- Inhibition of eukaryotic translation by tetratricopeptide-repeat proteins of Orientia tsutsugamushi
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Sunyoung Bang , Chan-Ki Min , Na-Young Ha , Myung-Sik Choi , Ik-Sang Kim , Yeon-Sook Kim , Nam-Hyuk Cho
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J. Microbiol. 2016;54(2):136-144. Published online February 2, 2016
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DOI: https://doi.org/10.1007/s12275-016-5599-5
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 Abstract
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Orientia tsutsugamushi, an obligate intracellular bacterium, is
the causative agent of scrub typhus. The genome of Orientia
tsutsugamushi has revealed multiple ORFs encoding tetratricopeptide-
repeat (TPR) proteins. The TPR protein family
has been shown to be involved in a diverse spectrum of cellular
functions such as cell cycle control, transcription, protein
transport, and protein folding, especially in eukaryotic
cells. However, little is known about the function of the TPR
proteins in O. tsutsugamushi. To investigate the potential role
of TPR proteins in host-pathogen interaction, two oriential
TPR proteins were expressed in E. coli and applied for GSTpull
down assay. DDX3, a DEAD-box containing RNA helicase,
was identified as a specific eukaryotic target of the TPR
proteins. Since the RNA helicase is involved in multiple RNAmodifying
processes such as initiation of translation reaction,
we performed in vitro translation assay in the presence
of GST-TPR fusion proteins by using rabbit reticulocyte lysate
system. The TPR proteins inhibited in vitro translation
of a reporter luciferase in a dose dependent manner whereas
the GST control proteins did not. These results suggested TPR
proteins of O. tsutsugamushi might be involved in the modulation
of eukarytotic translation through the interaction with
DDX3 RNA helicase after secretion into host cytoplasm.
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