Titolo | Heat-shock protein 70 from plant biofactories of recombinant antigens activate multiepitope-targeted immune responses |
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Tipo di pubblicazione | Articolo su Rivista peer-reviewed |
Anno di Pubblicazione | 2012 |
Autori | Buriani, G., Mancini C., Benvenuto Eugenio, and Baschieri Selene |
Rivista | Plant Biotechnology Journal |
Volume | 10 |
Paginazione | 363-371 |
ISSN | 14677644 |
Parole chiave | Agrobacterium tumefaciens, animal, Animals, Antibody Formation, antibody production, article, Bagg albino mouse, C57BL mouse, core protein, enzyme linked immunospot assay, Enzyme-Linked Immunospot Assay, epitope, Escherichia coli, Female, gene vector, Genetic Vectors, genetics, H1N1 Subtype, heat shock protein 70, Histocompatibility Antigens Class I, HLA antigen class 1, HSP70 Heat-Shock Proteins, Immunodominant Epitopes, immunology, Inbred BALB C, Inbred C57BL, Influenza A Virus, Influenza virus A H1N1, lymphocyte activation, Mammalia, metabolism, Mice, mouse, Mus, NP protein, Orthomyxoviridae, plant leaf, Plant leaves, recombinant protein, Recombinant Proteins, Rhizobium radiobacter, RNA binding protein, RNA-Binding Proteins, Tobacco, Viral Core Proteins |
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. © 2012 The Authors. Plant Biotechnology Journal © 2012 Society for Experimental Biology, Association of Applied Biologists and Blackwell Publishing Ltd. |
Note | cited By 7 |
URL | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84857919321&doi=10.1111%2fj.1467-7652.2011.00673.x&partnerID=40&md5=52a3801ca754c00c7b731df7a741b01e |
DOI | 10.1111/j.1467-7652.2011.00673.x |
Citation Key | Buriani2012363 |