MORICIN, A NOVEL TYPE OF ANTIBACTERIAL PEPTIDE ISOLATED FROM THE SILKWORM, BOMBYX-MORI
MORICIN, A NOVEL TYPE OF ANTIBACTERIAL PEPTIDE ISOLATED FROM THE SILKWORM, BOMBYX-MORI
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DOI：
10.1074/jbc.270.50.29923
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发表时间：
1995-12-15
影响因子：
4.8
通讯作者：
YAMAKAWA, M
中科院分区：
文献类型：
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作者：
HARA, S;YAMAKAWA, M
从家蚕血淋巴中分离得到一种具有抗金黄色葡萄球菌活性的抗菌肽。该新多肽由42个氨基酸组成，是高度碱性的。该抗菌肽与其他抗菌肽没有明显的相似性。该多肽对多种革兰氏阴性和革兰氏阳性菌均有抗菌活性，且对革兰氏阳性菌的抗菌活性高于家蚕主要抗菌肽天蚕素B-1。这种新型多肽可以通过细菌注射进行诱导。这些结果表明，该多肽与家蚕对革兰氏阳性菌的抗菌活性有关。多肽对细菌膜和脂体膜的作用表明，多肽的一个靶点是细菌的细胞质膜。结果还表明，含有预测的α-螺旋的多肽的N-末端部分与膜通透性的增加有关。我们建议将从家蚕中分离出来的这种新型抗菌肽命名为“Moricin”。
A novel antibacterial peptide that shows antibacterial activity against Staphylococcus aureus was isolated from the hemolymph of the silkworm, Bombyx mori. The novel peptide consisted of 42 amino acids and was highly basic. This peptide indicated no significant similarity with other antibacterial peptides. The peptide showed antibacterial activity against several Gram-negative and -positive bacteria and had a higher activity against Gram-positive bacteria than cecropin B-1, a major antibacterial peptide of B. mori. The novel peptide was inducible by bacterial injection. These results suggest that the peptide is responsible for the antibacterial activity in B. mori against Gram-positive bacteria. The effects of the peptide on bacterial and Liposomal membranes showed that a target of the peptide is the bacterial cytoplasmic membrane. The results also suggest that the N-terminal portion of the peptide, containing a predicted alpha-helix, is responsible for an increase in the membrane permeability. We propose the name ''moricin'' for this novel antibacterial peptide isolated from B. mori.