Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini.

ABSTRACT: Opisthorchis viverrini, a parasitic trematode, was recategorized as a group 1 biological carcinogen because it causes opisthorchiasis, which may result in cholangiocarcinoma. A new strategy for controlling opisthorchiasis is needed because of issues such as drug resistance and reinfection. Triosephosphate isomerase (TIM), a key enzyme in energy metabolism, is regarded as a potential drug target and vaccine candidate against various pathogens. Here, we determined the crystal structures of wild-type and 3 variants of TIMs from O. viverrini (OvTIM) at high resolution. The unique tripeptide of parasite trematodes, the SAD motif, was located on the surface of OvTIM and contributed to forming a 3₁₀-helix of the following loop in a sequence-independent manner. Through thermal stability

SUBMITTER: Son J 

PROVIDER: S-EPMC6180082 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature