Eimeria zapi sp. n. from the Meadow Jumping Mouse, Zapus hudsonius Zimmerman in Southwestern Michigan

SYNOPSIS Four of 5 meadow jumping mice ( Zapus hudsonius ) captured had in their feces a previously undescribed species of Eimeria which is named Eimeria zapi sp. n. The sporulated oocysts measured 21.7 (19.5–24.0) × 20.3 (17.5–23.0) μm. The single-layered oocyst wall was 1.5 μm thick, rough, pitted and appeared clear-to-amber. Usually 2 polar granules could be seen. An oocyst residuum was not observed. Each sporocyst averaged 16.0 (12.5–18.0) × 9.7 (7.5–11.5) μm. A substiedal body was present. The sporocyst residuum consisted of a membrane-enclosed packet of 15 to 20 granules. This is the first species of Eimeria to be described from the genus Zapus.     

Comparative Binding of 125I-and 99mTc-Labeled Native and Glycated Low-Density Lipoprotein to Human Microvascular Endothelial Cells-Potential for Atherosclerosis Imaging?

Native (n), glycated (g), and glycoxidated (go) low-density lipoproteins (LDL) were labeled with ¹²⁵I or ^99mTc, and the labeling efficiency and binding were assessed for potential use of these LDL compounds in imaging analysis of atherosclerotic lesions (PPAR-γ receptors) by determining the number of specific receptors for nLDL, gLDL or goLDL on human microvascular endothelial cells as well as the K_D s using either ¹²⁵I-or ^99mTc-labeled LDLs. The specific activity of labeled gLDL and goLDL was much higher (for goLDL 20 times higher) than that of nLDL. Gel filtration of labeled LDLs revealed, however, that ^99mTc–g/goLDL is significantly degraded by the labeling reaction. No fragmentation was observed for ^99mTc-nLDL and all the ¹²⁵I-labeled LDL forms. Binding studies using both ¹²⁵I-and ^99mTc-nLDL indicated a weak binding affinity (K_D 10^{? 7}mol/L) to human microvascular endothelial cells. The binding affinity of ¹²⁵I-g/goLDL to these cells was significantly higher (K_D 10^{? 9}mol/L) and could be increased further by preactivation of the endothelial cells using TNFα. Incubation with ^99mTc-goLDL, however, did not result in specific binding of the ligand, possibly as a consequence of the fragmentation of the lipoprotein during the labeling. Scatchard transformation of the binding data with ^99mTc-gLDL revealed the presence of only a few binding sites. This was in contrast to the results obtained with ¹²⁵I-labeled gLDL, which revealed a much higher membrane density of scavenger receptors for this ligand. We conclude that for in vitro binding studies as well as for potential in vivo imaging, only ¹²⁵I-labeled goLDL should be used, whereas nLDL may be applied as ¹²⁵I-or ^99mTc-labeled ligand.     

Tarsal contact chemoreceptor for the host marking pheromone of the cherry fruit fly, Rhagoletis cerasi: responses to natural and synthetic compounds

Abstract. The European cherry fruit fly (Rhagoletis cerasi L.; Diptera, Tephritidae) marks cherries (Prunus avium L.) after oviposition with a host marking pheromone (HMP). The marking trail prevents additional oviposition by the same or other females into the same fruit. On the ventral side of the tarsi of both sexes, contact-chemoreceptor sensilla were identified which contain a receptor cell selectively sensitive to HMP. The HMP receptors of males were slightly more sensitive than those of females, suggesting that the more general term ‘host-marking pheromone’ is more appropriate than the previously used ‘oviposition deterring pheromone (ODP)’. The four structural isomers of the HMP, N(15R, S(β-glucopyranosyl)-oxy-8RS-hydroxypalmitoyl)-taurine, and various derivatives were synthesized and tested in an electrophysiological bioassay. Both the 8R,15R and the 8S,15RS isomers of the HMP were equally active with a threshold of about 2 times 10^-10M, and were shown to be present in the female faeces in similar proportions. The two 15S HMP isomers were about 13 times less active. Testing synthetic derivatives of the HMP molecule revealed that the presence of the four moieties of the molecule are important for the activity: taurine, palmitic acid, C₍₈₎ hydroxyl group, and glucose (C₍₁₅₎). The chain length of the fatty acid, the hydroxyl group at C₍₈₎ and the position of glucose at C₍₁₅₎ also influenced the activity. Only minor loss of activity (factor 2) relative to the natural molecule was observed when the methyl group in the C₍₁₅₎ position was removed. The removal of the β-glycosidically linked glucose (replaced by a hydroxyl group) resulted in about a 4-fold loss of activity. The cation of the HMP molecule seemed to have no effect on its activity, whereas both low and high pH reduced it significantly. Based on these results, field experiments have been initiated to control oviposition by cherry fruit flies on cherries applying the 15-desmethyl-HMP derivative.