Dose-dependent dielectrophoretic response of Cryptosporidium oocysts treated with ozone

C.M. QUINN, G.P. ARCHER, W.B. BETTS AND J.G. O'NEILL. 1996. Dielectrophoresis, the motion of particles in non-uniform electric field, was investigated as a technology with the potential for rapid analysis of ozonated Cryptosporidium parvum oocysts. The ratio of dielectrophoretic collection at two key frequencies (100 kHz and 10 MHz) was determined to compare the effects of ozonation at various dosages. A relationship was found between this ratio and the in vitro excystation value obtained at the end of the experiments. The magnitude of the ratio changed in a non-linear manner with increasing ozone dose. The results are consistent with a decrease in oocyst internal conductivity as supported by the predictions of a mathematical model for the dielectrophoresis of two-shell spherical particles.     

Evidence for the mode of antischistosomal action of hycanthone

Evidence is presented which supports the hypothesis that the mode of action, or a slight variant thereof, suggested by Hartman and Hulbert (11) to account for the mutagenic effects of hycanthone (HC) is the mechanism whereby HC exerts its antischistosomal activity. HC is metabolically activated to a reactive ester which, upon dissociation, alkylates DNA. If resistant schistosomes are unaffected because they cannot convert HC to a reactive ester they should be killed upon direct exposure to an appropriately esterified drug. Hycanthone N-methylcarbamate (HNMC) was synthesized and shown to bind to DNA and also alkylate 4-(p-nitrobenzyl)-pyridine. When tested with schistosomes kept in vitro, HNMC caused an irreversible inhibition of 3H-uridine incorporation not only in sensitive S. mansoni (as HC does) but also in HC-resistant and immature S. mansoni worms and S. japonicum worms which are only transiently inhibited by HC. After in vitro contact with HNMC for 1 h both sensitive and resistant schistosomes died in three weeks if either kept in culture or re-transplanted into the host animal. Mice infected with HC-resistant schistosomes showed a drastic worm reduction after in vivo HNMC administration.     

Hevamine: A crystalline basic protein from Hevea brasiliensis latex

The isolation and purification of a basic protein from the bottom fraction of Hevea brasiliensis latex is described. Two protein fractions were obtained by chromatography on carboxymethyl cellulose which also differed in their electrophoretic mobility in polyacrylamide gel, but the similarity of their other properties precludes their classification as two protein entities at this stage.     

Preferences for Infant Facial Features in Pet Dogs and Cats

A set of infant features (large forehead, large and low‐lying eyes, and bulging cheeks), were described in classical ethology as social releasers, simple stimuli that evoke a stereotyped response, in this case nurturing. We assessed the attractiveness of such features in the faces of dogs or cats (adults and young) or teddy bears or human infants, and also related these preferences to the degree of attachment to a pet. Overall, faces with the infant features were rated as more attractive than those without. Human infant faces were no more attractive than those of kittens or puppies. Pet faces were rated as more attractive by pet owners than non‐pet owners, regardless of whether the faces had infant features. A preference was also found for infant features in teddy bear faces. Women showed higher ratings than men for pets with infant features, but not for human infants or pets without infant features. Parents found human infants’ faces more attractive than did non‐parents, but there were no differences for other faces with infant features. Preferences were to some extent specific to the participant’s preferred pet species. Owners who were more strongly attached to their pets showed stronger preferences for photographs with infant features. The findings are discussed in terms of the concept of social releaser, and its part in the development of attachment to a pet species.     

rab3A attachment to the synaptic vesicle membrane mediated by a conserved polyisoprenylated carboxy-terminal sequence.

rab3A is a small neuronal GTP-binding protein specifically localized to synaptic vesicles. Membrane-bound rab3A behaves like an intrinsic membrane protein in vitro, but reversibly dissociates from synaptic vesicles after exocytosis in vivo. Here we demonstrate that rab3A is attached to synaptic vesicle membranes by a carboxy-terminal Cys-X-Cys sequence that is posttranslationally modified. This modification is inhibited by compactin in a mevalonate-dependent manner, suggesting that the Cys-X-Cys sequence represents a novel polyisoprenylation sequence. Isolation of a rab3 homolog from D. melanogaster reveals high evolutionary conservation of rab3A, including its carboxy-terminal Cys-X-Cys sequence. The posttranslational modifications of soluble and membrane-bound rab3A are biochemically different, but both require the carboxy-terminal Cys-X-Cys sequence and are faithfully reproduced in nonneuronal cells. Our results suggest that the carboxy-terminal Cys-X-Cys sequence of rab3A is polyisoprenylated and is used as its regulatable membrane anchor. Furthermore, the hydrophobic modification of rab3A and its correct intracellular targeting to synaptic vesicles are independent, presumably consecutive events.