Abstract

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.

Links

Publisher Full Text

Authors

Buriani G, Mancini C, Benvenuto E, Baschieri S

Institution

Laboratorio Biotecnologie Unità Tecnica BIORAD, ENEA C.R. Casaccia, Roma, Italy.

Source

Plant biotechnology journal 10:3 2012 Apr pg 363-71

MeSH

Agrobacterium tumefaciens
Animals
Antibody Formation
Enzyme-Linked Immunospot Assay
Escherichia coli
Female
Genetic Vectors
HSP70 Heat-Shock Proteins
Histocompatibility Antigens Class I
Immunodominant Epitopes
Influenza A Virus, H1N1 Subtype
Lymphocyte Activation
Mice
Mice, Inbred BALB C
Mice, Inbred C57BL
Plant Leaves
RNA-Binding Proteins
Recombinant Proteins
Tobacco
Viral Core Proteins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22221920