Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.ijbiomac.2020.01.114
Title: Trxlp, a thioredoxin-like effector from Edwardsiella piscicida inhibits cellular redox signaling and nuclear translocation of NF-kappa B
Authors: Sayed, Ahmed
Chakraborty, Smarajit 
Leung, Ka Yin 
Sugii, Shigeki 
Mok, Yu Keung 
Keywords: Science & Technology
Life Sciences & Biomedicine
Physical Sciences
Biochemistry & Molecular Biology
Chemistry, Applied
Polymer Science
Chemistry
Thioredoxin-like effector
Redox signaling
Peroxiredoxin
III SECRETION SYSTEM
HYDROGEN-PEROXIDE
ACTIVE-SITE
ACTIVATION
PEROXIREDOXIN
TARDA
VIRULENCE
MECHANISM
PROTEINS
BACKBONE
Issue Date: 1-Apr-2020
Publisher: ELSEVIER
Citation: Sayed, Ahmed, Chakraborty, Smarajit, Leung, Ka Yin, Sugii, Shigeki, Mok, Yu Keung (2020-04-01). Trxlp, a thioredoxin-like effector from Edwardsiella piscicida inhibits cellular redox signaling and nuclear translocation of NF-kappa B. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 148 : 89-101. ScholarBank@NUS Repository. https://doi.org/10.1016/j.ijbiomac.2020.01.114
Abstract: © 2020 Elsevier B.V. Redox signaling and homeostasis are essential for cell survival and the immune response. Peroxiredoxin (Prx) modulates the level of H2O2 as a redox signal through H2O2 decomposition. The redox activity of thioredoxin (Trx) is required as a reducing equivalent to regenerate Prx. Edwardsiella piscicida is an opportunistic Gram-negative enteric pathogen that secretes a novel Trx-like effector protein, ETAE_2186 (Trxlp). Trxlp has unique structural properties compared with other Trx proteins. In enzymatic and binding assays, we confirmed Trxlp to be redox-inactive due to the low reactivity and flexibility of the resolving cysteine residue, C35, at the active site motif “31WCXXC35”. We identified key residues near the active site that are critical for reactivity and flexibility of C35 by site-directed mutagenesis analysis. NMR titration experiment demonstrated prolong inhibitory interaction of Trxlp with Prx1 resulting in the repression of Prx1–mediated H2O2 decomposition leading to increased ROS accumulation in infected host cells. Increased ROS in turn prevented nuclear translocation of NF-κB and inhibition of NF-κB target genes, leading to bacterial survival and enhanced replication inside host cells. Targeting Trxlp-mediated virulence promises to attenuate E. piscicida infection.
Source Title: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
URI: https://scholarbank.nus.edu.sg/handle/10635/168865
ISSN: 01418130
18790003
DOI: 10.1016/j.ijbiomac.2020.01.114
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