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A simple assay for detection of peptides promoting the assembly of HLA class I molecules
Author(s) -
Connan Francine,
Hlavac Frédéric,
Hoebeke Johan,
Guillet JeanGÉRard,
Choppin Jeannine
Publication year - 1994
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/eji.1830240344
Subject(s) - biology , human leukocyte antigen , simple (philosophy) , class (philosophy) , computational biology , microbiology and biotechnology , immunology , antigen , computer science , artificial intelligence , philosophy , epistemology
Abstract Synthetic peptides derived from influenza virus and human immunodeficiency virus were tested for their ability to promote the assembly of HLA‐A2 and HLA‐B51 molecules in T2 cell lysates. Specific assembly was detected by an enzyme‐linked immunosorbent assay. The most significant HLA‐A2 assembly was obtained in the presence of peptides known to be targets for HLA‐A2‐restricted cytotoxic T lymphocytes (influenza matrix M.58–66 and HIV Pol 476–484). Three of a batch of Nef peptides corresponding to epitopic regions for cytotoxic T lymphocytes, caused significant assembly of HLA‐A2 (Nef 83–91, 137–145 and 144–153), but only at high concentrations (100 μ M ). As these peptides bound relatively weakly, it is unlikely that they are good candidates for HLA‐A2‐restricted CTL epitopes. Peptides matrix M.60–68, Nef 186–194, and Plasmodium falciparum sh. 77–85 produced the most significant assembly of HLA‐B51. These peptides have a dominant hydrophobic anchor residue (V, L. I) at position 9 that could occupy pocket “F”. Our results also suggest that another hydrophobic residue (V, L) at position 3 or 4 may anchor to hydrophobic pocket “d” of HLA‐B51. Proline at position 2 greatly increases HLA‐B51 anchoring.