Localization of heat shock protein 70 genes inside the rat major histocompatibility complex close to class III genes

1989 ◽  
Vol 30 (1) ◽  
pp. 46-49 ◽  
Author(s):  
Wolfgang Wurst ◽  
Christoph Benesch ◽  
Birgit Drabent ◽  
Ellen Rothermel ◽  
Bernd-Joachim Benecke ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Major Histocompatibility ◽  
Class Iii ◽  
Histocompatibility Complex ◽  
Class Iii Genes

scholarly journals Conservation of Babesia bovis Small Heat Shock Protein (Hsp20) among Strains and Definition of T Helper Cell Epitopes Recognized by Cattle with Diverse Major Histocompatibility Complex Class II Haplotypes

2004 ◽  
Vol 72 (2) ◽  
pp. 1096-1106 ◽  
Author(s):  
Junzo Norimine ◽  
Juan Mosqueda ◽  
Guy H. Palmer ◽  
Harris A. Lewin ◽  
Wendy C. Brown
Keyword(s):  
Major Histocompatibility Complex ◽  
T Cell ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Babesia Bovis ◽  
T Helper Cell ◽  
Complex Class ◽  
T Helper ◽  
Histocompatibility Complex

ABSTRACT Babesia bovis small heat shock protein (Hsp20) is recognized by CD4+ T lymphocytes from cattle that have recovered from infection and are immune to challenge. This candidate vaccine antigen is related to a protective antigen of Toxoplasma gondii, Hsp30/bag1, and both are members of the α-crystallin family of proteins that can serve as molecular chaperones. In the present study, immunofluorescence microscopy determined that Hsp20 is expressed intracellularly in all merozoites. Importantly, Hsp20 is also expressed by tick larval stages, including sporozoites, so that natural tick-transmitted infection could boost a vaccine-induced response. The predicted amino acid sequence of Hsp20 from merozoites is completely conserved among different B. bovis strains. To define the location of CD4+ T-cell epitopes for inclusion in a multiepitope peptide or minigene vaccine construct, truncated recombinant Hsp20 proteins and overlapping peptides were tested for their ability to stimulate T cells from immune cattle. Both amino-terminal (amino acids [aa] 1 to 105) and carboxy-terminal (aa 48 to 177) regions were immunogenic for the majority of cattle in the study, stimulating strong proliferation and IFN-γ production. T-cell lines from all individuals with distinct DRB3 haplotypes responded to aa 11 to 62 of Hsp20, which contained one or more immunodominant epitopes for each animal. One epitope, DEQTGLPIKS (aa 17 to 26), was identified by T-cell clones. The presence of strain-conserved T helper cell epitopes in aa 11 to 62 of the ubiquitously expressed Hsp20 that are presented by major histocompatibility complex class II molecules represented broadly in the Holstein breed supports the inclusion of this region in vaccine constructs to be tested in cattle.

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