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Alternate subunit assembly diversifies the function of a bacterial toxin
Bacterial toxins with an AB 5 architecture consist of an active (A) subunit inserted into a ring-like platform comprised of five delivery (B) subunits. Salmonella Typhi, the cause of typhoid fever, produces an unusual A 2 B 5 toxin known as typhoid toxin. Here, we report that upon infection of human...
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Published in: | Nature communications 2019-08, Vol.10 (1), p.3684-10, Article 3684 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Bacterial toxins with an AB
5
architecture consist of an active (A) subunit inserted into a ring-like platform comprised of five delivery (B) subunits.
Salmonella
Typhi, the cause of typhoid fever, produces an unusual A
2
B
5
toxin known as typhoid toxin. Here, we report that upon infection of human cells,
S
. Typhi produces two forms of typhoid toxin that have distinct delivery components but share common active subunits. The two typhoid toxins exhibit different trafficking properties, elicit different effects when administered to laboratory animals, and are expressed using different regulatory mechanisms and in response to distinct metabolic cues. Collectively, these results indicate that the evolution of two typhoid toxin variants has conferred functional versatility to this virulence factor. More broadly, this study reveals a new paradigm in toxin biology and suggests that the evolutionary expansion of AB
5
toxins was likely fueled by the plasticity inherent to their structural design coupled to the functional versatility afforded by the combination of homologous toxin components.
Salmonella
Typhi produces the typhoid toxin. Here, Fowler et al. show that
S
. Typhi produces two forms of typhoid toxin that are differentially regulated and display different trafficking properties and different effects when administered to laboratory animals. |
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ISSN: | 2041-1723 2041-1723 |
DOI: | 10.1038/s41467-019-11592-0 |