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The Silencing of a 14-3-3? Homolog in Tenebrio molitor Leads to Increased Antimicrobial Activity in Hemocyte and Reduces Larval Survivability.


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 14-3-3? isoform from Tenebrio molitor (Tm14-3-3?) in the hemocyte antimicrobial activity. The Tm14-3-3? 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 Tm14-3-3? transcript shows a significant three-fold expression in the hemocyte of T. molitor larvae when infected with Escherichia coli Tm14-3-3? silenced larvae show significantly lower survival rates when infected with E. coli. Under Tm14-3-3? 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 Tm14-3-3? 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 Tm14-3-3? is required to maintain innate immunity in T. molitor by enabling antimicrobial secretion into the hemolymph and explains the functional specialization of the isoform.

SUBMITTER: Seo GW 

PROVIDER: S-EPMC4999841 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

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The Silencing of a 14-3-3ɛ Homolog in Tenebrio molitor Leads to Increased Antimicrobial Activity in Hemocyte and Reduces Larval Survivability.

Seo Gi Won GW   Jo Yong Hun YH   Seong Jeong Hwan JH   Park Ki Beom KB   Patnaik Bharat Bhusan BB   Tindwa Hamisi H   Kim Sun-Am SA   Lee Yong Seok YS   Kim Yu Jung YJ   Han Yeon Soo YS  

Genes 20160820 8


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) seque  ...[more]

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