Linked Life Data

8671682

Source:http://linkedlifedata.com/resource/pubmed/id/8671682

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-1-21
pubmed:abstractText
Peptides can affect the recognition of MHC class I molecules by allospecific antibodies. Two explanations have been proposed for this phenomenon. The 'conformational change' hypothesis suggests that peptide binding affects the availability of serologic determinants in the class I alpha1 and alpha2 domains while the 'peptide-side-chain effect' predicts that solvent exposed residues in the peptide are part of the serologic epitope. We have tested these possibilities by examining the recognition of peptide loaded HLA A*1101 molecules expressed in transporters associated with antigen processing (TAP)-deficient cell lines by three A11-specific mAb, and by comparing the effect of peptide analogues on the recognition of A11 complexes containing peptide epitopes from the Epstein-Barr virus nuclear antigen EBNA4 by antibodies and cytotoxic T lymphocytes (CT). The AUF5.13 and HB164 antibodies showed selective recognition of A11 molecules bound to partially overlapping sets of peptides from viral or cellular origin. The peptide dependence of AUF5.13 was confirmed in reconstitution experiments where A11 molecules were refolded at the surface of TAP-deficient T2/A11 cells that had been cultured at 26 degrees C and treated at pH3. Molecular modelling and Ala scanning mutagenesis of the IVTDFSVIK (IVT) and AVFDRKSDAK (AVF) peptides demonstrated that solvent-exposed peptide side chains affect CTL recognition as well as antibody binding. Substitution of Phe-P5 or Ser-P6 of the IVT peptide with Arg or Lys inhibited AUF5.13 recognition while binding was induced by substitution of the Arg-P5 and Lys-P6 of the AVF peptide with Ala. The results suggest that some allospecific antibodies recognized the surface of MHC class I-peptide complexes in a fashion similar to the TCR. This may involve direct interaction with the peptide side chains as well as recognition of peptide-induced perturbations in the class I complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0953-8178
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
927-38
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Solvent exposed side chains of peptides bound to HLA A*1101 have similar effects on the reactivity of alloantibodies and specific TCR.
pubmed:affiliation
Microbiology and Tumor Biology Center, Karolinska Institute, A-171 77 Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't