Gloverin, an antibacterial protein from the immune hemolymph of Hyalophora pupae
Gloverin, an antibacterial protein from the immune hemolymph of Hyalophora pupae
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DOI：
10.1111/j.1432-1033.1997.00614.x
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发表时间：
1997-07-15
期刊：
影响因子：
--
通讯作者：
Bennich, H
中科院分区：
文献类型：
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作者：
Axen, A;Carlsson, A;Bennich, H
Gloverin是从大蚕蛾Hyalophora的蛹中分离的可诱导的抗菌昆虫蛋白。这是一个基本（pI 8.5）蛋白，分子量为13.8 kDa，含有大量甘氨酸残基（18.5%），但不含半胱氨酸，并且其氨基酸序列与任何已知蛋白质没有很强的同一性。Gloverin在1-3 μ M的最低浓度下抑制大肠杆菌的生长，即小于感染脓疱血淋巴中葛兰素浓度的5%。在其与细菌包膜中的脂多糖（LPS）相互作用之后，葛洛佛林的主要作用是特异性抑制重要外膜蛋白的合成，导致更安全的膜的渗透性增加。热处理（100 ℃，10 min）不影响葛洛芬的活性，但Mg 2+和游离LPS可抑制葛洛芬的活性。当从水环境转移到疏水环境时，gloverin分子将经历从单体无规卷曲到α-螺旋的构象转变，这一性质可能对于其与细胞结合的LPS.The活性在许多方面类似于另一种抗菌蛋白attacin。最初发现于Hyalophora [综述见Boman，H. G.，菲伊岛Gudmundsson，G. H、李，J. - Y. &林霍尔姆。D. A.（1991）Eur. 201，23-31]。
Gloverin is an inducible antibacterial insect protein isolated from pupae of the giant silk moth Hyalophora. It is a basic (pI 8.5) protein with a molecular mass of 13.8 kDa, containing a large number of glycine residues (18.5%) but no cysteine, and has an amino acid sequence that reveals no strong degree of identity with any known proteins.Gloverin inhibits the growth of Escherichia coli at a minimal concentration of 1-3 mu M, i.e. less than 5% of the concentration of gloverin in the hemolymph of infected pupae. The prime effect of gloverin, following its interaction with lipopolysaccharide (LPS) in the bacterial envelope, is a specific inhibition of the synthesis of vital outer membrane proteins, leading to an increased permeability of the surer membrane. The activity of gloverin is not affected by heating (100 degrees C, 10 min) but is inhibited by Mg2+ and by free LPS. The gloverin molecule will undergo conformational transitions from a monomeric random coil to an alpha-helix upon transfer from an aqueous to a hydrophobic environment, a property likely to be of importance for its interaction with cell-bound LPS.The activity of gloverin is in many respects similar to that of attacin, another antibacterial protein. originally found in Hyalophora [for a review see Boman, H. G., Faye, I., Gudmundsson, G. H., Lee, J.-Y. & Lindholm. D. A. (1991) Eur. J. Biochem. 201, 23-31].