A second FADD mediates coelomocyte apoptosis response to Vibrio splendidus infection in sea cucumber Apostichopus japonicus.

Autor: Wang Y; College of Fisheries and Life Science, Dalian Ocean University, Dalian, 116023, PR China., Diao J; Shandong Key Laboratory of Disease Control in Mariculture, PR China., Wang B; Guangdong Provincial Key Laboratory of Aquatic Animal Disease Control and Healthy Culture, PR China., Xu X; State Key Laboratory for Quality and Safety of Agro-products, Ningbo University, Ningbo, 315211, PR China., Gui M; State Key Laboratory for Quality and Safety of Agro-products, Ningbo University, Ningbo, 315211, PR China., Li C; State Key Laboratory for Quality and Safety of Agro-products, Ningbo University, Ningbo, 315211, PR China; Laboratory for Marine Fisheries Science and Food Production Processes, Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266071, PR China. Electronic address: lichenghua@nbu.edu.cn., Guo M; Shandong Key Laboratory of Disease Control in Mariculture, PR China; Guangdong Provincial Key Laboratory of Aquatic Animal Disease Control and Healthy Culture, PR China; State Key Laboratory for Quality and Safety of Agro-products, Ningbo University, Ningbo, 315211, PR China. Electronic address: guoming@nbu.edu.cn.
Jazyk: angličtina
Zdroj: Fish & shellfish immunology [Fish Shellfish Immunol] 2022 Aug; Vol. 127, pp. 396-404. Date of Electronic Publication: 2022 Jun 28.
DOI: 10.1016/j.fsi.2022.06.046
Abstrakt: Fas-associated protein with death domain (FADD) is a pivotal adaptor protein that functions in mediating cell death, cell cycle regulation, and particular in innate immunity by the main death receptors. In this study, a second FADD gene in sea cucumber Apostichopus japonicus (termed AjFADD-2) was cloned and its potential function in the innate responses was analyzed. The full-length cDNA of AjFADD-2 consists of 2405 bp and contains a 47 bp 5'-untranslated region (UTR), a 1629 bp 3'-UTR, and a 729 bp ORF encoding 242 amino acids. AjFADD-2 possesses two conserved domains of intracellular N-terminal death effector domain and an extracellular C-terminal death domain, which is different from the first cloned FADD gene in A. japonicus that only possesses the death domain. AjFADD-2 was examined in all sampled six tissues and was significantly induced in V. splendidus-challenged sea cucumbers and LPS-exposed coelomocytes. Subcellular localization detection showed that AjFADD-2 was primarily observed in the coelomocyte cytoplasm, and transferred to the nucleus post V. splendidus challenge. Consistently, AjFADD-2 knockdown significantly inhibited apoptosis in V. splendidus-challenged sea cucumbers and LPS-exposed coelomocytes. Taken together, our results provided evidence that AjFADD functioned as a positive regulator of coelomocytes apoptosis in response to pathogen V. splendidus challenge.
(Copyright © 2022 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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