P38 is involved in immune response by regulating inflammatory cytokine expressions in the Pacific oyster Crassostrea gigas

Jiejie Sun,Lingling Wang,Zhaojun Wu,Shuo Han,Liyan Wang,Meijia Li,Zhaoqun Liu,Linsheng Song

Published 2019 in Developmental and Comparative Immunology

ABSTRACT

ABSTRACT P38 mitogen‐activated protein kinases are serine/threonine protein kinases reportedly involved in the innate immunity of vertebrates and invertebrates. In the present study, a P38 homolog (CgP38) was characterized from the Pacific oyster Crassostrea gigas. The full‐length cDNA of CgP38 was of 1515 bp containing a 1101 bp open reading frame. A serine/threonine protein kinase (S_TKc) domain with a conserved Thr–Gly–Tyr motif and an ATRW substrate‐binding site was found in the deduced amino acid sequence of CgP38. CgP38 shared a close evolutionary relationship with ChP38 from the Hong Kong oyster Crassostrea hongkongensis. The transcript levels of CgP38 in hemocytes increased significantly from 12 h to 48 h after lipopolysaccharide (LPS) stimulation and from 12 h to 24 h after Vibrio splendidus stimulation. The phosphorylation level of CgP38 in oyster hemocytes increased significantly at 2 h after LPS stimulation. CgP38 positively regulated the expression of interleukins, such as CgIL17‐1, CgIL17‐2, CgIL17‐3, CgIL17‐4 and CgIL17‐6, and tumor necrosis factor CgTNF after LPS or V. splendidus stimulation. These results suggested that CgP38 participated in oyster immune response by regulating the expressions of inflammatory cytokines. HighlightsA P38 homolog was identified from oyster Crassostrea gigas.The expression level of CgP38 increased significantly after LPS and Vibrio splendidus stimulations.LPS induced CgP38 phosphorylation in oyster hemocytes.CgP38 regulated the production of CgIL17s and CgTNF in oysters after LPS and Vibrio splendidus stimulations.

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