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首页> 外文期刊>Biochemistry >INTERACTIONS OF MONOMERIC RABBIT NEUTROPHIL DEFENSINS WITH BILAYERS - COMPARISON WITH DIMERIC HUMAN DEFENSIN HNP-2
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INTERACTIONS OF MONOMERIC RABBIT NEUTROPHIL DEFENSINS WITH BILAYERS - COMPARISON WITH DIMERIC HUMAN DEFENSIN HNP-2

机译：兔单核中性防御素与双分子的相互作用-与二聚体人类防御素HNP-2的比较

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摘要

Human antimicrobial neutrophil defensin HNP-2 has been shown to form large multimeric pores in pure 1-palmitoyl-2-oleoyl phosphatidylglycerol (POPG) bilayers that lead to all-or-none release of vesicle contents [Wimley et al. (1994) Protein Sci. 3, 1362-1373]. Because human neutrophil defensins form natural dimers in solution, the question arises as to the role of dimerization in pore formation. However, the dimers are so stable that this question is not easily answered directly, Rabbit neutrophil defensins, whose three-dimensional structures are very similar to those of human defensins, are monomeric in aqueous solution and thus provide an opportunity to test the hypothesis that dimerization may play a role in multimeric pore formation. We therefore examined the interactions of the six known rabbit neutrophil defensins with large unilamellar vesicles (LUV) under the conditions known to lead to stable pore formation by HNP-2. We find that the rabbit defensins bind strongly to LUVs formed from pure POPG or mixtures of POPG with neutral (zwitterionic) phospholipid but induce leakage of vesicle contents only from pure POPG vesicles. Rabbit defensin NP-4 does not cause leakage under any conditions examined. The remaining defensins, NP-1, NP-2, NP-3A, NP-3B, and NP-5. cause graded release of the contents of purr: POPG vesicles as does a mixture of the six defensins. The graded release indicates that the rabbit defensins do not form stable pores in the membrane. This result thus suggests that the structural features of human defensins that permit dimer formation in aqueous solution are likely to be important in the formation of multimeric ports.
机译：已显示人类抗菌素嗜中性粒细胞防御素HNP-2在纯的1-棕榈酰基-2-油酰基磷脂酰甘油（POPG）双层中形成大的多聚体孔，导致囊泡内容物的全部释放或全部释放[Wimley等。 （1994）蛋白质科学。 3，1362-1373]。由于人嗜中性粒细胞防御素在溶液中形成天然二聚体，因此出现关于二聚化在孔形成中的作用的问题。然而，二聚体是如此稳定，以至于不容易直接回答这个问题，其三维结构与人防御素的三维结构非常相似的兔嗜中性白细胞防御素在水溶液中是单体的，因此提供了一个检验二聚化这一假设的机会可能在多聚体孔形成中起作用。因此，我们在已知可导致HNP-2稳定形成孔的条件下，检查了六种已知的兔嗜中性白细胞防御素与大单层囊泡（LUV）的相互作用。我们发现，兔防御素与由纯POPG或POPG与中性（两性离子）磷脂的混合物形成的LUV强烈结合，但仅诱导纯POPG囊泡中囊泡内容物的泄漏。兔防御素NP-4在任何检查条件下均不会引起渗漏。其余防御素NP-1，NP-2，NP-3A，NP-3B和NP-5。导致purr：POPG囊泡，六种防御素的混合物分级释放。分级释放表明兔子的防御素在膜上没有形成稳定的孔。因此，该结果表明，允许在水溶液中形成二聚体的人防御素的结构特征可能在多聚体端口的形成中很重要。

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