Open AccessThe synthesis and function of the Escherichia coli hemolysin and related RTX exotoxins
Author(s) -
Welch R.A.,
Forestier C.,
Lobo A.,
Pellett S.,
Thomas W.,
Rowe G.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05883.x
Subject(s) - hemolysin , escherichia coli , microbiology and biotechnology , exotoxin , biology , actinobacillus pleuropneumoniae , peptide sequence , toxin , bacteria , genetics , virulence , serotype , gene
The RTX group of exotoxins represents a branch of a family of exoproteins produced by Gram‐negative bacteria which share the properties of being secreted by a leader‐independent pathway and a tandemly‐repeated nine‐amino‐acid sequence that is responsible for calcium binding. The Escherichia coli hemolysin (HlyA) is the prototype for the RTX exotoxin family which includes the leukotoxins of Pasteurella haemolytica and Actinobacillus actinomycetemcomitans and hemolysins from four Gram‐negative genera. A review of the genetics, synthesis, export and target cell reactivity of the E. coli hemolysin is given. An evolutionary tree of the RTX toxin family based on amino acid sequence similarity is presented.