Effect of the Heat Shock Protein 70 on the Adjuvanticity Induced by a Bacterial Flagellin of Vibrio ulnificus
Journal of Bacteriology and Virology
;
: 299-306, 2005.
Article
in Korean
| WPRIM
| ID: wpr-85878
ABSTRACT
Recently we have shown that a bacterial flagellin, Vibrio vulnifiucs FlaB (Vv-FlaB), has a strong adjuvant activity to induce protective immune response. In order to investigate the adjuvanticity of Vv-FlaB, we prepared highly purified recombinant protein by using an intein fusion protein purification system. However, in the process of the purification, we unexpectedly encountered a contamination with a 70 kDa protein. We proved the 70 kDa protein as the heat shock protein 70 (HSP70) by Western blotting. Unfortunately, it was reported that the HSP70 has a strong adjuvanticity. In this study we investigated the role of contaminating HSP70 on the Vv-FlaB-mediated adjuvanticity. We separated Vv-FlaB and HSP70 by using a high performance protein purification chromatography and compared adjuvant activities of Vv-FlaB, HSP70 and Vv-FlaB/HSP70 mixture. Using an intranasal immunization mouse model, we observed that co-administration of the flagellin with tetanus toxoid (TT) induced significantly enhanced TT-specific antibody (Ig) responses. However contaminating doses of HSP70 did not affect the adjuvanticity of Vv-FlaB and furthermore HSP70 alone did not enhance TT-specific Ig response and protective immunity against lethal challenge with tetanus toxin. These results show that the HSP70 contaminating Vv-FlaB preparations did not affect the adjuvanticity of Vv-FlaB.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Staphylococcal Protein A
/
Tetanus Toxin
/
Vibrio
/
Tetanus Toxoid
/
Blotting, Western
/
Chromatography
/
Immunization
/
HSP70 Heat-Shock Proteins
/
Vibrio vulnificus
/
Inteins
Limits:
Animals
Language:
Korean
Journal:
Journal of Bacteriology and Virology
Year:
2005
Type:
Article
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