Characterization of pertussis-like toxin from Salmonella spp. that catalyzes ADP-ribosylation of G proteins
Abstract Salmonella Typhimurium definitive phage type (DT) 104 produces a pertussis-like toxin (ArtAB-DT104), which catalyzes ADP-ribosylation of pertussis toxin sensitive G proteins. However, the prevalence of ArtAB and its toxicity have not been established. We report here that, in addition to DT1...
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2017
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oai:doaj.org-article:fd57dd5c8d0c49b6a838439cb478c8282021-12-02T15:05:55ZCharacterization of pertussis-like toxin from Salmonella spp. that catalyzes ADP-ribosylation of G proteins10.1038/s41598-017-02517-22045-2322https://doaj.org/article/fd57dd5c8d0c49b6a838439cb478c8282017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02517-2https://doaj.org/toc/2045-2322Abstract Salmonella Typhimurium definitive phage type (DT) 104 produces a pertussis-like toxin (ArtAB-DT104), which catalyzes ADP-ribosylation of pertussis toxin sensitive G proteins. However, the prevalence of ArtAB and its toxicity have not been established. We report here that, in addition to DT104, S. Worthington, and S. bongori, produce ArtAB homologs, designated ArtAB-SW and ArtAB-Sb, respectively. We purified and characterized these ArtAB toxins, which comprise a 27-kDa A subunit (ArtA) and 13.8-kDa pentameric B subunits (ArtB). While the sequence of the A subunit, which is ADP-ribosyltransferase, is similar to the A subunit sequences of other ArtABs, the B subunit of ArtAB-Sb is divergent compared to the B subunit sequences of other ArtABs. Intraperitoneal injection of purified ArtABs was fatal in mice; the 50% lethal doses of ArtAB-DT104 and ArtAB-SW were lower than that of ArtAB-Sb, suggesting that ArtB plays an influential role in the toxicity of ArtABs. ArtABs catalyzed ADP-ribosylation of G proteins in RAW 264.7 murine macrophage-like cells, and increased intracellular cyclic AMP levels. ArtAB-DT104 and ArtAB-SW, but not ArtAB-Sb, stimulated insulin secretion in mice; however, unlike Ptx, ArtABs did not induce leukocytosis. This disparity in biological activity may be explained by differences in ADP-ribosylation of target G proteins.Yukino TamamuraKiyoshi TanakaIkuo UchidaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017) |
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Medicine R Science Q Yukino Tamamura Kiyoshi Tanaka Ikuo Uchida Characterization of pertussis-like toxin from Salmonella spp. that catalyzes ADP-ribosylation of G proteins |
description |
Abstract Salmonella Typhimurium definitive phage type (DT) 104 produces a pertussis-like toxin (ArtAB-DT104), which catalyzes ADP-ribosylation of pertussis toxin sensitive G proteins. However, the prevalence of ArtAB and its toxicity have not been established. We report here that, in addition to DT104, S. Worthington, and S. bongori, produce ArtAB homologs, designated ArtAB-SW and ArtAB-Sb, respectively. We purified and characterized these ArtAB toxins, which comprise a 27-kDa A subunit (ArtA) and 13.8-kDa pentameric B subunits (ArtB). While the sequence of the A subunit, which is ADP-ribosyltransferase, is similar to the A subunit sequences of other ArtABs, the B subunit of ArtAB-Sb is divergent compared to the B subunit sequences of other ArtABs. Intraperitoneal injection of purified ArtABs was fatal in mice; the 50% lethal doses of ArtAB-DT104 and ArtAB-SW were lower than that of ArtAB-Sb, suggesting that ArtB plays an influential role in the toxicity of ArtABs. ArtABs catalyzed ADP-ribosylation of G proteins in RAW 264.7 murine macrophage-like cells, and increased intracellular cyclic AMP levels. ArtAB-DT104 and ArtAB-SW, but not ArtAB-Sb, stimulated insulin secretion in mice; however, unlike Ptx, ArtABs did not induce leukocytosis. This disparity in biological activity may be explained by differences in ADP-ribosylation of target G proteins. |
format |
article |
author |
Yukino Tamamura Kiyoshi Tanaka Ikuo Uchida |
author_facet |
Yukino Tamamura Kiyoshi Tanaka Ikuo Uchida |
author_sort |
Yukino Tamamura |
title |
Characterization of pertussis-like toxin from Salmonella spp. that catalyzes ADP-ribosylation of G proteins |
title_short |
Characterization of pertussis-like toxin from Salmonella spp. that catalyzes ADP-ribosylation of G proteins |
title_full |
Characterization of pertussis-like toxin from Salmonella spp. that catalyzes ADP-ribosylation of G proteins |
title_fullStr |
Characterization of pertussis-like toxin from Salmonella spp. that catalyzes ADP-ribosylation of G proteins |
title_full_unstemmed |
Characterization of pertussis-like toxin from Salmonella spp. that catalyzes ADP-ribosylation of G proteins |
title_sort |
characterization of pertussis-like toxin from salmonella spp. that catalyzes adp-ribosylation of g proteins |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/fd57dd5c8d0c49b6a838439cb478c828 |
work_keys_str_mv |
AT yukinotamamura characterizationofpertussisliketoxinfromsalmonellasppthatcatalyzesadpribosylationofgproteins AT kiyoshitanaka characterizationofpertussisliketoxinfromsalmonellasppthatcatalyzesadpribosylationofgproteins AT ikuouchida characterizationofpertussisliketoxinfromsalmonellasppthatcatalyzesadpribosylationofgproteins |
_version_ |
1718388683558617088 |