Journal
FISH & SHELLFISH IMMUNOLOGY
Volume 48, Issue -, Pages 285-294Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fsi.2015.12.014
Keywords
MKK7; JNK pathway; Litopenaeus vannamei; Vibrio parahaemolyticus
Funding
- National Natural Science Foundation of China [31402321]
- National Key Technology RD program [2011BAD13B10, 2012BAD17B03]
- China Agriculture Research System [47]
- Science and Technology Bureau of Guangdong Province [2011A020102002]
- National Infrastructure of Fishery Germplasm Resources [2012330004113000]
- Science and Technology Planning Project of Guangdong Province, China [2012A020800001]
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Mitogen-activated protein kinase kinase 7 (MKK7) is a key signal transduction regulator in c-Jun N-terminal kinase (INK) signaling pathway, which is involved in a wide range of physiological and pathological processes. In this study, we described the molecular cloning of a new member of MKK7 group from Litopenaeus vannamei named as LvMKK7. The full-length cDNA of LvMKK7 was 3093 bp in length, with an open reading frame (ORF) of 1440 bp encoding a putative protein of 479 amino acids. LvMKK7 contained a conserved kinase domain of 261 amino acids in which there was a characteristic S-K-A-K-T motif as a potential target site of phosphorylation by MKKK. Moreover, subcellular localization showed LvMKK7 was located in both the cytoplasm and the nucleus of Drosophila S2 cells. Real-time PCR indicated that LvMKK7 was universally expressed in all tested tissues and its expression in hepatopancreas was responsive to the challenge of LPS, Poly (I:C), Vibrio parahaemolyticus, Staphhylococcus aureus and white spot syndrome virus (WSSV). In addition, co-immunoprecipitation assay demonstrated that LvJNK was phosphorylated and activated by LvMKK7, which suggested LvMKK7 was the upper regulator of LvJNK. Furthermore, RNAi-mediated knockdown of LvMKK7 enhanced the sensitivity of shrimps to V. parahaemolyticus infection. Overall, our results suggested that LvMKK7 may play important roles in the shrimp innate immunity. (C) 2015 Elsevier Ltd. All rights reserved.
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