AUTHOR=Chen Min , Shi Xiao-Xiao , Wang Ni , Zhang Chao , Shi Zhe-Yi , Zhou Wen-Wu , Zhu Zeng-Rong 

TITLE=Alkaline ceramidase (ClAC) inhibition enhances heat stress response in Cyrtorhinus lividipennis (Reuter)

JOURNAL=Frontiers in Physiology

VOLUME=14

YEAR=2023

URL=https://www.frontiersin.org/journals/physiology/articles/10.3389/fphys.2023.1160846

DOI=10.3389/fphys.2023.1160846

ISSN=1664-042X

ABSTRACT=<p>Ceramidases (CDases) are vital sphingolipid enzymes involved in organismal growth and development. They have been reported as key mediators of thermal stress response. However, whether and how CDase responds to heat stress in insects remain unclear. Herein, we identified two CDase genes, <italic>C. lividipennis</italic> alkaline ceramidase (<italic>ClAC</italic>) and neutral ceramidase (<italic>ClNC</italic>), by searching the transcriptome and genome databases of the mirid bug, <italic>Cyrtorhinus lividipennis</italic>, an important natural predator of planthoppers. Quantitative PCR (qPCR) analysis showed that both <italic>ClNC</italic> and <italic>ClAC</italic> were highly expressed in nymphs than in adults. <italic>ClAC</italic> was especially highly expressed in the head, thorax, and legs, while <italic>ClNC</italic> was widely expressed in the tested organs. Only the <italic>ClAC</italic> transcription was significantly affected by heat stress. Knocking down <italic>ClAC</italic> increased the <italic>C. lividipennis</italic> nymph survival rate under heat stress. The transcriptome and lipidomics data showed that the RNA interference-mediated suppression of <italic>ClAC</italic> significantly upregulated the transcription level of <italic>catalase</italic> (<italic>CAT</italic>) and the content of long-chain base ceramides, including C16-, C18-, C24-, and C31- ceramides. In <italic>C. lividipennis</italic> nymphs, <italic>ClAC</italic> played an important role in heat stress response, and the upregulation of nymph survival rate might be caused by variation in the ceramide levels and transcriptional changes in <italic>CDase</italic> downstream genes. This study improves our understanding of the physiological functions of insect CDase under heat stress and provides valuable insights into the nature enemy application.</p>