HEMOLYSIN-DERIVED SYNTHETIC PEPTIDES WITH PORE-FORMING AND HEMOLYTIC-ACTIVITY

被引：21

作者：

OROPEZAWEKERLE, RL

MULLER, S

BRIAND, JP

BENZ, R

SCHMID, A

GOEBEL, W

机构：

[1] UNIV WURZBURG,INST GENET & MIKROBIOL,RONTGENRING 11,W-8700 WURZBURG,GERMANY

[2] CNRS,BIOL MOLEC & CELLULAIRE,STRASBOURG,FRANCE

[3] UNIV WURZBURG,LEHRSTUHL BIOTECHNOL,W-8700 WURZBURG,GERMANY

来源：

MOLECULAR MICROBIOLOGY | 1992年 / 6卷 / 01期

关键词：

D O I：

10.1111/j.1365-2958.1992.tb00843.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Escherichia coli haemolysin (Hlya) is a pore-forming protein which belongs to the family of 'Repeat-toxins' (RTX) (Lo et al., 1987; Lally et al., 1989; Kraig et al., 1990). A model for the pore-forming structure of HlyA has been proposed (Ludwig et al., 1991) which consists of eight transmembrane segments all present in this hydrophobic region of HlyA. We report here that two synthetic peptides of 10 and 8 amino acids in length (Pep1 and Pep2, respectively), which are derived from transmembrane segment V, are able to form pores in an artificial lipid bilayer. In addition, Pep1 exhibits strong haemolytic activity when tested on human red blood cells (HRBCs). The haemolytic activity of Pep1 and of E. coli haemolysin is completely inhibited by antibodies raised against Pep1.

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页码：115 / 121

页数：7

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