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| Intracellularly active toxin (total related VFs in database, current show from 71 to 80) |
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BoNT
(Botulinum neurotoxin) |
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BoNTs are the most toxic proteins known. Encoded on the chromosome, plasmids and bacteriophage. Seven immunologically distinct forms of BoNT exist, designated as serotypes A to G. The subtypes can differ up to 36% on the amino acid level within a given serotype. So far, more than 40 subtypes have been described in the literature. BoNT/A, B, E, F induce botulism in humans, BoNT/C and D and their mosaic variants CD and DC induce botulism in animals, BoNT/G has not been clearly assigned to a natural outbreak in humans or animals. Additionally, several novel BoNT molecules have been pronounced: BoNT/HA (also called BoNT/FA or BoNT/H) which was involved in an infant botulism case and has been characterised as a novel mosaic type toxin and BoNT/X, both produced or encoded by C. botulinum, as well as eBoNT/J (aka BoNT/En) encoded by Enterococcus faecium. BoNTs associate with non-toxic clostridial proteins to form large, stable complexes that exist in cultures known as progenitor toxins. These progenitor toxins comprise three different forms: 12S (C 300 kDa), 16S (C 500 kDa), and 19S (C 900 kDa), and consist of neurotoxin subunits coupled with one or more non-toxic components known as neurotoxin associated proteins (NAPs). NAPs possess hemagglutinin activity (HA) protect the neurotoxin from harsh environment inside host like low pH and proteases, and include HA-17, HA-22, HA-33, and HA-55. ... |
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BoNT
(Botulinum neurotoxin) |
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BoNTs are the most toxic proteins known. Encoded on the chromosome, plasmids and bacteriophage. Seven immunologically distinct forms of BoNT exist, designated as serotypes A to G. The subtypes can differ up to 36% on the amino acid level within a given serotype. So far, more than 40 subtypes have been described in the literature. BoNT/A, B, E, F induce botulism in humans, BoNT/C and D and their mosaic variants CD and DC induce botulism in animals, BoNT/G has not been clearly assigned to a natural outbreak in humans or animals. Additionally, several novel BoNT molecules have been pronounced: BoNT/HA (also called BoNT/FA or BoNT/H) which was involved in an infant botulism case and has been characterised as a novel mosaic type toxin and BoNT/X, both produced or encoded by C. botulinum, as well as eBoNT/J (aka BoNT/En) encoded by Enterococcus faecium. BoNTs associate with non-toxic clostridial proteins to form large, stable complexes that exist in cultures known as progenitor toxins. These progenitor toxins comprise three different forms: 12S (C 300 kDa), 16S (C 500 kDa), and 19S (C 900 kDa), and consist of neurotoxin subunits coupled with one or more non-toxic components known as neurotoxin associated proteins (NAPs). NAPs possess hemagglutinin activity (HA) protect the neurotoxin from harsh environment inside host like low pH and proteases, and include HA-17, HA-22, HA-33, and HA-55. ... |
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BoNT
(Botulinum neurotoxin) |
|
BoNTs are the most toxic proteins known. Encoded on the chromosome, plasmids and bacteriophage. Seven immunologically distinct forms of BoNT exist, designated as serotypes A to G. The subtypes can differ up to 36% on the amino acid level within a given serotype. So far, more than 40 subtypes have been described in the literature. BoNT/A, B, E, F induce botulism in humans, BoNT/C and D and their mosaic variants CD and DC induce botulism in animals, BoNT/G has not been clearly assigned to a natural outbreak in humans or animals. Additionally, several novel BoNT molecules have been pronounced: BoNT/HA (also called BoNT/FA or BoNT/H) which was involved in an infant botulism case and has been characterised as a novel mosaic type toxin and BoNT/X, both produced or encoded by C. botulinum, as well as eBoNT/J (aka BoNT/En) encoded by Enterococcus faecium. BoNTs associate with non-toxic clostridial proteins to form large, stable complexes that exist in cultures known as progenitor toxins. These progenitor toxins comprise three different forms: 12S (C 300 kDa), 16S (C 500 kDa), and 19S (C 900 kDa), and consist of neurotoxin subunits coupled with one or more non-toxic components known as neurotoxin associated proteins (NAPs). NAPs possess hemagglutinin activity (HA) protect the neurotoxin from harsh environment inside host like low pH and proteases, and include HA-17, HA-22, HA-33, and HA-55. ... |
