PMID- 21614583
OWN - NLM
STAT- MEDLINE
DCOM- 20110930
LR  - 20211020
IS  - 1432-1211 (Electronic)
IS  - 0093-7711 (Print)
IS  - 0093-7711 (Linking)
VI  - 63
IP  - 9
DP  - 2011 Sep
TI  - Rhesus macaque KIR bind human MHC class I with broad specificity and recognize 
      HLA-C more effectively than HLA-A and HLA-B.
PG  - 577-85
LID - 10.1007/s00251-011-0535-7 [doi]
AB  - Human killer cell immunoglobulin-like receptors (KIR) recognize A3/11, Bw4, C1, 
      and C2 epitopes carried by mutually exclusive subsets of human leukocyte antigen 
      (HLA)-A, -B, and -C allotypes. Chimpanzee and orangutan have counterparts to 
      HLA-A, -B, and -C, and KIR that recognize the A3/11, Bw4, C1, and C2 epitopes, 
      either individually or in combination. Because rhesus macaque has counterparts of 
      HLA-A and -B, but not HLA-C, we expected that rhesus KIR would better recognize 
      HLA-A and -B, than HLA-C. Comparison of the interactions of nine rhesus KIR3D 
      with 95 HLA isoforms, showed the KIR have broad specificity for HLA-A, -B, and 
      -C, but vary in avidity. Considering both the strength and breadth of reaction, 
      HLA-C was the major target for rhesus KIR, followed by HLA-B, then HLA-A. Strong 
      reactions with HLA-A were restricted to the minority of allotypes carrying the 
      Bw4 epitope, whereas strong reactions with HLA-B partitioned between allotypes 
      having and lacking Bw4. Contrasting to HLA-A and -B, every HLA-C allotype bound 
      to the nine rhesus KIR. Sequence comparison of high- and low-binding HLA 
      allotypes revealed the importance of polymorphism in the helix of the alpha(1) domain 
      and the peptide-binding pockets. At peptide position 9, nonpolar residues favor 
      binding to rhesus KIR, whereas charged residues do not. Contrary to expectation, 
      rhesus KIR bind more effectively to HLA-C, than to HLA-A and -B. This property is 
      consistent with major histocompatibility complex (MHC)-C having evolved in 
      hominids to be a generally superior ligand for KIR than MHC-A and MHC-B.
FAU - Older Aguilar, Anastazia M
AU  - Older Aguilar AM
AD  - Department of Structural Biology, Stanford University, CA 94305, USA.
FAU - Guethlein, Lisbeth A
AU  - Guethlein LA
FAU - Hermes, Meike
AU  - Hermes M
FAU - Walter, Lutz
AU  - Walter L
FAU - Parham, Peter
AU  - Parham P
LA  - eng
GR  - R01 AI024258/AI/NIAID NIH HHS/United States
GR  - R01 AI031168/AI/NIAID NIH HHS/United States
GR  - AI31168/AI/NIAID NIH HHS/United States
GR  - AI24258/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20110526
PL  - United States
TA  - Immunogenetics
JT  - Immunogenetics
JID - 0420404
RN  - 0 (Epitopes)
RN  - 0 (HLA-A Antigens)
RN  - 0 (HLA-B Antigens)
RN  - 0 (HLA-Bw4 antigen)
RN  - 0 (HLA-C Antigens)
RN  - 0 (Protein Isoforms)
RN  - 0 (Receptors, KIR)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Epitopes/immunology
MH  - HLA-A Antigens/*immunology
MH  - HLA-B Antigens/*immunology
MH  - HLA-C Antigens/*immunology
MH  - Humans
MH  - Macaca mulatta/*immunology
MH  - Molecular Sequence Data
MH  - Protein Isoforms/immunology
MH  - Receptors, KIR/*immunology
PMC - PMC3718024
MID - NIHMS478619
EDAT- 2011/05/27 06:00
MHDA- 2011/10/01 06:00
PMCR- 2013/07/22
CRDT- 2011/05/27 06:00
PHST- 2011/03/15 00:00 [received]
PHST- 2011/05/09 00:00 [accepted]
PHST- 2011/05/27 06:00 [entrez]
PHST- 2011/05/27 06:00 [pubmed]
PHST- 2011/10/01 06:00 [medline]
PHST- 2013/07/22 00:00 [pmc-release]
AID - 10.1007/s00251-011-0535-7 [doi]
PST - ppublish
SO  - Immunogenetics. 2011 Sep;63(9):577-85. doi: 10.1007/s00251-011-0535-7. Epub 2011 
      May 26.