S. Bourque et al., Comparison of binding properties and early biological effects of elicitinsin tobacco cells, PLANT PHYSL, 118(4), 1998, pp. 1317-1326
Elicitins are a family of small proteins secreted by Phytophthora species t
hat have a high degree of homology and elicit defense reactions in tobacco
(Nicotiana tabacum). They display acidic or basic characteristics, the acid
ic elicitins being less efficient in inducing plant necrosis. In this study
we compared the binding properties of four elicitins (two basic and two ac
idic) and early-induced signal transduction events (Ca2+ influx, extracellu
lar medium alkalinization, and active oxygen species production). The affin
ity for tobacco plasma membrane-binding sites and the number of binding sit
es were similar for all four elicitins. Furthermore, elicitins compete with
one another for binding sites, suggesting that they interact with the same
receptor. The four elicitins induced Ca2+ influx, extracellular medium alk
alinization, and the production of active oxygen species in tobacco cell su
spensions, but the intensity and kinetics of these effects were different f
rom one elicitin to another. As a general observation the concentrations th
at induce similar levels of biological activities were lower for basic elic
itins (with the exception of cinnamomin-induced Ca2+ uptake). The qualitati
ve similarity of early events induced by elicitins indicates a common trans
duction scheme, whereas fine signal transduction tuning is different in eac
h elicitin.