Modulations of elicitins activity by changes in proteins surface charge
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| Year of publication | 2013 |
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| Description | In plants, elicitins induce a hypersensitive response and non-specific systemic acquired resistance. They contain a hydrophobic cavity capable of binding sterols and fatty acids, and on the basis of their pI they are classified as either ??elicitins or more necrotizing ??elicitins. It has been assumed that conformational changes in the ?-loop evoke by sterol binding “activate” elicitins. However recent results suggest that the sterol-binding ability of elicitins associated with conformational changes in the ?-loop, might not be principal factors in elicitins biological activity and favour role of specific residues. The most probable candidates being lysine residues considering the previously observed correlation between necrotic index and pI together with a clear impact of the Lys13Val mutation in helix A on induction of a defence response in tobacco plants. In bioreactor a serious of cryptogein mutants with changed lysine residues was prepared. The significant impact of several mutations on cryptogein stability measured by differential scanning calorimetry was found. Moreover, some mutations alter the interaction of the protein with the binding site on the plasma membrane and the ability to induce a hypersensitive response and resistance. Determined results provide possibility to specifically modulate elicitins biological activity though the mutation of specific residues. |
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