Abstract:
: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.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Oropeza-Wekerle RL,Muller S,Briand JP,Benz R,Schmid A,Goebel Wdoi
10.1111/j.1365-2958.1992.tb00843.xsubject
Has Abstractpub_date
1992-01-01 00:00:00pages
115-21issue
1eissn
0950-382Xissn
1365-2958journal_volume
6pub_type
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