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BoNT
(Botulinum neurotoxin) |
|
BoNTs are the most toxic proteins known. Encoded on the chromosome, plasmids and bacteriophage. Seven immunologically distinct forms of BoNT exist, designated as serotypes A to G. The subtypes can differ up to 36% on the amino acid level within a given serotype. So far, more than 40 subtypes have been described in the literature. BoNT/A, B, E, F induce botulism in humans, BoNT/C and D and their mosaic variants CD and DC induce botulism in animals, BoNT/G has not been clearly assigned to a natural outbreak in humans or animals. Additionally, several novel BoNT molecules have been pronounced: BoNT/HA (also called BoNT/FA or BoNT/H) which was involved in an infant botulism case and has been characterised as a novel mosaic type toxin and BoNT/X, both produced or encoded by C. botulinum, as well as eBoNT/J (aka BoNT/En) encoded by Enterococcus faecium. BoNTs associate with non-toxic clostridial proteins to form large, stable complexes that exist in cultures known as progenitor toxins. These progenitor toxins comprise three different forms: 12S (C 300 kDa), 16S (C 500 kDa), and 19S (C 900 kDa), and consist of neurotoxin subunits coupled with one or more non-toxic components known as neurotoxin associated proteins (NAPs). NAPs possess hemagglutinin activity (HA) protect the neurotoxin from harsh environment inside host like low pH and proteases, and include HA-17, HA-22, HA-33, and HA-55. ... |
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BoNT
(Botulinum neurotoxin) |
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BoNTs are the most toxic proteins known. Encoded on the chromosome, plasmids and bacteriophage. Seven immunologically distinct forms of BoNT exist, designated as serotypes A to G. The subtypes can differ up to 36% on the amino acid level within a given serotype. So far, more than 40 subtypes have been described in the literature. BoNT/A, B, E, F induce botulism in humans, BoNT/C and D and their mosaic variants CD and DC induce botulism in animals, BoNT/G has not been clearly assigned to a natural outbreak in humans or animals. Additionally, several novel BoNT molecules have been pronounced: BoNT/HA (also called BoNT/FA or BoNT/H) which was involved in an infant botulism case and has been characterised as a novel mosaic type toxin and BoNT/X, both produced or encoded by C. botulinum, as well as eBoNT/J (aka BoNT/En) encoded by Enterococcus faecium. BoNTs associate with non-toxic clostridial proteins to form large, stable complexes that exist in cultures known as progenitor toxins. These progenitor toxins comprise three different forms: 12S (C 300 kDa), 16S (C 500 kDa), and 19S (C 900 kDa), and consist of neurotoxin subunits coupled with one or more non-toxic components known as neurotoxin associated proteins (NAPs). NAPs possess hemagglutinin activity (HA) protect the neurotoxin from harsh environment inside host like low pH and proteases, and include HA-17, HA-22, HA-33, and HA-55. ... |
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BoNT
(Botulinum neurotoxin) |
|
BoNTs are the most toxic proteins known. Encoded on the chromosome, plasmids and bacteriophage. Seven immunologically distinct forms of BoNT exist, designated as serotypes A to G. The subtypes can differ up to 36% on the amino acid level within a given serotype. So far, more than 40 subtypes have been described in the literature. BoNT/A, B, E, F induce botulism in humans, BoNT/C and D and their mosaic variants CD and DC induce botulism in animals, BoNT/G has not been clearly assigned to a natural outbreak in humans or animals. Additionally, several novel BoNT molecules have been pronounced: BoNT/HA (also called BoNT/FA or BoNT/H) which was involved in an infant botulism case and has been characterised as a novel mosaic type toxin and BoNT/X, both produced or encoded by C. botulinum, as well as eBoNT/J (aka BoNT/En) encoded by Enterococcus faecium. BoNTs associate with non-toxic clostridial proteins to form large, stable complexes that exist in cultures known as progenitor toxins. These progenitor toxins comprise three different forms: 12S (C 300 kDa), 16S (C 500 kDa), and 19S (C 900 kDa), and consist of neurotoxin subunits coupled with one or more non-toxic components known as neurotoxin associated proteins (NAPs). NAPs possess hemagglutinin activity (HA) protect the neurotoxin from harsh environment inside host like low pH and proteases, and include HA-17, HA-22, HA-33, and HA-55. ... |
