Thioredoxin H (TrxH) contributes to adversity adaptation and pathogenicity of Edwardsiella piscicida
Abstract Thioredoxins (Trxs) play an important role in defending against oxidative stress and keeping disulfide bonding correct to maintain protein function. Edwardsiella piscicida, a severe fish pathogen, has been shown to encode several thioredoxins including TrxA, TrxC, and TrxH, but their biolog...
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doaj-3f6522e8b19b42deaae09a36a88561782020-11-25T03:00:54ZengBMCVeterinary Research1297-97162019-04-0150111310.1186/s13567-019-0645-zThioredoxin H (TrxH) contributes to adversity adaptation and pathogenicity of Edwardsiella piscicidaBi-ying Wang0Hui-qin Huang1Shuang Li2Ping Tang3Hao-fu Dai4Jian-an Xian5Dong-mei Sun6Yong-hua Hu7College of Life Science and Technology, Heilongjiang Bayi Agricultural UniversityInstitute of Tropical Bioscience and Biotechnology, Chinese Academy of Tropical Agricultural SciencesCollege of Life Science and Technology, Heilongjiang Bayi Agricultural UniversityYunnan Agricultural UniversityInstitute of Tropical Bioscience and Biotechnology, Chinese Academy of Tropical Agricultural SciencesInstitute of Tropical Bioscience and Biotechnology, Chinese Academy of Tropical Agricultural SciencesCollege of Life Science and Technology, Heilongjiang Bayi Agricultural UniversityInstitute of Tropical Bioscience and Biotechnology, Chinese Academy of Tropical Agricultural SciencesAbstract Thioredoxins (Trxs) play an important role in defending against oxidative stress and keeping disulfide bonding correct to maintain protein function. Edwardsiella piscicida, a severe fish pathogen, has been shown to encode several thioredoxins including TrxA, TrxC, and TrxH, but their biological roles remain unknown. In this study, we characterized TrxH of E. piscicida (named TrxHEp) and examined its expression and function. TrxHEp is composed of 125 residues and possesses typical thioredoxin H motifs. Expression of trxH Ep was upregulated under conditions of oxidative stress, iron starvation, low pH, and during infection of host cells. trxH Ep expression was also regulated by ferric uptake regulator (Fur), an important global regulatory of E. piscicida. Compared to the wild type TX01, a markerless trxH Ep in-frame mutant strain TX01∆trxH exhibited markedly compromised tolerance of the pathogen to hydrogen peroxide, acid stress, and iron deficiency. Deletion of trxH Ep significantly retarded bacterial biofilm growth and decreased resistance against serum killing. Pathogenicity analysis shows that the inactivation of trxH Ep significantly impaired the ability of E. piscicida to invade host cells, reproduce in macrophages, and infect host tissues. Introduction of a trans-expressed trxH gene restored the lost virulence of TX01∆trxH. There is likely to be a complex relationship of functional complementation or expression regulation between TrxH and another two thioredoxins, TrxA and TrxC, of E. piscicida. This is the first functional report of TrxH in fish pathogens, and the findings suggest that TrxHEp is essential for coping with adverse circumstances and contributes to host infection of E. piscicida.http://link.springer.com/article/10.1186/s13567-019-0645-z |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Bi-ying Wang Hui-qin Huang Shuang Li Ping Tang Hao-fu Dai Jian-an Xian Dong-mei Sun Yong-hua Hu |
spellingShingle |
Bi-ying Wang Hui-qin Huang Shuang Li Ping Tang Hao-fu Dai Jian-an Xian Dong-mei Sun Yong-hua Hu Thioredoxin H (TrxH) contributes to adversity adaptation and pathogenicity of Edwardsiella piscicida Veterinary Research |
author_facet |
Bi-ying Wang Hui-qin Huang Shuang Li Ping Tang Hao-fu Dai Jian-an Xian Dong-mei Sun Yong-hua Hu |
author_sort |
Bi-ying Wang |
title |
Thioredoxin H (TrxH) contributes to adversity adaptation and pathogenicity of Edwardsiella piscicida |
title_short |
Thioredoxin H (TrxH) contributes to adversity adaptation and pathogenicity of Edwardsiella piscicida |
title_full |
Thioredoxin H (TrxH) contributes to adversity adaptation and pathogenicity of Edwardsiella piscicida |
title_fullStr |
Thioredoxin H (TrxH) contributes to adversity adaptation and pathogenicity of Edwardsiella piscicida |
title_full_unstemmed |
Thioredoxin H (TrxH) contributes to adversity adaptation and pathogenicity of Edwardsiella piscicida |
title_sort |
thioredoxin h (trxh) contributes to adversity adaptation and pathogenicity of edwardsiella piscicida |
publisher |
BMC |
series |
Veterinary Research |
issn |
1297-9716 |
publishDate |
2019-04-01 |
description |
Abstract Thioredoxins (Trxs) play an important role in defending against oxidative stress and keeping disulfide bonding correct to maintain protein function. Edwardsiella piscicida, a severe fish pathogen, has been shown to encode several thioredoxins including TrxA, TrxC, and TrxH, but their biological roles remain unknown. In this study, we characterized TrxH of E. piscicida (named TrxHEp) and examined its expression and function. TrxHEp is composed of 125 residues and possesses typical thioredoxin H motifs. Expression of trxH Ep was upregulated under conditions of oxidative stress, iron starvation, low pH, and during infection of host cells. trxH Ep expression was also regulated by ferric uptake regulator (Fur), an important global regulatory of E. piscicida. Compared to the wild type TX01, a markerless trxH Ep in-frame mutant strain TX01∆trxH exhibited markedly compromised tolerance of the pathogen to hydrogen peroxide, acid stress, and iron deficiency. Deletion of trxH Ep significantly retarded bacterial biofilm growth and decreased resistance against serum killing. Pathogenicity analysis shows that the inactivation of trxH Ep significantly impaired the ability of E. piscicida to invade host cells, reproduce in macrophages, and infect host tissues. Introduction of a trans-expressed trxH gene restored the lost virulence of TX01∆trxH. There is likely to be a complex relationship of functional complementation or expression regulation between TrxH and another two thioredoxins, TrxA and TrxC, of E. piscicida. This is the first functional report of TrxH in fish pathogens, and the findings suggest that TrxHEp is essential for coping with adverse circumstances and contributes to host infection of E. piscicida. |
url |
http://link.springer.com/article/10.1186/s13567-019-0645-z |
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