𝔖 Bobbio Scriptorium
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E.coli hemolysin interactions with prokaryotic and eukaryotic cell membranes

✍ Scribed by Colin Hughes; Peter Stanley; Vassilis Koronakis

Book ID
102759771
Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
842 KB
Volume
14
Category
Article
ISSN
0265-9247

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✦ Synopsis

Abstract

The hemolysin toxin (HlyA) is secreted across both the cytoplasmic and outer membranes of pathogenic Escherichia coli and forms membrane pores in cells of the host immune system, causing cell dysfunction and death. The processes underlying the interaction of HlyA with the bacterial and mammalian cell membranes are remarkable. Secretion of HlyA occurs without a periplasmic intermediate and is directed by an uncleaved C‐terminal targetting signal and the HlyB and HlyD translocator proteins, the former being a member of a transporter superfamily central to import and export of a wide range of substrates by prokaryotic and eukaryotic cells. The separate process by which HlyA is targetted to mammalian cell membranes is dependent upon fatty acylation of a non‐toxic precursor, proHlyA. This is achieved by a novel mechanism directed by the activator protein HlyC, which binds to an internal proHlyA recognition sequence and provides specificity for the transfer of fatty acid from cellular acyl carrier protein.

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