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THE PLANT CELL, Vol 3, Issue 6 619-628, Copyright © 1991 by American Society of Plant Biologists
Pathogen-Induced Proteins with Inhibitory Activity toward Phytophthora infestans
C. P. Woloshuk, J. S. Meulenhoff, M. Sela-Buurlage, PJM. van den Elzen and BJC. Cornelissen
MOGEN International NV, Einsteinweg 97, 2333 CB Leiden, The Netherlands
A bioassay using Phytophthora infestans was developed to determine whether
inhibitory proteins are induced in pathogen-inoculated plants. Using this
bioassay, AP24, a 24-kilodalton protein causing lysis of sporangia and
growth inhibition of P. infestans, was purified from tobacco plants
inoculated with tobacco mosaic virus. Analysis of the N-terminal amino acid
sequence identified AP24 as the thaumatin-like protein osmotin II. The
sequence was also similar to NP24, the salt-induced protein from tomato.
Subsequently, we purified a protein from tomato plants inoculated with P.
infestans that had inhibitory activities identical to those of the tobacco
AP24. The N-terminal amino acid sequence of this protein was also similar
to those of osmotin and NP24. In general, both the tobacco and tomato AP24
caused lysis of sporangia at concentrations greater than 40 nanomolar and
severely inhibited hyphal growth at concentrations greater than 400
nanomolar. Because both proteins were induced by pathogen inoculation, we
discussed the possible involvement of these proteins as a plant defense
mechanism.
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