Primary and secondary parasitoids (Hymenoptera) of aphids (Hemiptera: Aphididae) on blueberry and other Vaccinium in the Pacific Northwest.

Blueberry scorch virus, a commercially important Carlavirus in highbush blueberry, Vaccinium corymbosum L., is vectored by aphids (Hemiptera: Aphididae). We surveyed the aphids, primary parasitoids (Hymenoptera: Aphelinidae, Braconidae), and associated secondary parasitoids (Hymenoptera: Charipidae, Megaspilidae, Pteromalidae) on highbush blueberry and other Vaccinium in the Pacific Northwest from 1995 to 2006, with samples concentrated in 2005 and 2006, to lay the groundwork for augmentative biological control. Ericaphis fimbriata (Richards) was the principal aphid. The dominant parasitoid species were Praon unicum Smith, Aphidius n. sp., A. sp., and Aphidius ervi Haliday. Their frequency in relation to the other primary parasitoids varied significantly with geographical area; P. unicum dominated the frequency distribution in southwestern British Columbia, A. n. sp., west of the Cascades, and A. sp. and A. ervi east of the Cascades. Among the secondary parasitoids, pteromalids dominated, and their frequency in relation to the other secondary parasitoids was lowest in southwestern British Columbia. The parasitization rate for P. unicum and A. n. sp. in southwestern British Columbia increased from May or June to a maximum of 0.080 +/- 0.024 and 0.090 +/- 0.084 (SD), respectively, in late July or early August. P. unicum emerged in the spring 4 wk before A. n. sp. The parasitization rate for P. unicum was lower in conventional than organic fields. Whereas aphid density increased monotonically, P. unicum had two spring peaks. A simulation model showed that these peaks could reflect discrete generations. Releases of insectary-reared P. unicum at 150 or 450 DD above 5.6 degrees C, summing from 1 January, may effectively augment the natural spring populations by creating overlapping generations.

Assessing the stability of cystatin/cysteine proteinase complexes using mildly-denaturing gelatin-polyacrylamide gel electrophoresis.

A method for assessing the stability of cystatin/cysteine proteinase complexes using mildly-denaturing gelatin-polyacrylamide gel electrophoresis (gelatin-PAGE) is described. As suggested by the use of well-known cystatins (human stefins A and B, and oryzacystatins I and II) and the plant cysteine proteinase papain, the ability of cystatin/cysteine proteinase complexes to remain stable during electrophoresis is associated with the degree of affinity between the enzyme and the inhibitor (and inversely associated with the Ki values), at least with the disulfide bond-lacking cystatins. Complexes with Ki values > or = 10(-8) M (weak interactions) are partly or completely dissociated under the conditions used, while those with lower Ki values (strong interactions) remain stable. As shown by the differential effects of two plant cystatins, oryzacystatins I and II, against a cysteine proteinase present in crude (complex) extracts from a plant pest -- the two-spotted spider mite (Tetranychus urticae Koch), the gelatin-PAGE procedure is suitable for studying the ability of cystatins to form highly stable complexes with cysteine proteinases, without the need for prior purification steps. Considering the well-recognized potential of proteinase inhibitors for pest and pathogen control, this analytical approach will be useful for rapidly assessing the respective potential of various cystatins for protection of plants, animals, and humans.