The cytotoxin of Actinobacillus pleuropneumoniae (pleurotoxin) is distinct from the haemolysin and is associated with a 120 kDa polypeptide

Rycroft, Andrew N.; Williams, D.J.; Cullen, J. M.; Macdonald, J. W.

doi:10.1099/00221287-137-3-561

Cited by 51 publications

(41 citation statements)

References 24 publications

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“…These include ApxIA, ApxIIA, ApxIIIA of Actinobacillus sp. (Chang et al , 1989; Rycroft et al , 1991; Frey & Kuhnert, 2002;) and AqxA of Actinobacillus equuli (Berthoud et al , 2002) or PaxA of Pasteurella aerogenes (Frey & Kuhnert, 2002). In fact, genetic analysis suggests that RTX determinants might have evolved in Pasteurellaceae and spread to other Gram-negative bacteria by horizontal gene transfer.…”

Section: Classes Of Rtx Proteinsmentioning

confidence: 99%

RTX proteins: a highly diverse family secreted by a common mechanism

et al. 2010

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Repeats-in-toxin (RTX) exoproteins of Gram-negative bacteria form a steadily growing family of proteins with diverse biological functions. Their common feature is the unique mode of export across the bacterial envelope via the type I secretion system and the characteristic, typically nonapeptide, glycine- and aspartate-rich repeats binding Ca2+ ions. In this review, we summarize the current state of knowledge on the organization of rtx loci and on the biological and biochemical activities of therein encoded proteins. Applying several types of bioinformatic screens on the steadily growing set of sequenced bacterial genomes, over 1000 RTX family members were detected, with the biological functions of most of them remaining to be characterized. Activities of the so far characterized RTX family members are then discussed and classified according to functional categories, ranging from the historically first characterized pore-forming RTX leukotoxins, through the large multifunctional enzymatic toxins, bacteriocins, nodulation proteins, surface layer proteins, up to secreted hydrolytic enzymes exhibiting metalloprotease or lipase activities of industrial interest.

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Section: Classes Of Rtx Proteinsmentioning

confidence: 99%

RTX proteins: a highly diverse family secreted by a common mechanism

et al. 2010

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“…Both are cytotoxic and active on a broad range of cells of different types and species [45]. ApxIIIA is nonhemolytic, but it is strongly cytotoxic and targets mainly porcine alveolar macrophages and neutrophils [44,46]. The ApxA exotoxins are thought to be of particular importance as antigens for inducing protective immunity against pleuropneumonia and have been included in a broad range of tested subunit vaccines [21,47-49].…”

Section: Introductionmentioning

confidence: 99%

Type IV fimbrial subunit protein ApfA contributes to protection against porcine pleuropneumonia

Sadílková

Nepeřený

Vrzal

et al. 2012

Vet Res

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Porcine pleuropneumonia caused by Actinobacillus pleuropneumoniae accounts for serious economic losses in the pig farming industry worldwide. We examined here the immunogenicity and protective efficacy of the recombinant type IV fimbrial subunit protein ApfA as a single antigen vaccine against pleuropneumonia, or as a component of a multi-antigen preparation comprising five other recombinant antigens derived from key virulence factors of A. pleuropneumoniae (ApxIA, ApxIIA, ApxIIIA, ApxIVA and TbpB). Immunization of pigs with recombinant ApfA alone induced high levels of specific serum antibodies and provided partial protection against challenge with the heterologous A. pleuropneumoniae serotype 9 strain. This protection was higher than that engendered by vaccination with rApxIVA or rTbpB alone and similar to that observed after immunization with the tri-antigen combination of rApxIA, rApxIIA and rApxIIIA. In addition, rApfA improved the vaccination potential of the penta-antigen mixture of rApxIA, rApxIIA, rApxIIIA, rApxIVA and rTbpB proteins, where the hexa-antigen vaccine containing rApfA conferred a high level of protection on pigs against the disease. Moreover, when rApfA was used for vaccination alone or in combination with other antigens, such immunization reduced the number of pigs colonized with the challenge strain. These results indicate that ApfA could be a valuable component of an efficient subunit vaccine for the prevention of porcine pleuropneumonia.

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“…These two toxins are nonhemolytic, but they both show a significant CAMP reaction, a co-hemolytic reaction specified by the synergy of certain pore-forming toxins and the sphingomyelinase from b-hemolytic Staphylococcus aureus (Frey et al, 1994b;Kuhnert et al, 2000). ApxIIIA was shown to be highly cytotoxic against macrophages and was therefore previously also named macrophage toxin (Lally et al, 1989b;Macdonald and Rycroft, 1992;Rycroft et al, 1991). The cytotoxic activity of PaxA has not yet been analyzed.…”

Section: Introductionmentioning

confidence: 99%

“…The second cluster of RTX toxins of Pasteurellaceae currently includes only two toxins, ApxIIIA of A. pleuropneumoniae (Frey et al, 1993;Rycroft et al, 1991) and PaxA of Pasteurella aerogenes . These two toxins are nonhemolytic, but they both show a significant CAMP reaction, a co-hemolytic reaction specified by the synergy of certain pore-forming toxins and the sphingomyelinase from b-hemolytic Staphylococcus aureus (Frey et al, 1994b;Kuhnert et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

RTX toxins in Pasteurellaceae

Frey

Kuhnert

2002

International Journal of Medical Microbiology

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RTX toxins (repeats in the structural toxin) are pore-forming protein toxins produced by a broad range of pathogenic Gram-negative bacteria. In vitro, RTX toxins mostly exhibit a cytotoxic and often also a hemolytic activity. They are particularly widespread in species of the family Pasteurellaceae which cause infectious diseases, most frequently in animals but also in humans. Most RTX toxins are proteins with a molecular mass of 100 ± 200 kDa and are post-translationally activated by acylation via a specific activator protein. The repeated structure of RTX toxins, which gave them their name, is composed of iterative glycine-rich nonapeptides binding Ca 2 on the C-terminal half of the protein. Genetic analysis of RTX toxins of various species of Pasteurellaceae and of a few other Gram-negative bacteria gave evidence of horizontal transfer of genes encoding RTX toxins and led to speculations that RTX toxins might have originated from Pasteurellaceae. The toxic activities of RTX toxins in host cells may lead to necrosis and apoptosis and the underlying detailed mechanisms are currently under investigation. The impact of RTX toxins in pathogenicity and the immune responses of the host were described for several species of Pasteurellaceae. Neutralizing antibodies were shown to significantly reduce the cytotoxic activity of RTX toxins. They constitute a valuable strategy in the development of immuno-prophylactics against several animal diseases caused by pathogenic species of Pasteurellaceae. Although many RTX toxins possess cytotoxic and hemolytic activities toward a broad range of cells and erythrocytes, respectively, a few RTX toxins were shown to have cytotoxic activity only against cells of specific hosts and/or show cell-type specificity. Further evidence exists that RTX toxins play a potential role in host specificity of certain pathogens.

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The cytotoxin of Actinobacillus pleuropneumoniae (pleurotoxin) is distinct from the haemolysin and is associated with a 120 kDa polypeptide

Cited by 51 publications

References 24 publications

RTX proteins: a highly diverse family secreted by a common mechanism

RTX proteins: a highly diverse family secreted by a common mechanism

Type IV fimbrial subunit protein ApfA contributes to protection against porcine pleuropneumonia

RTX toxins in Pasteurellaceae

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