Cutting edge: Single-chain trimers of MHC class I molecules form stable structures that potently stimulate antigen-specific T cells and B cells

Yik Y L Yu, Nikolai Netuschil, Lonnie Lybarger, Janet M. Connolly, Ted H. Hansen

Research output: Contribution to journalArticle

78 Citations (Scopus)

Abstract

We report in this work the expression and characterization of class I molecules expressed as single-chain trimers consisting of an antigenic peptide-spacer-β2-microglobulin-spacer H chain. Our results indicate that these single-chain constructs assemble efficiently, maintain their covalent structure, and are unusually stable at the cell surface. Consequently, these constructs are at least 1000-fold less accessible to exogenous peptide than class I molecules loaded with endogenous peptides, and they are potent simulators of peptide-specific CTL and Abs. Our combined findings suggest that single-chain trimers may have applications as DNA vaccines against virus infection or tumors.

Original languageEnglish (US)
Pages (from-to)3145-3149
Number of pages5
JournalJournal of Immunology
Volume168
Issue number7
StatePublished - Apr 1 2002
Externally publishedYes

Fingerprint

B-Lymphocytes
T-Lymphocytes
Antigens
Peptides
Tumor Virus Infections
DNA Vaccines

ASJC Scopus subject areas

  • Immunology

Cite this

Cutting edge : Single-chain trimers of MHC class I molecules form stable structures that potently stimulate antigen-specific T cells and B cells. / Yu, Yik Y L; Netuschil, Nikolai; Lybarger, Lonnie; Connolly, Janet M.; Hansen, Ted H.

In: Journal of Immunology, Vol. 168, No. 7, 01.04.2002, p. 3145-3149.

Research output: Contribution to journalArticle

@article{54244f14097f4721abb8d7bdd0663302,
title = "Cutting edge: Single-chain trimers of MHC class I molecules form stable structures that potently stimulate antigen-specific T cells and B cells",
abstract = "We report in this work the expression and characterization of class I molecules expressed as single-chain trimers consisting of an antigenic peptide-spacer-β2-microglobulin-spacer H chain. Our results indicate that these single-chain constructs assemble efficiently, maintain their covalent structure, and are unusually stable at the cell surface. Consequently, these constructs are at least 1000-fold less accessible to exogenous peptide than class I molecules loaded with endogenous peptides, and they are potent simulators of peptide-specific CTL and Abs. Our combined findings suggest that single-chain trimers may have applications as DNA vaccines against virus infection or tumors.",
author = "Yu, {Yik Y L} and Nikolai Netuschil and Lonnie Lybarger and Connolly, {Janet M.} and Hansen, {Ted H.}",
year = "2002",
month = "4",
day = "1",
language = "English (US)",
volume = "168",
pages = "3145--3149",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "7",

}

TY - JOUR

T1 - Cutting edge

T2 - Single-chain trimers of MHC class I molecules form stable structures that potently stimulate antigen-specific T cells and B cells

AU - Yu, Yik Y L

AU - Netuschil, Nikolai

AU - Lybarger, Lonnie

AU - Connolly, Janet M.

AU - Hansen, Ted H.

PY - 2002/4/1

Y1 - 2002/4/1

N2 - We report in this work the expression and characterization of class I molecules expressed as single-chain trimers consisting of an antigenic peptide-spacer-β2-microglobulin-spacer H chain. Our results indicate that these single-chain constructs assemble efficiently, maintain their covalent structure, and are unusually stable at the cell surface. Consequently, these constructs are at least 1000-fold less accessible to exogenous peptide than class I molecules loaded with endogenous peptides, and they are potent simulators of peptide-specific CTL and Abs. Our combined findings suggest that single-chain trimers may have applications as DNA vaccines against virus infection or tumors.

AB - We report in this work the expression and characterization of class I molecules expressed as single-chain trimers consisting of an antigenic peptide-spacer-β2-microglobulin-spacer H chain. Our results indicate that these single-chain constructs assemble efficiently, maintain their covalent structure, and are unusually stable at the cell surface. Consequently, these constructs are at least 1000-fold less accessible to exogenous peptide than class I molecules loaded with endogenous peptides, and they are potent simulators of peptide-specific CTL and Abs. Our combined findings suggest that single-chain trimers may have applications as DNA vaccines against virus infection or tumors.

UR - http://www.scopus.com/inward/record.url?scp=0036533556&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036533556&partnerID=8YFLogxK

M3 - Article

C2 - 11907065

AN - SCOPUS:0036533556

VL - 168

SP - 3145

EP - 3149

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 7

ER -