Source:http://linkedlifedata.com/resource/pubmed/id/20802150
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
|
pubmed:dateCreated |
2010-9-22
|
pubmed:abstractText |
Modulation of human NK cell function by killer cell Ig-like receptors (KIR) and MHC class I is dominated by the bipartite interactions of inhibitory lineage III KIR with the C1 and C2 epitopes of HLA-C. In comparison, the ligand specificities and functional contributions of the activating lineage III KIR remain poorly understood. Using a robust, sensitive assay of KIR binding and a representative panel of 95 HLA class I targets, we show that KIR2DS1 binds C2 with ~50% the avidity of KIR2DL1, whereas KIR2DS2, KIR2DS3, and KIR2DS5 have no detectable avidity for C1, C2, or any other HLA class I epitope. In contrast, the chimpanzee has activating C1- and C2-specific lineage III KIR with strong avidity, comparable to those of their paired inhibitory receptors. One variant of chimpanzee Pt-KIR3DS2, the activating C2-specific receptor, has the same avidity for C2 as does inhibitory Pt-KIR3DL4, and a second variant has ~73% the avidity. Chimpanzee Pt-KIR3DS6, the activating C1-specific receptor, has avidity for C1 that is ~70% that of inhibitory Pt-KIR2DL6. In both humans and chimpanzees we observe an evolutionary trend toward reducing the avidity of the activating C1- and C2-specific receptors through selective acquisition of attenuating substitutions. However, the extent of attenuation has been extreme in humans, as exemplified by KIR2DS2, an activating C1-specific receptor that has lost all detectable avidity for HLA class I. Supporting such elimination of activating C1-specific receptors as a uniquely human phenomenon is the presence of a high-avidity activating C1-specific receptor (Gg-KIR2DSa) in gorilla.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
AIM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-C Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/KIR2DS2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/NK Cell Lectin-Like Receptor...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, KIR
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
1550-6606
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:day |
1
|
pubmed:volume |
185
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4233-7
|
pubmed:dateRevised |
2011-10-3
|
pubmed:meshHeading |
pubmed-meshheading:20802150-Animals,
pubmed-meshheading:20802150-Biological Evolution,
pubmed-meshheading:20802150-Epitopes,
pubmed-meshheading:20802150-Gorilla gorilla,
pubmed-meshheading:20802150-HLA-C Antigens,
pubmed-meshheading:20802150-Humans,
pubmed-meshheading:20802150-Lymphocyte Activation,
pubmed-meshheading:20802150-NK Cell Lectin-Like Receptor Subfamily C,
pubmed-meshheading:20802150-Pan troglodytes,
pubmed-meshheading:20802150-Receptors, KIR
|
pubmed:year |
2010
|
pubmed:articleTitle |
Humans differ from other hominids in lacking an activating NK cell receptor that recognizes the C1 epitope of MHC class I.
|
pubmed:affiliation |
Department of Structural Biology, School of Medicine, Stanford University, Stanford, CA 94305, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
|