|
|
||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
,

*
Institute of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht, The Netherlands;
Department of Pediatrics, University of California at San Diego, La Jolla, CA 92093; and
Department of Pediatric Immunology, University Medical Center Utrecht, Wilhelmina Childrens Hospital, Utrecht, The Netherlands
Bacterial heat shock proteins (hsp) are evolutionary conserved
immunodominant proteins that manifest amino acid homologies with hsp
present in mammalian cells. Preimmunization with mycobacterial hsp65
has been found to protect against various forms of experimental
arthritis. As these protective effects have previously been attributed
to induction of self homologue cross-reactive T cell responses, the
question was raised as to whether this protective effect could be
extended to other highly conserved and immunodominant microbial Ags
with mammalian homologues. Therefore, we immunized Lewis rats with
conserved bacterial Ags (superoxide dismutase, aldolase, GAPDH, and
hsp70). Although all Ags appeared highly immunogenic, we only found a
protective effect in experimental arthritis after immunization with
bacterial hsp70. The protective effect of hsp70 was accompanied with a
switch in the subclasses of hsp70-specific Abs, suggesting the
induction of Th2-like response. The most striking difference between
immunization with hsp70 and all other immunodominant Ags was the
expression of IL-10 found after immunization with hsp70. Even more,
while immunization with hsp70 led to Ag-induced production of IL-10 and
IL-4, immunization with aldolase led to increased production of IFN-
and TNF-
. Thus, the protective effect of conserved immunodominant
proteins in experimental arthritis seems to be a specific feature of
hsp. Therefore, hsp may offer unique possibilities for immunological
intervention in inflammatory diseases.
This article has been cited by other articles:
![]() |
G. Galazka, M. Stasiolek, A. Walczak, A. Jurewicz, A. Zylicz, C. F. Brosnan, C. S. Raine, and K. W. Selmaj Brain-Derived Heat Shock Protein 70-Peptide Complexes Induce NK Cell-Dependent Tolerance to Experimental Autoimmune Encephalomyelitis J. Immunol., February 1, 2006; 176(3): 1588 - 1599. [Abstract] [Full Text] [PDF] |
||||
![]() |
J.-E. Park, J. Facciponte, X. Chen, I. MacDonald, E. A. Repasky, M. H. Manjili, X.-Y. Wang, and J. R. Subjeck Chaperoning Function of Stress Protein grp170, a Member of the hsp70 Superfamily, Is Responsible for its Immunoadjuvant Activity Cancer Res., January 15, 2006; 66(2): 1161 - 1168. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |