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'''Cytotoxin-K''' ('''CytK''') is a [[protein toxin]] produced by the gram-positive bacteria ''[[Bacillus cereus]]''. It was first discovered in a certain Bacillus cereus strain which was isolated from a food poisoning epidemic that occurred in a French nursing home in 1998. There were six cases of bloody diarrhea, three of which were fatal<ref name=":1">{{Cite journal | |
'''Cytotoxin-K''' ('''CytK''') is a [[protein toxin]] produced by the gram-positive bacteria ''[[Bacillus cereus]]''. It was first discovered in a certain Bacillus cereus strain which was isolated from a food poisoning epidemic that occurred in a French nursing home in 1998. There were six cases of bloody diarrhea, three of which were fatal<ref name=":1">{{Cite journal |last1=Dietrich |first1=Richard |last2=Jessberger |first2=Nadja |last3=Ehling-Schulz |first3=Monika |last4=Märtlbauer |first4=Erwin |last5=Granum |first5=Per Einar |date=February 2021 |title=The Food Poisoning Toxins of Bacillus cereus |journal=Toxins |language=en |volume=13 |issue=2 |pages=98 |doi=10.3390/toxins13020098 |issn=2072-6651 |pmc=7911051 |pmid=33525722|doi-access=free }}</ref>. None of the known enterotoxins from B. cereus could be detected at this time. Later, this B. cereus strain and its relatives were classified as a brand-new species called Bacillus cytotoxicus, which is the thermo-tolerant member of the B. cereus genus<ref name=":2">{{Cite journal |last1=Koné |first1=Klèma Marcel |last2=Hinnekens |first2=Pauline |last3=Jovanovic |first3=Jelena |last4=Rajkovic |first4=Andreja |last5=Mahillon |first5=Jacques |date=2021-10-01 |title=New Insights into the Potential Cytotoxic Role of Bacillus cytotoxicus Cytotoxin K-1 |journal=Toxins |language=en |volume=13 |issue=10 |pages=698 |doi=10.3390/toxins13100698 |issn=2072-6651 |pmc=8540763 |pmid=34678991|doi-access=free }}</ref>. The cytotoxin-K gene is present in approximately 50% of Bacillus cereus isolates, and its expression is regulated by several factors, including temperature and nutrient availability. |
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Further studies showed that Cytotoxin-K is a [[pore-forming toxin]] that can create small holes in [[cell membrane]]s, leading to [[cell death]]. It has been shown to cause damage to [[intestinal epithelial cell]]s, indicating its potential role in the pathogenesis of ''Bacillus cereus'' infections in humans. The toxicity in humans has not been studied in detail but [[CC50 value]]s of 500-1000nM dTHP-1 cells. In addition, CytK has been shown to have [[hemolytic]] activity, meaning it can damage red blood cells.<ref name=":1" /> |
Further studies showed that Cytotoxin-K is a [[pore-forming toxin]] that can create small holes in [[cell membrane]]s, leading to [[cell death]]. It has been shown to cause damage to [[intestinal epithelial cell]]s, indicating its potential role in the pathogenesis of ''Bacillus cereus'' infections in humans. The toxicity in humans has not been studied in detail but [[CC50 value]]s of 500-1000nM dTHP-1 cells. In addition, CytK has been shown to have [[hemolytic]] activity, meaning it can damage red blood cells.<ref name=":1" /> |
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In addition to its role in ''Bacillus cereus'' pathogenesis, Cytotoxin-K has also been studied for its potential as a diagnostic tool for detecting ''Bacillus cereus'' contamination in food products. [[PCR method]]s have been analyzed that can detect the presence of CytK in food samples, showing CytK detection could be used for rapid and sensitive detection of potentially contaminated products.<ref>{{Cite journal | |
In addition to its role in ''Bacillus cereus'' pathogenesis, Cytotoxin-K has also been studied for its potential as a diagnostic tool for detecting ''Bacillus cereus'' contamination in food products. [[PCR method]]s have been analyzed that can detect the presence of CytK in food samples, showing CytK detection could be used for rapid and sensitive detection of potentially contaminated products.<ref>{{Cite journal |last1=Tallent |first1=S.M. |last2=Hait |first2=J.M. |last3=Bennett |first3=R.W. |date=April 2015 |title=Analysis of Bacillus cereus toxicity using PCR, ELISA and a lateral flow device |url=https://academic.oup.com/jambio/article/118/4/1068/6716906 |journal=Journal of Applied Microbiology |language=en |volume=118 |issue=4 |pages=1068–1075 |doi=10.1111/jam.12766|pmid=25627167 |s2cid=25638015 }}</ref> |
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Overall, the discovery and characterization of CytK have led to a greater understanding of the virulence factors of Bacillus cereus and have provided insights into potential targets for detecting, preventing and treating Bacillus cereus infections in humans.<ref name=":2" /> |
Overall, the discovery and characterization of CytK have led to a greater understanding of the virulence factors of Bacillus cereus and have provided insights into potential targets for detecting, preventing and treating Bacillus cereus infections in humans.<ref name=":2" /> |
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The Cytotoxin-K gene encodes the Cytotoxin-K toxin. It was initially suggested during the early studies that cytK is not very common among various ''B. cereus'' isolates. Further research revealed two distinct cytK gene variants with substantial sequence homology; these were designated cytK-1 and cytK-2 in accordance with their discovery. Studies showed that 89% of the amino acids in the sequences of the related toxins CytK-1 and CytK-2 are identical.<ref name=":1" /> |
The Cytotoxin-K gene encodes the Cytotoxin-K toxin. It was initially suggested during the early studies that cytK is not very common among various ''B. cereus'' isolates. Further research revealed two distinct cytK gene variants with substantial sequence homology; these were designated cytK-1 and cytK-2 in accordance with their discovery. Studies showed that 89% of the amino acids in the sequences of the related toxins CytK-1 and CytK-2 are identical.<ref name=":1" /> |
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The variations between the proteins CytK-1 and CytK-2 were centered in specific areas of the proteins. When CytK-1 was first analyzed, it was discovered that the toxin was very harmful to human intestinal epithelial cells and that it was hemolytic, dermo necrotic and that it was capable of creating pores in lipid layers.<ref name=":1" /> Although their toxicity was only around 20% that of CytK-1, the isolated CytK-2 proteins likewise demonstrated hemolysis and toxicity towards human intestinal [[Caco-2]] cells and [[Vero cell]]s. The ''B. cereus'' CytK-2 proteins, both native and recombinant, were capable of forming pores in planar [[lipid bilayer]]s, although the majority of the channels they produced had lower conductance than those made by CytK-1. Although not all CytK-2 toxins may be as dangerous as the first discovered CytK-1, it is likely that CytK-2 toxins contribute to the [[enterotoxicity]] of some strains of ''B. cereus''.<ref>{{Cite journal | |
The variations between the proteins CytK-1 and CytK-2 were centered in specific areas of the proteins. When CytK-1 was first analyzed, it was discovered that the toxin was very harmful to human intestinal epithelial cells and that it was hemolytic, dermo necrotic and that it was capable of creating pores in lipid layers.<ref name=":1" /> Although their toxicity was only around 20% that of CytK-1, the isolated CytK-2 proteins likewise demonstrated hemolysis and toxicity towards human intestinal [[Caco-2]] cells and [[Vero cell]]s. The ''B. cereus'' CytK-2 proteins, both native and recombinant, were capable of forming pores in planar [[lipid bilayer]]s, although the majority of the channels they produced had lower conductance than those made by CytK-1. Although not all CytK-2 toxins may be as dangerous as the first discovered CytK-1, it is likely that CytK-2 toxins contribute to the [[enterotoxicity]] of some strains of ''B. cereus''.<ref>{{Cite journal |last1=Fagerlund |first1=Annette |last2=Ween |first2=Ola |last3=Lund |first3=Terje |last4=Hardy |first4=Simon P. |last5=Granum |first5=Per E.YR 2004 |title=Genetic and functional analysis of the cytK family of genes in Bacillus cereus |url=https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.26975-0 |journal=Microbiology |year=2004 |volume=150 |issue=8 |pages=2689–2697 |doi=10.1099/mic.0.26975-0 |pmid=15289565 |issn=1465-2080}}</ref> |
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The production of Cytotoxin-K is important for the pathogenesis of ''Bacillus cereus'', as it plays a role in the disruption of host cell membranes, allowing the bacterium to invade and colonize host tissues.<ref name=":1" /> Understanding the different forms of CytK is important for developing effective strategies to control the spread of ''Bacillus cereus'' and prevent foodborn illness. |
