Abstract
NK clones that were inhibited by target cell expression of HLA-B*2705 displayed peptide-specific recognition of HLA-B*2705. To evaluate the specificity of this recognition, synthetic versions of 14 endogenous ligands of HLA-B*2705 were tested for their ability to provide protection from NK-mediated lysis by binding to surface HLA-B*2705 molecules on RMA-S cells deficient in the transporter for Ag presentation. Several unrelated peptides inhibited lysis by the same NK clones. Despite similar capacities to stabilize HLA-B*2705 molecules on RMA-S cells, the 14 peptides differed widely in their abilities to provide protection. Single amino acid substitutions in both a protective and a nonprotective peptide revealed the importance of residues 7 and 8 in the peptide for recognition by NK clones, thus localizing the peptide influence to a polymorphic region of the α-helix of HLA class I molecules known to control discrimination among allelic variants of HLA-B and HLA-C by NK cells.
| Original language | English |
|---|---|
| Pages (from-to) | 3350-3356 |
| Number of pages | 7 |
| Journal | Journal of Immunology |
| Volume | 157 |
| Issue number | 8 |
| Publication status | Published - Oct 15 1996 |
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ASJC Scopus subject areas
- Immunology
Cite this
Peptide Sequence Requirements for the Recognition of HLA-B*2705 by Specific Natural Killer Cells. / Peruzzi, Marta; Parker, Kenneth C.; Long, Eric O.; Malnati, Mauro S.
In: Journal of Immunology, Vol. 157, No. 8, 15.10.1996, p. 3350-3356.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Peptide Sequence Requirements for the Recognition of HLA-B*2705 by Specific Natural Killer Cells
AU - Peruzzi, Marta
AU - Parker, Kenneth C.
AU - Long, Eric O.
AU - Malnati, Mauro S.
PY - 1996/10/15
Y1 - 1996/10/15
N2 - NK clones that were inhibited by target cell expression of HLA-B*2705 displayed peptide-specific recognition of HLA-B*2705. To evaluate the specificity of this recognition, synthetic versions of 14 endogenous ligands of HLA-B*2705 were tested for their ability to provide protection from NK-mediated lysis by binding to surface HLA-B*2705 molecules on RMA-S cells deficient in the transporter for Ag presentation. Several unrelated peptides inhibited lysis by the same NK clones. Despite similar capacities to stabilize HLA-B*2705 molecules on RMA-S cells, the 14 peptides differed widely in their abilities to provide protection. Single amino acid substitutions in both a protective and a nonprotective peptide revealed the importance of residues 7 and 8 in the peptide for recognition by NK clones, thus localizing the peptide influence to a polymorphic region of the α-helix of HLA class I molecules known to control discrimination among allelic variants of HLA-B and HLA-C by NK cells.
AB - NK clones that were inhibited by target cell expression of HLA-B*2705 displayed peptide-specific recognition of HLA-B*2705. To evaluate the specificity of this recognition, synthetic versions of 14 endogenous ligands of HLA-B*2705 were tested for their ability to provide protection from NK-mediated lysis by binding to surface HLA-B*2705 molecules on RMA-S cells deficient in the transporter for Ag presentation. Several unrelated peptides inhibited lysis by the same NK clones. Despite similar capacities to stabilize HLA-B*2705 molecules on RMA-S cells, the 14 peptides differed widely in their abilities to provide protection. Single amino acid substitutions in both a protective and a nonprotective peptide revealed the importance of residues 7 and 8 in the peptide for recognition by NK clones, thus localizing the peptide influence to a polymorphic region of the α-helix of HLA class I molecules known to control discrimination among allelic variants of HLA-B and HLA-C by NK cells.
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M3 - Article
C2 - 8871631
AN - SCOPUS:0030587862
VL - 157
SP - 3350
EP - 3356
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 8
ER -