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Molecular basis of HLA-C recognition by p58 natural killer cell inhibitory receptors

Authors
 Jongsun Kim  ;  Yong Joon Chwae  ;  Mi Yeon Kim  ;  In Hong Choi  ;  Jeon Han Park  ;  Se Jong Kim 
Citation
 JOURNAL OF IMMUNOLOGY, Vol.159(8) : 3857-3882, 1997 
Journal Title
 JOURNAL OF IMMUNOLOGY 
ISSN
 0022-1767 
Issue Date
1997
MeSH
Amino Acid Sequence ; Antigens/physiology ; Blood Donors ; Cloning, Molecular ; DNA, Complementary/isolation & purification ; HLA-C Antigens/chemistry ; HLA-C Antigens/genetics ; HLA-C Antigens/metabolism* ; Humans ; Immunoglobulins/physiology ; Killer Cells, Natural/metabolism* ; Molecular Sequence Data ; Peptides/immunology ; Peptides/physiology ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Receptors, Immunologic/biosynthesis ; Receptors, Immunologic/chemistry* ; Receptors, Immunologic/genetics ; Receptors, KIR ; Receptors, KIR2DL3 ; Receptors, Natural Killer Cell ; Solubility
Abstract
NK cells express several inhibitory receptors that recognize class I MHC molecules expressed on target cells. The NK cell inhibitory receptors (KIRs) provide a key regulatory function for NK cells via specific interaction with MHC/peptide complexes, but the molecular details for recognition of class I MHC molecules by KIRs still remain unclear. Here we report cDNA cloning and expression of p58 KIRs and a p50 killer cell activatory receptor (KAR) from a Korean blood donor and demonstrate direct binding between recombinant soluble p58 KIRs and recombinant soluble HLA-C molecules. We identified three p58/p50 killer cell receptors (KAR-K1, KIR-K6, and KIR-K7), which are homologous to p50 cl-39, p58 47.11, and p58 cl-6, respectively. Native gel shift assay revealed that p58 KIR-K6 and KIR-K7 bind both HLA-Cw3 and HLA-Cw6 molecules, but p50 KAR-K1 binds neither of the HLA-C molecules. However, binding of HLA-C molecule by p58 KIR is affected by the antigenic peptide bound on the MHC molecule, suggesting that the p58 KIR binding to the HLA-C molecule may be dependent on the peptide. In addition, the binding interaction requires the presence of both p58 Ig domains, suggesting that the binding mode of HLA-C and p58 KIR may have some similarity to that of the neonatal Fc receptor and the Fc fragment of Ab and may be distinct from that of TCR and MHC.
Full Text
https://www.jimmunol.org/content/159/8/3875.long
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Se Jong(김세종)
Kim, Jong Sun(김종선) ORCID logo https://orcid.org/0000-0002-3149-669X
Park, Jeon Han(박전한) ORCID logo https://orcid.org/0000-0001-9604-3205
Choi, In Hong(최인홍) ORCID logo https://orcid.org/0000-0001-9851-0137
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/177325
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