The production of Cytotoxin-K is important for the pathogenesis of ''Bacillus cereus'', as it plays a role in the disruption of host cell membranes, allowing the bacterium to invade and colonize host tissues.<ref name=":1" /> Understanding the different forms of CytK is important for developing effective strategies to control the spread of ''Bacillus cereus'' and prevent foodborn illness. |
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== Structure == |
== Structure == |
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Cytotoxin K is a protein with a size of 34 [[kDa]]. The X-ray structure of this protein has not yet been determined but genetic analysis has elucidated some things about the structure. The CytK-2 gene is more studied but did not show any similarity with other genes which encode for enterotoxins produced by the bacteria B. cereus. It did show a similar sequence for a putative [[histidine kinase]] site and this can act as an recognition site for PlcR.<ref name=":3">{{Cite journal | |
Cytotoxin K is a protein with a size of 34 [[kDa]]. The X-ray structure of this protein has not yet been determined but genetic analysis has elucidated some things about the structure. The CytK-2 gene is more studied but did not show any similarity with other genes which encode for enterotoxins produced by the bacteria B. cereus. It did show a similar sequence for a putative [[histidine kinase]] site and this can act as an recognition site for PlcR.<ref name=":3">{{Cite journal |last1=Lund |first1=Terje |last2=De Buyser |first2=Marie-Laure |last3=Granum |first3=Per Einar |date=October 2000 |title=A new cytotoxin from Bacillus cereus that may cause necrotic enteritis |url=http://doi.wiley.com/10.1046/j.1365-2958.2000.02147.x |journal=Molecular Microbiology |language=en |volume=38 |issue=2 |pages=254–261 |doi=10.1046/j.1365-2958.2000.02147.x |pmid=11069652 |s2cid=5729364 |issn=0950-382X}}</ref>. PlcR does regulate the transcription of other known enterotoxins produced by this bacteria like HBL and Nhe<ref name=":3" /> which lead to believe that also CytK-2 does have a similar disease pattern like HBL and Nhe even if the sequence of the gene itself does not show this directly <ref name=":3" /> |
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The [[amino acid sequence]] of CytK-2 does actually show 30% similarity with [[α-hemolysin]] of ''[[S. aureus]]'' which lead to believe that CytK-2 falls in the same group of β-barrel channel-forming toxins<ref>{{Cite journal | |
The [[amino acid sequence]] of CytK-2 does actually show 30% similarity with [[α-hemolysin]] of ''[[S. aureus]]'' which lead to believe that CytK-2 falls in the same group of β-barrel channel-forming toxins<ref>{{Cite journal |last1=Song |first1=Langzhou |last2=Hobaugh |first2=Michael R. |last3=Shustak |first3=Christopher |last4=Cheley |first4=Stephen |last5=Bayley |first5=Hagan |last6=Gouaux |first6=J. Eric |date=1996-12-13 |title=Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore |url=https://www.science.org/doi/10.1126/science.274.5294.1859 |journal=Science |language=en |volume=274 |issue=5294 |pages=1859–1865 |doi=10.1126/science.274.5294.1859 |pmid=8943190 |bibcode=1996Sci...274.1859S |s2cid=45663016 |issn=0036-8075}}</ref> which may explain the idea that CytK plays a role in a similar disease pattern as HBL and Nhe. The [[glycine]]-rich part of CytK, which aligns the most with the stem region of α-hemolysin (64%) and may adopt a similar structure. |
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This α-hemolysin of S. aureus synthesis which really does have much similarities with CytK-2 depends on different pairs of histidine kinases and response regulators, it is therefore tempting to suggest the possibility that a two-component system with a histidine kinase and a response regulator is also involved in regulation of the transcription of CytK, in addition to PlcR' at least on behalf of and on behalf of <ref name=":3" /> who showed this recognition site in the [[promotor region]] of CytK-2. |
This α-hemolysin of S. aureus synthesis which really does have much similarities with CytK-2 depends on different pairs of histidine kinases and response regulators, it is therefore tempting to suggest the possibility that a two-component system with a histidine kinase and a response regulator is also involved in regulation of the transcription of CytK, in addition to PlcR' at least on behalf of and on behalf of <ref name=":3" /> who showed this recognition site in the [[promotor region]] of CytK-2. |
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== Mechanism of toxicity == |
== Mechanism of toxicity == |
