Asperciones de permetrina microencapsulada para el control de la garrapata sureña del ganado, Boophilus microplus (Aeari:Ixodidae), infestando novillas lecheras Holstein en Santa Cruz, Islas Vírgenes Americanas

The effectiveness of two acaricides was evaluated for control of populations of the southern cattle tick, Boophilus microplus on dairy cattle in St. Croix, U.S. Virgin Islands. Two different concentrations of a microencapsulated (ME) formulation of permethrin (0.05% and 0.10% ai) and one concentration of coumaphos emulsifiable concentrate (EC) (0.117% ai) were sprayed on Holstein heifers that had a natural infestation of ticks. The length of residual activity of EC coumaphos and ME permethrin at 0.05% (ai) was at least four days, and for ME permethrin at 0.10% ai at least seven days.There was no apparent increase in the residual activity period of ME permethrin in comparison to that in field trials of other formulations of permethrin against B. microplus. Percentage control for the three treatment groups from days 4 through 21 was ME permethrin (0.05% ai) 96%; ME permethrin (0.10% ai), 97%; coumaphos, 98.3%. There were no significant differences among the treatment groups (F = 2.21, df = 2,17, P> 0.10). This research confirms the usefulness of permethrin as an alternative to coumaphos for control of B. microplus populations on cattle.Se evaluaron dos acaricidas por su efectividad para controlar las poblaciones de la garrapata sureña Boophilus microplus en ganado lechero en Santa Cruz, Islas Virgenes Americanas. Se asperjaron dos concentraciones diferentes de una formulación microencapsulada (ME) de permetrína (0.05 y 0.10% ia) y una concentración de coumaphos concentrado emulsificable (0,117% ia) sobre novillas Holstein que presentaban una infestación natural de garrapatas. La actividad residual del coumaphos y la permetrina ME (0.05% ia) fue por lo menos de cuatro días y la de permetrina ME (0.10% ia) fue de por lo menos siete días. El largo del periodo residual de la permetrina ME sobre el Boophilus microplus no aumentó en comparación con experimentos de campo con otras formulaciones de permetrinas. El porcentaje de control para los tres tratamientos desde los días 4 al 21 fue: permetrina ME (0.05% ia), 96%; permetrina ME (0,10% ia), 97%; coumaphos, 98.3%. Las diferencias entre las medias de los diferentes tratamientos no fueron significativas (F= 2.21; g.l. = 2,17, P> 0.10). Esta investigación confirma que la permetrina es una alternativa para el control de B. microplus en poblaciones de ganado

Nucleotide analogs and molecular modeling studies reveal key interactions involved in substrate recognition by the yeast RNA triphosphatase

RNA triphosphatases (RTPases) are involved in the addition of the distinctive cap structure found at the 5′ ends of eukaryotic mRNAs. Fungi, protozoa and some DNA viruses possess an RTPase that belongs to the triphosphate tunnel metalloenzyme family of enzymes that can also hydrolyze nucleoside triphosphates. Previous crystallization studies revealed that the phosphohydrolase catalytic core is located in a hydrophilic tunnel composed of antiparallel β-strands. However, all past efforts to obtain structural information on the interaction between RTPases and their substrates were unsuccessful. In the present study, we used computational molecular docking to model the binding of a nucleotide substrate into the yeast RTPase active site. In order to confirm the docking model and to gain additional insights into the molecular determinants involved in substrate recognition, we also evaluated both the phosphohydrolysis and the inhibitory potential of an important number of nucleotide analogs. Our study highlights the importance of specific amino acids for the binding of the sugar, base and triphosphate moieties of the nucleotide substrate, and reveals both the structural flexibility and complexity of the active site. These data illustrate the functional features required for the interaction of an RTPase with a ligand and pave the way to the use of nucleotide analogs as potential inhibitors of RTPases of pathogenic importance

The Core Protein of Classical Swine Fever Virus Is Dispensable for Virus Propagation In Vitro

Core protein of Flaviviridae is regarded as essential factor for nucleocapsid formation. Yet, core protein is not encoded by all isolates (GBV- A and GBV- C). Pestiviruses are a genus within the family Flaviviridae that affect cloven-hoofed animals, causing economically important diseases like classical swine fever (CSF) and bovine viral diarrhea (BVD). Recent findings describe the ability of NS3 of classical swine fever virus (CSFV) to compensate for disabling size increase of core protein (Riedel et al., 2010). NS3 is a nonstructural protein possessing protease, helicase and NTPase activity and a key player in virus replication. A role of NS3 in particle morphogenesis has also been described for other members of the Flaviviridae (Patkar et al., 2008; Ma et al., 2008). These findings raise questions about the necessity and function of core protein and the role of NS3 in particle assembly. A reverse genetic system for CSFV was employed to generate poorly growing CSFVs by modification of the core gene. After passaging, rescued viruses had acquired single amino acid substitutions (SAAS) within NS3 helicase subdomain 3. Upon introduction of these SAAS in a nonviable CSFV with deletion of almost the entire core gene (Vp447Δc), virus could be rescued. Further characterization of this virus with regard to its physical properties, morphology and behavior in cell culture did not reveal major differences between wildtype (Vp447) and Vp447Δc. Upon infection of the natural host, Vp447Δc was attenuated. Hence we conclude that core protein is not essential for particle assembly of a core-encoding member of the Flaviviridae, but important for its virulence. This raises questions about capsid structure and necessity, the role of NS3 in particle assembly and the function of core protein in general