Abstract
KIR3DL1 and LILRB1 interact with HLA class I. Using KIR3DL1/HLA-B interaction to set up the procedure, structural immune-informatics approaches have been performed in LILRB1/HLA-B alleles’ combination also considering the contribution of the HLA bound peptide. All KIR3DL1 alleles interact strongly with HLA-B alleles carrying Bw4 epitope and negative charged amino acid residues in peptide position P8 disrupt KIR3DL1 binding. HLA-B alleles carrying Ile 194 show a higher strength of interaction with LILRB1 in all the analyzed haplotypes. Finally, we hypothesize a contribution of the amino acid at position 1 of the HLA bound peptide in the modulation of HLA-B/LILRB1 interaction.
Highlights
The modulation of NK cells’ immune response is mediated by inhibitory and activating receptors expressed on their surface [1,2,3,4]
In order to compare different HLA-B alleles interacting with different LILRB1 receptor alleles, we focused our study on the three known haplotypes (LILRB1.01, LILRB1.02, and LILRB1.03) carrying amino acid variants located in amino acid positions 45, 70, 119, and 132 of the mature protein sequence within known LILRB1 alleles and located on the HLA-LILRB1 interaction binding site [33, 34] (Table 2)
The presence of HLA-B Bw4/Bw6 epitope (Bw4) epitope leads to a stronger interaction with all the KIR3DL1 alleles with respect to HLA-B Bw6 epitope
Summary
The modulation of NK cells’ immune response is mediated by inhibitory and activating receptors expressed on their surface [1,2,3,4]. KIR3DL1 is able to interact with HLA class I molecules carrying Bw4 epitope, while no interaction has been observed in the presence of Bw6 epitope. Association studies between KIR3DL1 alleles and infectious diseases have been extensively reported in the past years. In this context, high expressive and nonexpressive alleles lead to a delayed HIV infection progression in the presence of HLA-B carrying Bw4 epitope [7]. High expressive and nonexpressive alleles lead to a delayed HIV infection progression in the presence of HLA-B carrying Bw4 epitope [7] These results encouraged the evaluation of HLA/KIR3DL1 pattern of interaction [8,9,10,11]. Beside the strong interaction with HLA Bw4 epitope, structural evidences have shown a role for the HLA bound peptide in the recognition by KIR3DL1 [12,13,14,15,16,17]
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