLA-B interaction and its role in the immune regulation we studied the formation of complexes between different HLA-B alleles carrying Bw4/Bw6 and KIR3DL1∗001 allele in presence of different peptides using a structural immunoinformatic approach
Summary
Killer immunoglobulin receptor (KIR)3DL1 is among the most interesting receptors studied within the KIR family It interacts with polymorphisms located on human leukocyte antigen (HLA)-A and HLA-B molecules that have been widely associated with the control of several infections and autoimmune disorders [1,2,3,4,5,6]. KIR3DL1 D1 domain is capable to interact both with the HLA bond peptide and the HLA class I molecule alpha-1 domain including the Bw4/Bw6 epitope [12] This notion supports the observed differences in NK mediated cytotoxic effects due to peptides with different amino acids residues in the relative positions P7 and P8 [2, 8, 13, 14]
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