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
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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.
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