Augmentation of DNA vaccine potency through secretory heat shock protein-mediated antigen targeting

被引:45
作者
Hauser, H
Chen, SY
机构
[1] Baylor Coll Med, Dept Mol & Human Genet, Ctr Cell & Gene Therapy, Houston, TX 77030 USA
[2] Univ Vienna, Inst Immunol, Vienna, Austria
[3] St Anna Childrens Hosp, Childrens Canc Res Inst, A-1090 Vienna, Austria
关键词
cytotoxic T-lymphocyte response; antigen; human papilloma virus; fusion molecule; dendritic cell;
D O I
10.1016/S1046-2023(03)00136-1
中图分类号
Q5 [生物化学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
In an effort to enhance the potency of DNA vaccines, we have developed a new strategy to increase antigen presentation by dendritic cells, one that results in markedly improved cytotoxic T-lymphocyte responses, antibody production, and antitumor effects in vivo. Here, we present the rationale and design of a vaccine encoding a secreted antigen-heat shock protein 70 fusion molecule, targeted to the MHC class 1 cross-presentation pathway of dendritic cells. Using the human papilloma virus 16 E7 protein as a model antigen, we illustrate the preparation of this vaccine and the main experimental procedures used to test such constructs. (C) 2003 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:225 / 231
页数:7
相关论文
共 51 条
[1]
IN-VIVO TRANSFER AND EXPRESSION OF A HUMAN EPIDERMAL GROWTH-FACTOR GENE ACCELERATES WOUND REPAIR [J].
ANDREE, C ;
SWAIN, WF ;
PAGE, CP ;
MACKLIN, MD ;
SLAMA, J ;
HATZIS, D ;
ERIKSSON, E .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (25) :12188-12192
[2]
Arnold-Schild D, 1999, J IMMUNOL, V162, P3757
[3]
Novel signal transduction pathway utilized by extracellular HSP70 -: Role of Toll-like receptor (TLR) 2 AND TLR4 [J].
Asea, A ;
Rehli, M ;
Kabingu, E ;
Boch, JA ;
Baré, O ;
Auron, PE ;
Stevenson, MA ;
Calderwood, SK .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (17) :15028-15034
[4]
HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine [J].
Asea, A ;
Kraeft, SK ;
Kurt-Jones, EA ;
Stevenson, MA ;
Chen, LB ;
Finberg, RW ;
Koo, GC ;
Calderwood, SK .
NATURE MEDICINE, 2000, 6 (04) :435-442
[5]
Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway [J].
Basu, S ;
Binder, RJ ;
Suto, R ;
Anderson, KM ;
Srivastava, PK .
INTERNATIONAL IMMUNOLOGY, 2000, 12 (11) :1539-1546
[6]
CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin [J].
Basu, S ;
Binder, RJ ;
Ramalingam, T ;
Srivastava, PK .
IMMUNITY, 2001, 14 (03) :303-313
[7]
CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes [J].
Becker, T ;
Hartl, FU ;
Wieland, F .
JOURNAL OF CELL BIOLOGY, 2002, 158 (07) :1277-1285
[8]
Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity [J].
Blachere, NE ;
Li, ZH ;
Chandawarkar, RY ;
Suto, R ;
Jaikaria, NS ;
Basu, S ;
Udono, H ;
Srivastava, PK .
JOURNAL OF EXPERIMENTAL MEDICINE, 1997, 186 (08) :1315-1322
[9]
Breloer M, 1999, J IMMUNOL, V162, P3141
[10]
Castelli C, 2001, CANCER RES, V61, P222