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BoNT
(Botulinum neurotoxin) |
|
BoNTs are the most toxic proteins known. Encoded on the chromosome, plasmids and bacteriophage. Seven immunologically distinct forms of BoNT exist, designated as serotypes A to G. The subtypes can differ up to 36% on the amino acid level within a given serotype. So far, more than 40 subtypes have been described in the literature. BoNT/A, B, E, F induce botulism in humans, BoNT/C and D and their mosaic variants CD and DC induce botulism in animals, BoNT/G has not been clearly assigned to a natural outbreak in humans or animals. Additionally, several novel BoNT molecules have been pronounced: BoNT/HA (also called BoNT/FA or BoNT/H) which was involved in an infant botulism case and has been characterised as a novel mosaic type toxin and BoNT/X, both produced or encoded by C. botulinum, as well as eBoNT/J (aka BoNT/En) encoded by Enterococcus faecium. BoNTs associate with non-toxic clostridial proteins to form large, stable complexes that exist in cultures known as progenitor toxins. These progenitor toxins comprise three different forms: 12S (C 300 kDa), 16S (C 500 kDa), and 19S (C 900 kDa), and consist of neurotoxin subunits coupled with one or more non-toxic components known as neurotoxin associated proteins (NAPs). NAPs possess hemagglutinin activity (HA) protect the neurotoxin from harsh environment inside host like low pH and proteases, and include HA-17, HA-22, HA-33, and HA-55. ... |
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BoNT
(Botulinum neurotoxin) |
|
BoNTs are the most toxic proteins known. Encoded on the chromosome, plasmids and bacteriophage. Seven immunologically distinct forms of BoNT exist, designated as serotypes A to G. The subtypes can differ up to 36% on the amino acid level within a given serotype. So far, more than 40 subtypes have been described in the literature. BoNT/A, B, E, F induce botulism in humans, BoNT/C and D and their mosaic variants CD and DC induce botulism in animals, BoNT/G has not been clearly assigned to a natural outbreak in humans or animals. Additionally, several novel BoNT molecules have been pronounced: BoNT/HA (also called BoNT/FA or BoNT/H) which was involved in an infant botulism case and has been characterised as a novel mosaic type toxin and BoNT/X, both produced or encoded by C. botulinum, as well as eBoNT/J (aka BoNT/En) encoded by Enterococcus faecium. BoNTs associate with non-toxic clostridial proteins to form large, stable complexes that exist in cultures known as progenitor toxins. These progenitor toxins comprise three different forms: 12S (C 300 kDa), 16S (C 500 kDa), and 19S (C 900 kDa), and consist of neurotoxin subunits coupled with one or more non-toxic components known as neurotoxin associated proteins (NAPs). NAPs possess hemagglutinin activity (HA) protect the neurotoxin from harsh environment inside host like low pH and proteases, and include HA-17, HA-22, HA-33, and HA-55. ... |
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| C3 toxin |
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A single-domain (A-only) mART toxin. The prototype C. botulinum exoenzyme C3bot includes the isoforms C3bot1 and C3bot2. Other members of C3-like toxins have been described so far: C3lim from C. limosum, C3cer from B. cereus, C3larvin and Plx2A Paenibacillus larvae, and three isoforms C3stau1, C3stau2, and C3stau3 produced by Staphyococcus aureus. ... |
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CDT
(Clostridium difficile toxin) |
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CDT is an iota-like toxin, consisting of CDTa and CDTb components that respectively share 80 and 82% amino acid sequence identity to C. perfringens Ia and Ib. The binding component CDTb becomes active only after trypsinization. The N terminal part of CDTa is involved in interaction with the binding component. The C-terminal part of CDTa harbours the enzymatic activity. ... |
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