TL;DRAbstract
The major cellular effect of RTX toxins has been ascribed to their pore-forming capacity, resulting in plasma membrane lesions and osmotic lysis. One group of RTX toxins consists of hemolysins, such as Escherichia coli α-hemolysin (HlyA) and Actinobacillus pleuropneumoniae (ApxIA), that are toxic for a wide range of cell types from various species including humans and ruminants. The other category embraces leukotoxins produced by A. actinomycetemcomitans (LtxA) and Pasteurella haemolytica (LktA), which display a more restricted target cell cytolytic activity. Both the number and the length of the fatty acyl groups differ among the RTX toxins. The characteristic feature of RTX toxins is a Ca2+-binding repeat domain (GGXGXDXUX, where U represents a large hydrophobic residue and X represents any amino acid) located in the C-terminal part of the protein. More recently, data have been presented that suggest that RTX toxins also affect intracellular signaling pathways without causing lysis o
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The major cellular effect of RTX toxins has been ascribed to their pore-forming capacity, resulting in plasma membrane lesions and osmotic lysis. One group of RTX toxins consists of hemolysins, such as Escherichia coli α-hemolysin (HlyA) and Actinobacillus pleuropneumoniae (ApxIA), that are toxic for a wide range of cell types from various species including humans and ruminants. The other category embraces leukotoxins produced by A. actinomycetemcomitans (LtxA) and Pasteurella haemolytica (LktA), which display a more restricted target cell cytolytic activity. Both the number and the length of the fatty acyl groups differ among the RTX toxins. The characteristic feature of RTX toxins is a Ca2+-binding repeat domain (GGXGXDXUX, where U represents a large hydrophobic residue and X represents any amino acid) located in the C-terminal part of the protein. More recently, data have been presented that suggest that RTX toxins also affect intracellular signaling pathways without causing lysis o
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