Peptide Sequence Requirements for the Recognition of HLA-B*2705 by Specific Natural Killer Cells

Marta Peruzzi, Kenneth C. Parker, Eric O. Long, Mauro S. Malnati

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)3350-3356
Number of pages7
JournalJournal of Immunology
Volume157
Issue number8
Publication statusPublished - Oct 15 1996

Fingerprint

Natural Killer Cells
Peptides
Clone Cells
HLA-C Antigens
HLA-B Antigens
Amino Acid Substitution
HLA-B*27:05 antigen
Ligands

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 journalArticle

Peruzzi, Marta ; Parker, Kenneth C. ; Long, Eric O. ; Malnati, Mauro S. / Peptide Sequence Requirements for the Recognition of HLA-B*2705 by Specific Natural Killer Cells. In: Journal of Immunology. 1996 ; Vol. 157, No. 8. pp. 3350-3356.
@article{b1cdd2227f6c4bf2beffb81d53e56f03,
title = "Peptide Sequence Requirements for the Recognition of HLA-B*2705 by Specific Natural Killer Cells",
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.",
author = "Marta Peruzzi and Parker, {Kenneth C.} and Long, {Eric O.} and Malnati, {Mauro S.}",
year = "1996",
month = "10",
day = "15",
language = "English",
volume = "157",
pages = "3350--3356",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "8",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0030587862&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030587862&partnerID=8YFLogxK

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 -