Molecules participating in insect immunity of Sarcophaga peregrina

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Molecules participating in insect immunity of Sarcophaga peregrina

Pricking the body wall of Sarcophaga peregrina (flesh fly) larvae with a needle activated the immune system of this insect and induced various immune molecules, including antibacterial proteins, in the hemolymph. In this review, I summarize and discuss the functions of these immune molecules, with particular emphasis on the dual roles of some of these molecules in defense and development.

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We purified a novel serine protease with a molecular mass of 26 kDa from Sarcophaga pupae. This protease appeared almost exclusively in the yellow body, an organ that develops temporarily in the pupae of dipteran insects and expands to form the adult midgut by engulfing the larval midgut. cDNA analysis revealed that this protease consists of 239 amino acid residues and has significant structura...

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Identification of storage-protein messenger RNA of the fleshfly Sarcophaga peregrina.

Storage-protein mRNA was found to be abundant in poly(A)-containing RNA extracted from the fat-body of third-instar larvae of Sarcophaga peregrina (fleshfly). This RNA sedimented at the position of 19S on sucrose-density-gradient centrifugation and the product of its translation in vitro was 75K protein (protein of mol.wt. 75 000), which was precipitated specifically with antibody against stora...

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Purification of lectin induced in the hemolymph of Sarcophaga peregrina larvae on injury.

A lectin was purified from the hemolymph of Sarcophaga peregrina larvae, obtained after injury of their body wall. This lectin agglutinated sheep red blood cells markedly and the hemagglutinating activity was inhibited by galactose and lactose. The active lectin was found to have a molecular weight of 190,000 and to consist of four alpha subunits and two beta subunits, with molecular weights of...

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Ionophore activity of sarcotoxin I, a bactericidal protein of Sarcophaga peregrina.

When Escherichia coli was treated with sarcotoxin I, a potent bactericidal protein of Sarcophaga peregrina (fleshfly), K+ inside of the cells leaked out rapidly and the ATP pool of the cells rapidly decreased. These results suggested that the bactericidal effect of sarcotoxin I was due to its ionophore activity, and that it blocked the generation of ATP by inhibiting formation of the proton gra...

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ژورنال

عنوان ژورنال: Proceedings of the Japan Academy, Series B

سال: 2010

ISSN: 0386-2208,1349-2896

DOI: 10.2183/pjab.86.927