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[[File:CytotoxinK.png|thumb|287x287px|cytotoxin K forms pores in the outer membrane]] |
[[File:CytotoxinK.png|thumb|287x287px|cytotoxin K forms pores in the outer membrane]] |
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Cytotoxin-K (CytK) is excreted via [[de Sec translocation pathway]].<ref>{{Cite journal | |
Cytotoxin-K (CytK) is excreted via [[de Sec translocation pathway]].<ref>{{Cite journal |last1=Desvaux |first1=Mickaël |last2=Hébraud |first2=Michel |date=September 2006 |title=The protein secretion systems in Listeria : inside out bacterial virulence |url=https://academic.oup.com/femsre/article-lookup/doi/10.1111/j.1574-6976.2006.00035.x |journal=FEMS Microbiology Reviews |language=en |volume=30 |issue=5 |pages=774–805 |doi=10.1111/j.1574-6976.2006.00035.x |pmid=16911044 |issn=1574-6976}}</ref> and has shown to be [[hemolytic dermonecrotic]] and highly toxic towards human [[epithelial cell]]s by inducing [[pyroptosis]].<ref>{{Cite journal |last1=Desvaux |first1=Mickaël |last2=Hébraud |first2=Michel |date=September 2006 |title=The protein secretion systems in Listeria : inside out bacterial virulence |url=https://academic.oup.com/femsre/article-lookup/doi/10.1111/j.1574-6976.2006.00035.x |journal=FEMS Microbiology Reviews |language=en |volume=30 |issue=5 |pages=774–805 |doi=10.1111/j.1574-6976.2006.00035.x |pmid=16911044 |issn=1574-6976}}</ref><ref name=":0">{{cite journal |last1=Zhao |first1=Yan |last2=Sun |first2=Li |date=4 July 2022 |title=Bacillus cereus cytotoxin K triggers gasdermin D-dependent pyroptosis |journal=Cell Death Discovery |volume=8 |issue=1 |pages=1–8 |doi=10.1038/s41420-022-01091-5|s2cid=256605262 }}</ref> Cytotoxin K induces this inflammatory cell death by interacting with [[phosphatidic acid]] (PA) and to a lesser extent PtdIns(4)P, PtdIns(4,5)P2, and PtdIns(3,4,5)P3 which are [[membrane lipid]]s <ref name=":0" /> . By binding to the cellular membrane and oligomerization of cytotoxin K the protein forms pores that have a predicted opening size of 7 Armstrong<ref name=":1" />. These pores cause changes the integrity of the membrane. As a result of this [[potassium ion]]s efflux out of the cells while calcium ions accumulate disrupting the cellular homeostasis <ref name=":0" />. The change in intercellular ion concentrations results in the activation of NLRP3 <ref name=":0" /> . NLRP3 activation results in the formation of the [[inflammasome]] which in turn activates [[Gasdermin D]] and interleukin 1B <ref name=":0" />. Gasdermin D then forms pores in the membrane and releases the interleukins and causes swelling and eventually bursting of the cell <ref>{{Cite journal |last1=Shao |first1=Bo-Zong |last2=Xu |first2=Zhe-Qi |last3=Han |first3=Bin-Ze |last4=Su |first4=Ding-Feng |last5=Liu |first5=Chong |date=2015 |title=NLRP3 inflammasome and its inhibitors: a review |journal=Frontiers in Pharmacology |volume=6 |doi=10.3389/fphar.2015.00262 |issn=1663-9812 |pmc=4633676 |pmid=26594174|doi-access=free }}</ref>. The pore forming mechanisms of the two variants CytK1 and CytK2 haven’t been fully investigated but are deducted from close protein families such as S. aureus α- and γ-hemolysin, C. perfringens β-toxin, and B. cereus hemolysin II which share significant homology.<ref name=":1" /> Thus, CytK is classified as member of the family of β-barrel pore-forming toxins<ref name=":1" /> |
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== Indications == |
== Indications == |
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Revision as of 05:18, 23 March 2023
| Cytotoxin K | |||||||
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 | |||||||
| Identifiers | |||||||
| Organism | |||||||
| Symbol | CytK | ||||||
| UniProt | Q9EVA1 | ||||||
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Cytotoxin-K (CytK) is a protein toxin produced by the gram-positive bacteria Bacillus cereus. It was first discovered in a certain Bacillus cereus strain which was isolated from a food poisoning epidemic that occurred in a French nursing home in 1998. There were six cases of bloody diarrhea, three of which were fatal[1]. None of the known enterotoxins from B. cereus could be detected at this time. Later, this B. cereus strain and its relatives were classified as a brand-new species called Bacillus cytotoxicus, which is the thermo-tolerant member of the B. cereus genus[2]. The cytotoxin-K gene is present in approximately 50% of Bacillus cereus isolates, and its expression is regulated by several factors, including temperature and nutrient availability.
