Oxyspirura petrowi is a heteroxenous nematode that infects the harderian gland and other ocular tissues in birds. High-intensity infections often cause damage to the infected tissues. Due to the nature of the infection sites, treatment of O. petrowi in these hosts can be difficult. Fenbendazole (FBZ) is a common anthelmintic used to treat birds for helminth infections; however, little information exists as to the efficacy of the drug on O. petrowi infections. The present study aims to estimate lethal concentrations of FBZ to O. petrowi. Adult O. petrowi were maintained in vitro and exposed to doses of 5, 50, 100, and 200 µM concentrations of FBZ and included both negative and vehicle controls. Exposure lasted 7.5 days and lethality was determined for each treatment. Negative and vehicle controls did not differ, and both had 75% survival at the end of the treatment period. The percentage survivorship in ascending order of concentration, corrected for the controls, was 66.67%, 44.44%, 33.33%, and 0%. LC₁₀, LC₅₀, and LC₉₀ estimates were 7.5 ± 0.26, 49.1 ± 1.69, and 163.2 ± 5.63 µM, respectively. In the context of known pharmacokinetics of FBZ in birds, a single oral dose of FBZ can achieve exposure levels that are lethal to O. petrowi, but the drug does not stay in the system long enough. Thus, treatment of O. petrowi infections will require multiple oral doses over several days.

A novel method for metabolite monitoring is presented for diverse applications in biometric identification.

The small GTPases Arf, Ras, and Rho cycle between their active GTP-bound and inactive GDP-bound forms. Their effector proteins or inorganic redox agents regulate this cycle, which in turn regulates various important cell signals. Unlike effector protein-based regulation, redox-mediated regulation that occurs through the redox response of small GTPases to a redox agent is feasible only when the small GTPases are redox sensitive. The known redox-sensitive small GTPases including Ras and Rho have the reactive Cys in their unique redox motif. This study is the first to show the redox-response feature of Arf1 linked to a novel redox-sensitive Cys in the Arf-specific redox motif and its importance for cell functions. The Arf1 redox motif is currently the simplest form as it lacks the additional redox components found in Ras and Rho. The study also identifies critical radical intermediates implicated in the Arf1 redox response, along with the production of chemically modified nucleotides such as a GDP adduct. These results suggest the most elementary radical action-based mechanism for the Arf1 redox response. Although the presence of the radical intermediates was not reported, they were also suggested for the Ras and Rho redox response. Thus, the previously unknown mechanistic aspects of the Ras and Rho redox response are clarified by comparing them with those of Arf1.