Heat-shock protein 70 from plant biofactories of recombinant antigens activate multiepitope-targeted immune responses.
Although a physiological role of heat-shock proteins (HSP) in antigen presentation and immune response activation has not been directly demonstrated, their use as vaccine components is under clinical trial. We have previously demonstrated that the structure of plant-derived HSP70 (pHSP70) can be superimposed to the mammalian homologue and similarly to the mammalian counterpart, pHSP70-polypeptide complexes can activate the immune system. It is here shown that pHSP70 purified from plant tissues transiently expressing the influenza virus nucleoprotein are able to induce both the activation of major histocompatibility complex class I-restricted polyclonal T-cell responses and antibody production in mice of different haplotypes without the need of adjuvant co-delivery. These results indicate that pHSP70 derived from plants producing recombinant antigens may be used to formulate multiepitope vaccines.
Laboratorio Biotecnologie Unità Tecnica BIORAD, ENEA C.R. Casaccia, Roma, Italy.
SourcePlant biotechnology journal 10:3 2012 Apr pg 363-71
Enzyme-Linked Immunospot Assay
HSP70 Heat-Shock Proteins
Histocompatibility Antigens Class I
Influenza A Virus, H1N1 Subtype
Mice, Inbred BALB C
Mice, Inbred C57BL
Viral Core Proteins
Pub Type(s)Journal Article
Research Support, Non-U.S. Gov't