MECHANISMS OF ACTION ON ESCHERICHIA-COLI OF CECROPIN-P1 AND PR-39, 2 ANTIBACTERIAL PEPTIDES FROM PIG INTESTINE
MECHANISMS OF ACTION ON ESCHERICHIA-COLI OF CECROPIN-P1 AND PR-39, 2 ANTIBACTERIAL PEPTIDES FROM PIG INTESTINE
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DOI：
10.1128/iai.61.7.2978-2984.1993
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发表时间：
1993-07-01
影响因子：
3.1
通讯作者：
BOMAN, A
中科院分区：
文献类型：
--
作者：
BOMAN, HG;AGERBERTH, B;BOMAN, A
天蚕素P1和PR-39是从猪小肠上部分离得到的两种抗菌肽。对它们进行了测序，并研究了它们的抗菌谱(J.-Y.Lee，A.Boman，C.Sun，M.Andersson，H.Jornvall，V.Mutt和H.G.Boman，Proc.娜塔莉。阿卡德。SCI。美国86：9159-9162，；B.Agerberth，J.Y.Lee，T.Bergman，M.Carlquist，H.G.Boman，V.Mutt，和H.Jornvall，EUR。J.生物化学。202：849-854,1991)。我们现在通过使用三个不同标记的菌株来比较这两种多肽对大肠杆菌K-12的作用机制。我们的结果表明，天蚕素P1和其他天蚕素一样，通过裂解杀死细菌，这个反应需要更多的肽来杀死更多的细胞。PR-39需要大约8分钟的滞后期才能穿透野生型大肠杆菌的外膜，然后杀灭速度相当快。在envA1突变体中没有这种滞后期；在该菌株中，外膜对两种多肽都是自由渗透的。PR-39对生长的细菌的杀灭速度比不生长的细胞快；对于天蚕素P1，则没有这样的差异。同位素掺入实验表明，PR-39通过阻止蛋白质和DNA合成并导致这些成分的降解来杀灭细菌。
Cecropin P1 and PR-39 are two antibacterial peptides isolated from the upper part of the small intestine of the pig. They have been sequenced, and their antibacterial spectra have been investigated (J.-Y. Lee, A. Boman, C. Sun, M. Andersson, H. Jornvall, V. Mutt, and H. G. Boman, Proc. Natl. Acad. Sci. USA 86:9159-9162, 1989; B. Agerberth, J.-Y. Lee, T. Bergman, M. Carlquist, H. G. Boman, V. Mutt, and H. Jornvall, Eur. J. Biochem. 202:849-854, 1991). We have now compared these two peptides for their mechanism of action on Escherichia coli K-12 by using three strains with different markers. Our results show that cecropin P1, like other cecropins, kills bacteria by lysis and that this reaction requires more peptide to kill more cells. PR-39 requires a lag period of about 8 min to penetrate the outer membrane of wild-type E. coli; then killing is quite fast. This lag period was absent in the envA1 mutant; in this strain the outer membrane was freely permeable to both peptides. PR-39 killed growing bacteria faster than nongrowing cells; for cecropin P1 there was no such difference. It is suggested from isotope incorporation experiments that PR-39 kills bacteria by a mechanism that stops protein and DNA synthesis and results in degradation of these components.