The 24-kDa protein from Fusarium oxysporum f.sp. erythroxyli: occurrence in related fungi and the effect of growth medium on its production.

Abstract

A 24-kDa protein that elicits ethylene production and necrosis in leaves of dicotyledonous plants was previously purified from culture filtrates of Fusarium oxysporum Schlechtend:Fr. f.sp. erythroxyli. Antisera to the denatured 24-kDa protein detected 2.5 ng of the 24-kDa protein on Western blots at 100000-fold dilutions. The antisera cross-reacted with a 24-kDa protein on Western blots of culture filtrates from three other F. oxysporum formae speciales. Of seven Fusarium species, only F. oxysporum, F. acuminatum Ellis and Kellerm., and F. avenaceum (Fr.:Fr.) Sacc. isolates produced an antigenically related 24-kDa protein. Although there were differences in the profiles of proteins extracted from stems of coca (Erythroxylum coca var. coca L. Lam.) infected with F. oxysporum f.sp. erythroxyli compared with uninfected stems, antisera to the 24-kDa protein did not cross-react with any proteins from the infected coca stems. For the fungal isolates studied, the best medium tested for production of the 24-kDa protein contained 1% sucrose and 1% asparagine. Biological activity of the F. oxysporum culture filtrates on sweet basil leaves was consistently correlated with the presence of the 24-kDa protein. Production of the 24-kDa protein was limited in cultures containing pectin or cellulose as the primary carbon source, or in cultures lacking sucrose or casamino acids. Water-soluble extracts from coca stems inhibited production of the 24-kDa protein, whereas cellulose and pectin did not. Components produced by the plant may limit production of the 24-kDa protein in infected plant tissue and thereby limit the response of the plant to the fungus. These results suggest the 24-kDa protein does not function in the symptomatic phase of the F. oxysporum f.sp. erythroxylicoca disease interaction.