Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations.
Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations.
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DOI：
10.1016/s0021-9258(18)60560-5
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发表时间：
1989-06
期刊：
影响因子：
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通讯作者：
P. Gray;G. Flaggs;S. Leong;R. Gumina;J. Weiss;C. E. Ooi;P. Elsbach
中科院分区：
文献类型：
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作者：
P. Gray;G. Flaggs;S. Leong;R. Gumina;J. Weiss;C. E. Ooi;P. Elsbach
细菌通透性增加蛋白（BPI）是从多形核白细胞颗粒中分离出来的50 - 60 kda的膜相关蛋白。一个编码人类BPI的全长cDNA克隆已经被分离出来，衍生的氨基酸序列揭示了一个与先前确定的生物学特性一致的结构。BPI可能被组织成两个结构域：氨基末端一半，先前显示包含所有已知的抗菌活性，包含大部分碱性和亲水残基。相比之下，羧基末端的一半含有比碱性更多的酸性残基，并包括几个潜在的跨膜区域，这些区域可能将全蛋白固定在颗粒膜上。BPI的细胞毒作用仅限于许多革兰氏阴性菌；这种特异性可能是由于非常基本的氨基末端对革兰氏阴性细菌包膜特有的带负电荷的脂多糖具有很强的亲和力。BPI的氨基末端与兔脂多糖结合蛋白的序列具有显著的相似性，表明两者具有相似的结合脂多糖的结构。
The bactericidal permeability increasing protein (BPI) is a 50–60-kDa membrane-associated protein isolated from granules of polymorphonuclear leukocytes. A full-length cDNA clone encoding human BPI has been isolated and the derived amino acid sequence reveals a structure that is consistent with previously determined biological properties. BPI may be organized into two domains: the amino-terminal half, previously shown to contain all known antimicrobial activity, contains a large fraction of basic and hydrophilic residues. In contrast, the carboxyl-terminal half contains more acidic than basic residues and includes several potential transmembrane regions which may anchor the holoprotein in the granule membrane. The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic aminoterminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial envelope. The amino-terminal end of BPI exhibits significant similarity with the sequence of a rabbit lipopolysaccharide-binding protein, suggesting that both molecules share a similar structure for binding lipopolysaccharides.