›› 2009, Vol. 52 ›› Issue (1): 27-32.

• RESEARCH PAPERS • Previous Articles     Next Articles

Purification and partial biological functions of β-1,3-glucan recognition protein from Tenebrio molitor (Coleoptera: Tenebrionidae) larvae

  

  • Online:2009-01-20 Published:2009-01-20

Abstract: One kind of β-1,3-glucan recognition protein (Tm-βGRP) was purified from Tenebrio molitor larvae by such traditional means as neutral salt precipitation and gel chromatography, etc., and its biological functions in pro-phenoloxidase activation system were primarily studied. The results showed that the molecular weight of Tm-βGRP was approximately 70 kDa, and the protein mainly existed in plasma. Purified Tm-βGRP could only specifically recognize β-1,3-glucan, but not peptidoglycan. During the process of pro-phenoloxidase activation induced by β-1,3-glucan, with the proceeding of pro-phenoloxidase activation, the amount of endogenous Tm-βGRP decreased significantly. The polyclonal antibody against Tm-βGRP could inhibit phenoloxidase activity in the hemolymph of T. molitor induced by β-1, 3-glucan in a dose-dependent manner. This research may help us deeply elucidate the biological function of β-1, 3-glucan in pro-phenoloxidase activation system in the hemolymph of T. molitor.

Key words: Tenebrio molitor, β-1, 3-glucan recognition protein, isolation and purification, biological function, pro-phenoloxidase activation system, innate immunity