Major venom proteins of the fire ant Solenopsis invicta: insights into possible pheromone-binding function from mass spectrometric analysis.

Major venom proteins of the fire ant Solenopsis invicta: insights into possible pheromone-binding function from mass spectrometric analysis.
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DOI:
10.1111/imb.12388
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发表时间:
2018-08
影响因子:
2.6
通讯作者:
Renthal R
Renthal R
中科院分区:
农林科学2区
文献类型:
--
作者:
Das T;Alabi I;Colley M;Yan F;Griffith W;Bach S;Weintraub ST;Renthal R

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火蚁(Solenopsis invicta)毒液中的蛋白质被认为具有与信息素结合的功能。来自蚁后和工蚁的毒液含有这些蛋白质的不同亚型,与它们分泌的不同信息素一致,但关于毒液蛋白质的组成和腺体来源仍然存在疑问。我们发现,女王毒液包含一个以前未知的信息素结合蛋白paramount称为溶胶i 2X1。使用成像质谱,我们位于毒囊中的主要毒液蛋白,这意味着信息素可能要与毒液生物碱竞争结合。使用已知的结构的工蜂毒液蛋白溶胶i 2w,我们产生的三维同源模型的工蜂毒液蛋白溶胶i 4.02,和两个主要的毒液蛋白在女王和女性有翅类,溶胶i 2q和溶胶i 2X1。令人惊讶的是,这些模型表明,蛋白质具有相对较小的内部疏水结合口袋,这些口袋被C末端区域的约10个氨基酸阻断。为了使这些蛋白质充当疏水性配体的载体,需要发生构象变化来取代C末端区域,有点像已知在蚕蛾信息素结合蛋白中发生的机制。
Proteins in the venom of the fire ant, Solenopsis invicta, have been suggested to function in pheromone-binding. Venom from queens and workers contain different isoforms of these proteins, consistent with the differing pheromones they secrete, but questions remain about the venom protein composition and glandular source. We found that the queen venom contains a previously uncharacterized pheromone-binding protein paralog known as Sol i 2X1. Using imaging mass spectrometry, we located the main venom proteins in the poison sac, implying that pheromones might have to compete with venom alkaloids for binding. Using the known structure of the worker venom protein Sol i 2w, we generated three dimensional homology models of the worker venom protein Sol i 4.02, and of the two main venom proteins in queens and female alates, Sol i 2q and Sol i 2X1. Surprisingly, the models show that the proteins have relatively small internal hydrophobic binding pockets that are blocked by about ten amino acids of the C-terminal region. For these proteins to function as carriers of hydrophobic ligands, a conformational change would be required to displace the C-terminal region, somewhat like the mechanism known to occur in the silk moth pheromone-binding protein.
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