Abstract
Heat shock proteins (HSPs) are molecular chaperones involved in many cellular functions. It has been shown that mammalian cytosolic HSP70 binds antigenic peptides mediating the activation of the immune system, and that it plays a determining role in tumour immunogenicity. This suggests that HSP70 may be used for the production of conjugated vaccines. Human and plant HSPs share high sequence similarity and some important biological functions in vitro. In addition, plant HSPs have no endotoxic side effects. Extraction of HSP70 from plants for use as vaccine adjuvant requires enhancing its concentration in plant tissues. In this work, we explored the possibility to produce HSP70 in both transgenic and non-transgenic plants, using alfalfa as a model species. First, a transcriptional analysis of a constitutive and an inducible HSP70 genes was conducted in Arabidopsis thaliana. Then the coding sequence of the inducible form was cloned and introduced into alfalfa by Agrobacterium-mediated transformation, and the accumulation of the protein in leaf tissue of transgenic plants was demonstrated. We also tested diverse alfalfa varieties for heat-inducible expression of endogenous HSP70, revealing variety-specific responses to heat shock.
Highlights
Heat shock proteins (HSPs) are a class of proteins conserved in all living organisms and involved in basic cellular functions such as homeostasis, folding of nascent proteins, refolding of denatured proteins, preventing protein aggregation and assisting protein transport across membranes [1]
Inducible HSPs are transiently activated after heat shock (HS) and their expression level remains high up to few hours after induction; this response is dependent on the genotype and the environmental conditions [2]
We explored the possibility to accumulate one of the inducible forms of HSP70, that was previously demonstrated to be upregulated upon stress in Arabidopsis [22], in both transgenic
Summary
Heat shock proteins (HSPs) are a class of proteins conserved in all living organisms and involved in basic cellular functions such as homeostasis, folding of nascent proteins, refolding of denatured proteins, preventing protein aggregation and assisting protein transport across membranes [1]. These functions earned them the name “molecular chaperones”. HSPs are classified into several families according their molecular size [3] They are located in all cellular and subcellular compartments (nucleus, membrane, cytosol, endoplasmic reticulum, mitochondria, lysosome)
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