A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm

Adrian Davies, Suzanne Kalb, Bitao Liang, Carla Aldrich, François A. Lemonnier, Hong Jiang, Robert Cotter, Mark J. Soloski

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

The MHC class Ib molecule Qa-1 binds specifically and predominantly to a single 9-aa peptide (AMAPRTLLL) derived from the leader sequence of many MHC class Ia proteins. This peptide is referred to as Qdm. In this study, we report the isolation and sequencing of a heat shock protein 60-derived peptide (GMKFDRGYI) from Qa-1. This peptide is the dominant peptide bound to Qa-1 in the absence of Qdm. A Qa-1-restricted CTL clone recognizes this heat shock protein 60 peptide, further verifying that it binds to Qa-1 and a peptide from the homologous Salmonella typhimurium protein GroEL (GMQFDRGYL). These observations have implications for how Qa-1 can influence NK cell and T cell effector function via the TCR and CD94/NKG2 family members, and how this effect can change under conditions that cause the peptides bound to Qa-1 to change.

Original languageEnglish
Pages (from-to)5027-5033
Number of pages7
JournalJournal of Immunology
Volume170
Issue number10
StatePublished - May 15 2003

Fingerprint

Chaperonin 60
Protein Sorting Signals
Peptides
Salmonella typhimurium
Natural Killer Cells
Clone Cells
T-Lymphocytes

ASJC Scopus subject areas

  • Immunology

Cite this

A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm. / Davies, Adrian; Kalb, Suzanne; Liang, Bitao; Aldrich, Carla; Lemonnier, François A.; Jiang, Hong; Cotter, Robert; Soloski, Mark J.

In: Journal of Immunology, Vol. 170, No. 10, 15.05.2003, p. 5027-5033.

Research output: Contribution to journalArticle

Davies, A, Kalb, S, Liang, B, Aldrich, C, Lemonnier, FA, Jiang, H, Cotter, R & Soloski, MJ 2003, 'A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm', Journal of Immunology, vol. 170, no. 10, pp. 5027-5033.
Davies, Adrian ; Kalb, Suzanne ; Liang, Bitao ; Aldrich, Carla ; Lemonnier, François A. ; Jiang, Hong ; Cotter, Robert ; Soloski, Mark J. / A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm. In: Journal of Immunology. 2003 ; Vol. 170, No. 10. pp. 5027-5033.
@article{8ee9cf3c4ae34336a51f9b1546fb19d9,
title = "A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm",
abstract = "The MHC class Ib molecule Qa-1 binds specifically and predominantly to a single 9-aa peptide (AMAPRTLLL) derived from the leader sequence of many MHC class Ia proteins. This peptide is referred to as Qdm. In this study, we report the isolation and sequencing of a heat shock protein 60-derived peptide (GMKFDRGYI) from Qa-1. This peptide is the dominant peptide bound to Qa-1 in the absence of Qdm. A Qa-1-restricted CTL clone recognizes this heat shock protein 60 peptide, further verifying that it binds to Qa-1 and a peptide from the homologous Salmonella typhimurium protein GroEL (GMQFDRGYL). These observations have implications for how Qa-1 can influence NK cell and T cell effector function via the TCR and CD94/NKG2 family members, and how this effect can change under conditions that cause the peptides bound to Qa-1 to change.",
author = "Adrian Davies and Suzanne Kalb and Bitao Liang and Carla Aldrich and Lemonnier, {Fran{\cc}ois A.} and Hong Jiang and Robert Cotter and Soloski, {Mark J.}",
year = "2003",
month = "5",
day = "15",
language = "English",
volume = "170",
pages = "5027--5033",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "10",

}

TY - JOUR

T1 - A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm

AU - Davies, Adrian

AU - Kalb, Suzanne

AU - Liang, Bitao

AU - Aldrich, Carla

AU - Lemonnier, François A.

AU - Jiang, Hong

AU - Cotter, Robert

AU - Soloski, Mark J.

PY - 2003/5/15

Y1 - 2003/5/15

N2 - The MHC class Ib molecule Qa-1 binds specifically and predominantly to a single 9-aa peptide (AMAPRTLLL) derived from the leader sequence of many MHC class Ia proteins. This peptide is referred to as Qdm. In this study, we report the isolation and sequencing of a heat shock protein 60-derived peptide (GMKFDRGYI) from Qa-1. This peptide is the dominant peptide bound to Qa-1 in the absence of Qdm. A Qa-1-restricted CTL clone recognizes this heat shock protein 60 peptide, further verifying that it binds to Qa-1 and a peptide from the homologous Salmonella typhimurium protein GroEL (GMQFDRGYL). These observations have implications for how Qa-1 can influence NK cell and T cell effector function via the TCR and CD94/NKG2 family members, and how this effect can change under conditions that cause the peptides bound to Qa-1 to change.

AB - The MHC class Ib molecule Qa-1 binds specifically and predominantly to a single 9-aa peptide (AMAPRTLLL) derived from the leader sequence of many MHC class Ia proteins. This peptide is referred to as Qdm. In this study, we report the isolation and sequencing of a heat shock protein 60-derived peptide (GMKFDRGYI) from Qa-1. This peptide is the dominant peptide bound to Qa-1 in the absence of Qdm. A Qa-1-restricted CTL clone recognizes this heat shock protein 60 peptide, further verifying that it binds to Qa-1 and a peptide from the homologous Salmonella typhimurium protein GroEL (GMQFDRGYL). These observations have implications for how Qa-1 can influence NK cell and T cell effector function via the TCR and CD94/NKG2 family members, and how this effect can change under conditions that cause the peptides bound to Qa-1 to change.

UR - http://www.scopus.com/inward/record.url?scp=0037988743&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037988743&partnerID=8YFLogxK

M3 - Article

C2 - 12734347

AN - SCOPUS:0037988743

VL - 170

SP - 5027

EP - 5033

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 10

ER -