Jarchau, T., Chakraborty, T., Garcia, F. and Goebel, W. (1994) Selection for transport competence of C-terminal polypeptides derived from Escherichia coli hemolysin: The shortest peptide capable of autonomous HlyB/HlyD- dependent secretion comprises the C-terminal 62 amino acids of HlyA. Molecular and General Genetics, 245, 53-60.

has been cited by the following article:

• TITLE: The lytic mechanism of Escherichia coli α-hemolysin associated to outer membrane vesicles

  AUTHORS: Vanesa Herlax, Maria Florencia Henning, Ana María Bernasconi, Felix María Goni, Laura Bakas

  KEYWORDS: OMVs; Toxin; Lipid Mixing; Hemolytic Activity; Erythrocytes

  JOURNAL NAME: Health, Vol.2 No.5, May 27, 2010

  ABSTRACT: Alpha-hemolysin (HlyA) is an extracellular toxin secreted by Escherichia coli, targeting to plasma membranes of eukaryotic cells. Recently it was found that this toxin is released to external media associated to bacterial outer membrane vesicles (OMVs), but the hemolytic mechanism in this way has not been studied yet. Our results report that HlyA is the only protein present in OMVs that is responsible for erythrocyte lysis, and show that no fusion event is involved in the lytic mechanism of OMVs-HlyA. Furthermore, the specific hemolytic activity is approximately 10 fold higher than that of purified free-HlyA, showing the same relative lysis efficiency and specificity for erythrocytes from different species. OMVs could be an important auxiliary way of secretion, acting mainly as a concentration mechanism of HlyA near the target cells. Cell lysis would occur after toxin transfer from OMVs to target membranes, as demonstrated by hemolysis kinetic studies, lipid mixing and western blot assays.