Lipid transfer proteins (LTPs) and elicitins are both able to load and tran
sfer lipidic molecules and share some structural and functional properties.
While elicitins are known as elicitors of plant defence mechanisms, the bi
ological function of LTP is still an enigma. We show that a wheat LTP1 bind
s with high affinity sites. Binding and in vivo competition experiments poi
nt out that these binding sites are common to LTP1 and elicitins and confir
m that they are the biological receptors of elicitins. A mathematical analy
sis suggests that these receptors could be represented by an allosteric mod
el corresponding to an oligomeric structure with four identical subunits. (
C) 2001 Federation of European Biochemical Societies. Published by Elsevier
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