Abstract
The 14-3-3 family of phosphorylated serine-binding proteins acts as signaling molecules in biological processes such as metabolism, division, differentiation, autophagy, and apoptosis. Herein, we report the requirement of 14-3-3ɛ isoform from Tenebrio molitor (Tm14-3-3ɛ) in the hemocyte antimicrobial activity. The Tm14-3-3ɛ transcript is 771 nucleotides in length and encodes a polypeptide of 256 amino acid residues. The protein has the typical 14-3-3 domain, the nuclear export signal (NES) sequence, and the peptide binding residues. The Tm14-3-3ɛ transcript shows a significant three-fold expression in the hemocyte of T. molitor larvae when infected with Escherichia coli Tm14-3-3ɛ silenced larvae show significantly lower survival rates when infected with E. coli. Under Tm14-3-3ɛ silenced condition, a strong antimicrobial activity is elicited in the hemocyte of the host inoculated with E. coli. This suggests impaired secretion of antimicrobial peptides (AMP) into the hemolymph. Furthermore, a reduction in AMP secretion under Tm14-3-3ɛ silenced condition would be responsible for loss in the capacity to kill bacteria and might explain the reduced survivability of the larvae upon E. coli challenge. This shows that Tm14-3-3ɛ is required to maintain innate immunity in T. molitor by enabling antimicrobial secretion into the hemolymph and explains the functional specialization of the isoform.
Highlights
IntroductionThe 14-3-3 family of phosphorylated serine-binding proteins acts as signaling molecules in biological processes such as metabolism, division, differentiation, autophagy, and apoptosis
Trident School of Biotech Sciences, Trident Academy of Creative Technology, Chandrasekharpur, The Soil Microbiology Laboratory, Department of Soil and Geological Sciences, College of Agriculture, Jeonnam Bioindustry Foundation Bio Control Research Center, Gokseong 516-942, Korea; Department of Life Science and Biotechnology, College of Natural Sciences, Soonchunhyang University, Department of Chemistry and Biochemistry, College of Natural Sciences, California State University, These authors contributed to this work
After confirmation and validation of the full-length cDNA sequence of Tm14-3-3ε gene by cloning and sequencing, the information was submitted in GenBank under the accession number KP099937
Summary
The 14-3-3 family of phosphorylated serine-binding proteins acts as signaling molecules in biological processes such as metabolism, division, differentiation, autophagy, and apoptosis. We report the requirement of 14-3-3ε isoform from Tenebrio molitor (Tm14-3-3ε) in the hemocyte antimicrobial activity. The protein has the typical 14-3-3 domain, the nuclear export signal (NES) sequence, and the peptide binding residues. The Tm14-3-3ε transcript shows a significant three-fold expression in the hemocyte of T. molitor larvae when infected with Escherichia coli Tm14-3-3ε silenced larvae show significantly lower survival rates when infected with E. coli. This shows that Tm14-3-3ε is required to maintain innate immunity in T. molitor by enabling antimicrobial secretion into the hemolymph and explains the∗functional specialization
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