ANTIMICROBIAL PEPTIDES, ISOLATED FROM HORSESHOE-CRAB HEMOCYTES, TACHYPLESIN-II, AND POLYPHEMUSIN-I AND POLYPHEMUSIN-II - CHEMICAL STRUCTURES AND BIOLOGICAL-ACTIVITY
ANTIMICROBIAL PEPTIDES, ISOLATED FROM HORSESHOE-CRAB HEMOCYTES, TACHYPLESIN-II, AND POLYPHEMUSIN-I AND POLYPHEMUSIN-II - CHEMICAL STRUCTURES AND BIOLOGICAL-ACTIVITY
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DOI：
10.1093/oxfordjournals.jbchem.a122913
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发表时间：
1989-10-01
影响因子：
2.7
通讯作者：
SHIMONISHI, Y
中科院分区：
文献类型：
--
作者：
MIYATA, T;TOKUNAGA, F;SHIMONISHI, Y
Tachyplesin是最近在日本马蹄蟹(Tachypleus Tridentatus)血细胞的酸性提取物中发现的一种抗菌肽[Nakamura，T.et al.(1988)J.Biol.化学。263、16709-16713]。在我们对该多肽的持续研究中，我们在中华绒螯蟹的血细胞中发现了一种异肽--河蟹多粘菌素II，也发现了多粘菌素I和II。这些多肽的完整一级结构被确定为：Polyphemusin I，NH2-R-R-W-C-F-R-V-C-Y-R-G-F-C-Y-R-K-C-R-COHN2，Polyphemusin II，NH2-R-R-W-C-F-R-V-C-Y-K-G-F-C-Y-R-K-C-R-CONH2，和Tachyplesin II，NH2-R-W-C-F-R-V-C-Y-R-G-I-C-Y-R-K-C-R-CONH2。异肽Tachyplesin II由17个残基组成，端基为精氨酸α-酰胺。另一方面，由于在NH2末端增加了一个Arg残基以及COOH末端的精氨酸α-酰胺，多粘菌素I和II都被发现含有18个残基。多肽I的二硫键由Cys-4和Cys-17之间以及Cys-8和Cys-13之间的两个桥组成，这与Tachyplesin I的情况相同。此外，所有这些多肽不仅抑制革兰氏阴性和阳性细菌的生长，而且还抑制真菌，如白色念珠菌M9。此外，在双向扩散试验中还观察到这些多肽与细菌脂多糖之间形成了络合物。这些结果表明，中国对虾血细胞膜上可能存在中国仓鼠抗菌素和多粘菌素，它们在血细胞膜上作用于抗菌肽，是河蟹抵御入侵微生物的一种自卫机制。
Tachyplesin is an antimicrobial peptide recently found in the acid extract of hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus) [Nakamura, T. et al. (1988) J. Biol. Chem. 263, 16709-16713]. In our continuing studies on the peptide, we have found an isopeptide, tachyplesin II, and also polyphemusins I and II in hemocytes of the American horseshoe crab (Limulus polyphemus). The complete primary structures of these peptides, which are very similar to that of the previously isolated peptide, now named tachyplesin I, were determined to be as follows: Polyphemusin I, NH2-R-R-W-C-F-R-V-C-Y-R-G-F-C-Y-R-K-C-R-COHN2, Polyphemusin II, NH2-R-R-W-C-F-R-V-C-Y-K-G-F-C-Y-R-K-C-R-CONH2, and Tachyplesin II, NH2-R-W-C-F-R-V-C-Y-R-G-I-C-Y-R-K-C-R-CONH2. The isopeptide, tachyplesin II, consists of 17 residues with a COOH-terminal arginine .alpha.-amide. On the other hand, both polyphemusins I and II were found to contain 18 residues due to an additional Arg residue at the NH2-terminal end as well as a COOH-terminal arginine .alpha.-amide. The disulfide linkages for polyphemusin I consisted of two bridges between Cys-4 and Cys-17 and between Cys-8 and Cys-13, which was identical to in the case of tachyplesin I. Moreover, all of these peptides inhibited the growth of not only Gram-negative and -positive bacteria but also fungi, such as Candida albicans M9. Furthermore, complex formation between these peptides and bacterial lipopolysaccharides was also observed in a double diffusion test. These results suggest that tachyplesins and polyphemusins are probably located int he hemocyte membrane, where they act on antimicrobial peptides as a self-defense mechanism in the horseshoe crab against invading microorganisms.