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当前位置: 首页 > 文章 > 丽蝇蛹集金小蜂寄生对寄主蛹可溶性蛋白与芳基蛋白组成与含量的影响 昆虫学报 2008,51 (10) 1003-1010
Position: Home > Articles > Effects of parasitization by Nasonia vitripennis(Hymenoptera:Pteromalidae) on the compositions and contents of soluble proteins and arylphorin in host Boettcherisca peregrina(Diptera:Sarcophagidae) pupae Acta Entomologica Sinica 2008,51 (10) 1003-1010

丽蝇蛹集金小蜂寄生对寄主蛹可溶性蛋白与芳基蛋白组成与含量的影响

作  者：
韩成香;方琦;李凯;胡萃;叶恭银
单  位：
浙江大学昆虫科学研究所;东华大学生物科学与乍物技术研究所
关键词：
丽蝇蛹集金小蜂;棕尾别麻蝇;可溶性蛋白;芳基蛋白;寄生
摘  要：
为了探讨蛹期寄生蜂对寄主蛋白代谢的寄生生理效应,利用Bradford蛋白含量测定法、Western免疫印迹法及酶联免疫吸附检测法研究了棕尾别麻蝇Boettcherisca peregrina蛹被丽蝇蛹集金小蜂Nasonia vitripennis寄生后其脂肪体和血淋巴中可溶性蛋白及芳基蛋白组成与含量的变化。结果表明:寄生蛹脂肪体和血淋巴中可溶性蛋白的组成与未寄生相比基本无明显差异;不论寄生与否寄主蛹脂肪体和血淋巴中芳基蛋白亚基分子量均为80kDa,该亚基在脂肪体中未出现降解现象,而在血淋巴中仅于寄生后12h的寄主蛹中呈现2条分子量相近的Western免疫印迹带,说明其降解可能先于未寄生对照。就含量而言,寄生蛹脂肪体中可溶性蛋白含量除寄生后24h外均显著低于未寄生对照,芳基蛋白含量除寄生后48h外也均显著低于未寄生对照,其中寄生后12h的含量仅为未寄生的32.0%。寄生蛹血淋巴中可溶性蛋白含量多低于未寄生蛹,且寄生后2,12,24h的差异达显著水平;芳基蛋白的含量均有低于未寄生的趋势,其中寄生后12h的含量为未寄生的17.0%。综合认为,丽蝇蛹集金小蜂的寄生可导致寄主脂肪体和血淋巴中可溶性蛋白及芳基蛋白含量下降。
译  名：
Effects of parasitization by Nasonia vitripennis(Hymenoptera:Pteromalidae) on the compositions and contents of soluble proteins and arylphorin in host Boettcherisca peregrina(Diptera:Sarcophagidae) pupae
作  者：
HAN Cheng-Xiang1, FANG Qi1, LI Kai2, HU Cui1, YE Gong-Yin 1,(1. Institute of Insect Sciences, Zhejiang University, Hangzhou 310029, China; 2. Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai 201620, China)
关键词：
Nasonia vitripennis; Boettcherisca peregrina; soluble proteins; arylphorin; parasitization
摘  要：
For further exploring the physiological effects of parastization by pupa-specific parasitoids on protein metabolic efficiency of hosts, the changes in compositions and contents of soluble proteins and arylphorin in the fat body and hemolymph of Boettcherisca peregrina pupae parasitized by Nasonia vitripennis were investigated by using the Bradford method for protein quantitation, Western blotting, and enzyme-linked immunosorbent assay. The results showed that the compositions of soluble proteins in the fat body and hemolymph of parasitized pupae were similar to those of non-parasitized pupae. There was a storage protein, namely arylphorin with a subunit molecular weight of 80 kDa, in the fat body and hemolymph of both parasitized and non-parasitized pupae. The arylphorin subunit was not degraded in the fat body of both parasitized and non-parasitized pupae, but was found to be broken up into two bands with similar molecular weight only in the hemolymph of parasitized pupae at 12 h after parasitization by the Western blotting. This suggests that the arylphorin in the hemolymph might be broken down earlier in parasitized pupae than in non-parasitized pupae. The contents of soluble proteins in the fat body were significantly lower in parasitized pupae than in non-parasitized pupae at all the sampling stages except at 24 h after parasitization. In contrast, the contents of arylphorin in the fat body of parasitized pupae were also significantly lower than those of non-parasitized ones except at 48 h after parasitization, only 32.0% of that for non-parasitized pupae at 12 h after parasitization. The contents of soluble proteins in the hemolymph were more or less lower in parasitized pupae than in non-parasitized pupae, and their differences were significant at 2, 12 and 24 h after parasitization. There was a tendency that the content of arylphorin in the hemolymph was lower in parasitized pupae than in non-parasitized pupae, especially at 12 h after parasitization which was only 17% as high as that in non-parasitized pupae. In general, the results suggest that the parasitization by N. vitripennis may result in marked decreases in the contents of both soluble proteins and arylphorin in the fat body and hemolymph of hosts.

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