TY - JOUR T1 - Differential Activation of Diverse Glutathione Transferases of Clonorchis sinensis in Response to the Host Bile and Oxidative Stressors A1 - Bae, Young-An A1 - Ahn, Do-Whan A1 - Lee, Eung-Goo A1 - Kim, Seon-Hee A1 - Cai, Guo-Bin A1 - Kang, Insug A1 - Sohn, Woon-Mok A1 - Kong, Yoon Y1 - 2013/05/16 N2 - Author Summary Clonorchis sinensis is a trematode parasite that infects the hepatobiliary ducts of the mammals including humans. Approximately 35 million people are infected and 600 million people are at risk of infections. Epidemiological studies have convincingly demonstrated relationships between clonorchiasis and cholangiocarcinoma. C. sinensis is a Group 1 biological carcinogen. C. sinensis excretory-secretory products (ESP) constitute the first-line effector system affecting the host-parasite interrelationship. We observed global expression pattern of C. sinensis ESP in the presence of host bile/oxidative stresses, which mimics natural host environments. The secretory proteome displayed common and unique features, which might be related to its habitat in the definitive host. The universal proteins were found to be several enzymes involved in glucose metabolism, glutathione transferases (GSTs) and oxygen transporters. C. sinensis differentially regulated the secretion of diverse GSTs in response to bile and oxidative stressors, which suggested that these enzymes are importantly involved in the protection from immune cell-derived oxidizing molecules and detoxification of hydrophobic substances. C. sinensis secreted less cysteine proteases, which play roles in tissue migration and immune evasion, compared to other tissue-invasive or intravascular trematodes. Our data suggest strongly that different GSTs might have differentially evolved with their specialized functions to cope with stressful conditions and ensure parasite's long-standing survival in the hosts. JF - PLOS Neglected Tropical Diseases JA - PLOS Neglected Tropical Diseases VL - 7 IS - 5 UR - https://doi.org/10.1371/journal.pntd.0002211 SP - e2211 EP - PB - Public Library of Science M3 - doi:10.1371/journal.pntd.0002211 ER -