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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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N-terminal GNBP homology domain of Gram-negative binding protein 3 functions as a beta-1,3-glucan binding motif in Tenebrio molitor

  • Lee, Han-Na (National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University) ;
  • Kwon, Hyun-Mi (National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University) ;
  • Park, Ji-Won (National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University) ;
  • Kurokawa, Kenji (National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University) ;
  • Lee, Bok-Luel (National Research Laboratory of Defense Proteins, College of Pharmacy, Pusan National University)
  • Published : 2009.08.31
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Abstract

The Toll signalling pathway in invertebrates is responsible for defense against Gram-positive bacteria and fungi, leading to the expression of antimicrobial peptides via NF-$\kappa$B-like transcription factors. Gram-negative binding protein 3 (GNBP3) detects beta-1,3-glucan, a fungal cell wall component, and activates a three step serine protease cascade for activation of the Toll signalling pathway. Here, we showed that the recombinant N-terminal domain of Tenebrio molitor GNBP3 bound to beta-1,3-glucan, but did not activate down-stream serine protease cascade in vitro. Reversely, the N-terminal domain blocked GNBP3-mediated serine protease cascade activation in vitro and also inhibited beta-1,3-glucan-mediated antimicrobial peptide induction in Tenebrio molitor larvae. These results suggest that the N-terminal GNBP homology domain of GNBP3 functions as a beta-1,3-glucan binding domain and the C-terminal domain of GNBP3 may be required for the recruitment of immediate down-stream serine protease zymogen during Toll signalling pathway activation.

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References

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