RRC ID 27181
Author Buriani G, Mancini C, Benvenuto E, Baschieri S.
Title Heat-shock protein 70 from plant biofactories of recombinant antigens activate multiepitope-targeted immune responses.
Journal Plant Biotechnol. J.
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.
Volume 10(3)
Pages 363-71
Published 2012-4
DOI 10.1111/j.1467-7652.2011.00673.x
PMID 22221920
MeSH Agrobacterium tumefaciens / genetics Agrobacterium tumefaciens / metabolism Animals Antibody Formation Enzyme-Linked Immunospot Assay Escherichia coli / genetics Escherichia coli / metabolism Female Genetic Vectors / genetics Genetic Vectors / metabolism HSP70 Heat-Shock Proteins / immunology* Histocompatibility Antigens Class I / immunology Immunodominant Epitopes / immunology* Influenza A Virus, H1N1 Subtype / immunology Lymphocyte Activation* Mice Mice, Inbred BALB C Mice, Inbred C57BL Plant Leaves / genetics Plant Leaves / metabolism RNA-Binding Proteins / immunology Recombinant Proteins / immunology Tobacco / genetics Tobacco / metabolism Viral Core Proteins / immunology
IF 6.84
Times Cited 5
DNA material pBMSA-NP (RDB01972)