The characterization of BCL-xL displays a non-apoptotic role in suppression of NLRP1 inflammasome assembly in common carp (Cyprinus carpio L.).

Autor: Jiang H; Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, No. 88 East Wenhua Road, Jinan, 250014, China., Zhang J; Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, No. 88 East Wenhua Road, Jinan, 250014, China., Liu T; Shandong Industrial Technician College, No.6789 West Ring Road, Weifang, 261000, China., Chen X; Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, No. 88 East Wenhua Road, Jinan, 250014, China., Yang G; Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, No. 88 East Wenhua Road, Jinan, 250014, China. Electronic address: yanggw@sdnu.edu.cn., Li H; Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, No. 88 East Wenhua Road, Jinan, 250014, China. Electronic address: lihua@sdnu.edu.cn.
Jazyk: angličtina
Zdroj: Fish & shellfish immunology [Fish Shellfish Immunol] 2024 Dec; Vol. 155, pp. 110001. Date of Electronic Publication: 2024 Nov 01.
DOI: 10.1016/j.fsi.2024.110001
Abstrakt: The NLRP1 inflammasome is a crucial muti-protein complex in the host anti-pathogen immune response. The previous studies have revealed that the anti-apoptotic protein BCL-xL played a non-apoptotic role by impeding the activation of NLRP1 inflammasome in mammals. However, the potential role of BCL-xL in regulating the inflammasome in fish remains unclear. In the present study, the BCL-xL (CcBCL-xL) was cloned from the head kidney of common carp (Cyprinus carpio L.), and its regulatory effect on the NLRP1 inflammasome was explored. It was found that CcBCL-xL predominantly localized in the brain, spleen and head kidney of common carp, and upon stimulation with Aeromonas hydrophila (A. hydrophila), Edwardsiella tarda (E. tarda), or spring viremia of carp virus (SVCV), the expression of CcBCL-xL significantly increased in multiple immune organs. The interaction between CcBCL-xL and CcNLRP1 was confirmed by co-immunoprecipitation and immunofluorescence. Meanwhile, we also found that CcBCL-xL significantly inhibited the assembly of the CcNLRP1 inflammasome, through ASC oligomerization, ASC specks formation and cytotoxicity experiments. Furthermore, our results revealed that CcBCL-xL interacted with the NACHT, LRR, FIIND, and CARD domains of CcNLRP1. Taken together, the results provide a theoretical foundation for further exploring the regulatory mechanism of NLRP1, and for the prevention and treatment of infectious diseases in fish.
Competing Interests: Declaration of competing interest The authors declare that they have no competing interests.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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