A 90 kDa protein elicitor, PB90, was purified from the culture filtrate of Phytophthora boehmeriae. Procedures including hydrophobic interaction and ion-exchange chromatography were used to purify the protein. PB90 induced hypersensitive reaction in tobacco leaves at a concentration as low as 200 pM and induced systemic acquired resistance (SAR) to TMV, Alternaria alternata, P. parasitica and Ralstonia solanacearum. In addition, it also caused hypersensitive necrosis in leaves of Chinese cabbage and induced SAR to Collectorium higginsianum in the plant. Tobacco leaves infiltrated with 200 pM of the elicitor exhibited an enhanced phenylalanine ammonia lyase activity and peroxidase activity. The behavior on ion-exchange columns indicated that PB90 is an acidic protein. It is stable to heat, acidic and alkaline conditions, but sensitive to ProteaseK. An antiserum raised against the pure protein allowed localization of PB90 by immunogold labeling on the cell wall of the mycelia and encysting zoospores when the fungus is grown in vitro. It was implied that there is a novel protein elicitor secreted by P. boehmeriae, which has a broad activity spectrum. The characters of PB90 distinguished it clearly from the other elicitors previously identified from Phytophthora spp. The possible implications of such a novel elicitor in plant–microbe interactions are discussed.