CgCaspase-3 activates the translocation of CgGSDME in haemocytes of Pacific oyster Crassostrea gigas.
Caspase-3
Crassostrea gigas
Gasdermin E
Haemocytes
Vibrio splendidus
Journal
Fish & shellfish immunology
ISSN: 1095-9947
Titre abrégé: Fish Shellfish Immunol
Pays: England
ID NLM: 9505220
Informations de publication
Date de publication:
Dec 2022
Dec 2022
Historique:
received:
16
08
2022
revised:
12
10
2022
accepted:
19
10
2022
pubmed:
25
10
2022
medline:
20
12
2022
entrez:
24
10
2022
Statut:
ppublish
Résumé
Cysteinyl aspartate specific proteinase-3 (Caspase-3) is an important protein involved in the apoptosis and gasdermin E (GSDME)-mediated cell pyroptosis pathways in vertebrates. A Caspase-3 homologue (designated as CgCaspase-3) was previously identified as an immune receptor specific for lipopolysaccharide (LPS) to regulate apoptosis in the Pacific oyster Crassostrea gigas. In the present study, the binding activity of CgCaspase-3 to different pathogen associated molecular patterns (PAMPs) and its effects on CgGSDME translocation in haemocytes were further investigated in C. gigas. The mRNA expression of CgCaspase-3 could be detected in all the tested tissues, including hepatopancreas, labial palp, adductor muscle, gonad, gill, mantle and haemocytes, and it was highly expressed in labial palp, gonad, haemocytes, and adductor muscle. The mRNA expression of CgCaspase-3 in haemocytes increased significantly at 3, 24, 48 and 72 h after LPS stimulation, and it increased significantly at 6, 12, 24 and 48 h after Vibrio splendidus stimulation. The recombinant CgCaspase-3 displayed binding activity towards LPS, mannose (MAN), peptidoglycan (PGN), and polyinosinic-polycytidylic acid potassium salt (Poly (I:C)). The positive signals of CgGSDME on haemocyte membrane became stronger at 3 h after V. splendidus stimulation, compared with that of Seawater group, and the co-localization of CgCaspase-3 and CgGSDME was observed in the haemocyte membrane. After the injection of dsCgCaspase-3, the positive signals of CgGSDME on haemocyte membrane became weaker compared with that of EGFP-RNAi group at 24 h after V. splendidus stimulation. The results suggested that CgCaspase-3 was able to bind diverse PAMPs and activate the translocation of CgGSDME in haemocytes of oyster response against pathogen invasion.
Identifiants
pubmed: 36280129
pii: S1050-4648(22)00712-4
doi: 10.1016/j.fsi.2022.10.036
pii:
doi:
Substances chimiques
Caspase 3
EC 3.4.22.-
Lipopolysaccharides
0
Pathogen-Associated Molecular Pattern Molecules
0
RNA, Messenger
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
757-765Informations de copyright
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