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Identification of a mitochondrial-targeting secretory protein from Nocardia seriolae which induces apoptosis in fathead minnow cells.

Authors
  • Chen, Jianlin1, 2, 3
  • Xia, Liqun1, 2, 3
  • Wang, Wenji1, 2, 3
  • Wang, Zhiwen1, 2, 3
  • Hou, Suying1, 2, 3
  • Xie, Caixia1, 2, 3
  • Cai, Jia1, 2, 3
  • Lu, Yishan1, 2, 3
  • 1 Shenzhen Institute of Guangdong Ocean University, Shenzhen City, China. , (China)
  • 2 Guangdong Provincial Key Laboratory of Pathogenic Biology and Epidemiology for Aquatic Economic Animals, Fishery College of Guangdong Ocean University, Zhanjiang City, China. , (China)
  • 3 Guangdong Provincial Engineering Research Center for Aquatic Animal Health Assessment, Shenzhen Public Service Platform for Evaluation of Marine Economic Animal Seedings, Shenzhen City, China. , (China)
Type
Published Article
Journal
Journal of fish diseases
Publication Date
Nov 01, 2019
Volume
42
Issue
11
Pages
1493–1507
Identifiers
DOI: 10.1111/jfd.13062
PMID: 31482589
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Nocardia seriolae is the main pathogen responsible for fish nocardiosis. A mitochondrial-targeting secretory protein (MTSP) 3141 with an N-terminal transit peptide (TP) from N. seriolae was predicted by bioinformatic analysis based on the genomic sequence of the N. seriolae strain ZJ0503. However, the function of the MTSP3141 and its homologs remains totally unknown. In this study, mass spectrometry analysis of the extracellular products from N. seriolae proved that MTSP3141 was a secretory protein, subcellular localization research showed the MTSP3141-GFP fusion protein co-localized with mitochondria in fathead minnow (FHM) cells, the TP played an important role in mitochondria targeting, and only the TP located at N-terminus but not C-terminus can lead to mitochondria directing. Moreover, quantitative assays of mitochondrial membrane potential (ΔΨm) value, caspase-3 activity and apoptosis-related gene (Bcl-2, Bax, Bad, Bid and p53) mRNA expression suggested that cell apoptosis was induced in FHM cells by the overexpression of both MTSP3141 and MTSP3141ΔTP (with the N-terminal TP deleted) proteins. Taken together, the results of this study indicated that the MTSP3141 of N. seriolae was a secretory protein, might target mitochondria, induce apoptosis in host cells and function as a virulence factor. © 2019 John Wiley & Sons Ltd.

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