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Hsp70: a carrier molecule with built-in adjuvanticity
1World Health Organisation-Immunology Research and Training Centre, Department of Pathology, University of Geneva, Switzerland.
Experientia
|November 30, 1994
Summary
Mycobacterial heat shock proteins (HSPs) like hsp70 can enhance subunit vaccines without adjuvants. Microbial hsp70 shows promise for designing effective conjugated vaccine constructs for human use.
Area of Science:
- Vaccinology
- Immunology
- Protein Chemistry
Background:
- Subunit vaccines often have limited immunogenicity due to structural issues or the need for adjuvants.
- Carrier proteins are typically used to conjugate target epitopes, providing T-cell epitopes for enhanced immune response.
Purpose of the Study:
- To investigate the potential of mycobacterial heat shock proteins (HSPs) as carrier proteins in conjugated vaccines.
- To evaluate the adjuvant-free helper effect of mycobacterial hsp65 and hsp70 when conjugated with target epitopes.
Main Methods:
- Conjugation of synthetic peptides or oligosaccharides with mycobacterial hsp65 and hsp70.
- In vivo immunogenicity testing in mice and monkeys, with and without prior priming.
- Comparison with HSP molecules from Escherichia coli.
Main Results:
- Mycobacterial hsp65 and hsp70 demonstrated a strong in vivo helper effect when conjugated to epitopes, eliminating the need for adjuvants.
- Hsp65 required prior priming (BCG or hsp65), while hsp70 did not require priming.
- Similar adjuvant-free helper effects were observed with HSPs from Escherichia coli.
Conclusions:
- Microbial HSPs, particularly hsp70, can act as effective carriers in conjugated vaccines, enhancing immunogenicity without adjuvants.
- The adjuvant-free helper effect of HSPs extends beyond mycobacteria to other prokaryotes.
- Microbial hsp70 is a promising candidate for the development of novel conjugated vaccine constructs for human application.