Linked Life Data

15944288

Source:http://linkedlifedata.com/resource/pubmed/id/15944288

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2005-6-9
pubmed:abstractText
Tapasin (Tpn) is a chaperone of the endoplasmic reticulum involved in peptide loading to MHC class I proteins. The influence of mouse Tpn (mTpn) on the HLA-B*2705-bound peptide repertoire was analyzed to characterize the species specificity of this chaperone. B*2705 was expressed on Tpn-deficient human 721.220 cells cotransfected with human (hTpn) or mTpn. The heterodimer to beta(2)-microglobulin-free H chain ratio on the cell surface was reduced with mTpn, suggesting lower B*2705 stability. The B*2705-bound peptide repertoires loaded with hTpn or mTpn shared 94-97% identity, although significant differences in peptide amount were observed in 16-17% of the shared ligands. About 3-6% of peptides were bound only with either hTpn or mTpn. Nonamers differentially bound with mTpn had less suitable anchor residues and bound B*2705 less efficiently in vitro than those loaded only with hTpn or shared nonamers. Decamers showed a different pattern: those found only with mTpn had similarly suitable residues as shared decamers and bound B*2705 with high efficiency. Peptides differentially presented by B*2705 on human or mouse cells showed an analogous pattern of residue suitability, suggesting that the effect of mTpn on B*2705 loading is comparable in both cell types. Thus, mTpn has quantitative and qualitative effects on the B*2705-bound peptide repertoire, impairing presentation of some suitable ligands and allowing others with suboptimal anchor residues and lower affinity to be presented. Our results favor a size-dependent peptide editing role of Tpn for HLA-B*2705 that is species-dependent and suboptimally performed, at least for nonamers, by mTpn.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
174
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7833-44
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:15944288-Animals, pubmed-meshheading:15944288-Antigen Presentation, pubmed-meshheading:15944288-Antiporters, pubmed-meshheading:15944288-Cell Line, Transformed, pubmed-meshheading:15944288-Cell Line, Tumor, pubmed-meshheading:15944288-Cell Membrane, pubmed-meshheading:15944288-HLA-B Antigens, pubmed-meshheading:15944288-HLA-B27 Antigen, pubmed-meshheading:15944288-Humans, pubmed-meshheading:15944288-Immunoglobulins, pubmed-meshheading:15944288-Ligands, pubmed-meshheading:15944288-Membrane Transport Proteins, pubmed-meshheading:15944288-Mice, pubmed-meshheading:15944288-Molecular Chaperones, pubmed-meshheading:15944288-Oligopeptides, pubmed-meshheading:15944288-Protein Binding, pubmed-meshheading:15944288-RNA Editing, pubmed-meshheading:15944288-Species Specificity, pubmed-meshheading:15944288-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:15944288-Transfection
pubmed:year
2005
pubmed:articleTitle
Qualitative and quantitative differences in peptides bound to HLA-B27 in the presence of mouse versus human tapasin define a role for tapasin as a size-dependent peptide editor.
pubmed:affiliation
Centro de Biología Molecular Severo Ochoa (Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid), Facultad de Ciencias, Universidad Autónoma, Madrid, Spain.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't