D0179 Temperature stress, anti-oxidative enzyme activity and virus acquisition in Bemisia tabaci (Hemiptera: Aleyrodidae)

Monday, December 13, 2010
Grand Exhibit Hall (Town and Country Hotel and Convention Center)
Adeel Faruki , Biology Department, University of St. Thomas, Houston, TX
Duc Lam , Biology Department, University of St. Thomas, Houston, TX
Isioma Agboli , Biology Department, University of St. Thomas, Houston, TX
Cindy McKenzie , U.S. Horticultural Research Laboratory, USDA - ARS, Fort Pierce, FL
Robert Shatters , U.S. Horticultural Research Laboratory, USDA - ARS, Fort Pierce, FL
Rosie Rosell , Biology, University of St. Thomas, Houston, TX
In most eukaryotic systems, antioxidants provide protection when cells are exposed to stressful environmental conditions. Antioxidants, such as superoxide dismutase (SOD), glutathione peroxidase (GPX) and catalase, function in a stepwise series with SOD initially preventing oxidative damage by converting O2– free radicals to hydrogen peroxides. GPx then reduces free hydrogen peroxide to water, preventing damage to the proteins, DNA, and lipids of the cell. We hypothesize that the activity of SOD and GPx provides mechanisms that contribute to the survival of whiteflies during times of stress. Previously, we characterized and quantified SOD activity in Bemisia tabaci to determine the effects of heat stress on whiteflies fed on either begomovirus-infected tomato or healthy tomato plants. Two begomoviruses, tomato mottle virus (ToMoV) and tomato yellow leaf curl virus (TYLCV), were used in this study. Our data showed a negative correlation between SOD activity, heat stress, and the TYLCV acquisition and a positive correlation between SOD, heat stress and ToMoV acquisition. In this study, we quantified the GPx activity using a commercially available spectrophotometric assay aiming to establish a correlation between SOD and GPx activity in whiteflies under heat stress fed on begomovirus–infected plants.

doi: 10.1603/ICE.2016.48703