Further studies showed that Cytotoxin-K is a pore-forming toxin that can create small holes in cell membranes, leading to cell death. It has been shown to cause damage to intestinal epithelial cells, indicating its potential role in the pathogenesis of Bacillus cereus infections in humans. The toxicity in humans has not been studied in detail but CC50 values of 500-1000nM dTHP-1 cells. In addition, CytK has been shown to have hemolytic activity, meaning it can damage red blood cells.[1]
In addition to its role in Bacillus cereus pathogenesis, Cytotoxin-K has also been studied for its potential as a diagnostic tool for detecting Bacillus cereus contamination in food products. PCR methods have been analyzed that can detect the presence of CytK in food samples, showing CytK detection could be used for rapid and sensitive detection of potentially contaminated products.[3]
Overall, the discovery and characterization of CytK have led to a greater understanding of the virulence factors of Bacillus cereus and have provided insights into potential targets for detecting, preventing and treating Bacillus cereus infections in humans.[2]
Available forms
The Cytotoxin-K gene encodes the Cytotoxin-K toxin. It was initially suggested during the early studies that cytK is not very common among various B. cereus isolates. Further research revealed two distinct cytK gene variants with substantial sequence homology; these were designated cytK-1 and cytK-2 in accordance with their discovery. Studies showed that 89% of the amino acids in the sequences of the related toxins CytK-1 and CytK-2 are identical.[1]
The variations between the proteins CytK-1 and CytK-2 were centered in specific areas of the proteins. When CytK-1 was first analyzed, it was discovered that the toxin was very harmful to human intestinal epithelial cells and that it was hemolytic, dermo necrotic and that it was capable of creating pores in lipid layers.[1] Although their toxicity was only around 20% that of CytK-1, the isolated CytK-2 proteins likewise demonstrated hemolysis and toxicity towards human intestinal Caco-2 cells and Vero cells. The B. cereus CytK-2 proteins, both native and recombinant, were capable of forming pores in planar lipid bilayers, although the majority of the channels they produced had lower conductance than those made by CytK-1. Although not all CytK-2 toxins may be as dangerous as the first discovered CytK-1, it is likely that CytK-2 toxins contribute to the enterotoxicity of some strains of B. cereus.[4]
The production of Cytotoxin-K is important for the pathogenesis of Bacillus cereus, as it plays a role in the disruption of host cell membranes, allowing the bacterium to invade and colonize host tissues.[1] Understanding the different forms of CytK is important for developing effective strategies to control the spread of Bacillus cereus and prevent foodborn illness.
Structure
Cytotoxin K is a protein with a size of 34 kDa. The X-ray structure of this protein has not yet been determined but genetic analysis has elucidated some things about the structure. The CytK-2 gene is more studied but did not show any similarity with other genes which encode for enterotoxins produced by the bacteria B. cereus. It did show a similar sequence for a putative histidine kinase site and this can act as an recognition site for PlcR.[5]. PlcR does regulate the transcription of other known enterotoxins produced by this bacteria like HBL and Nhe[5] which lead to believe that also CytK-2 does have a similar disease pattern like HBL and Nhe even if the sequence of the gene itself does not show this directly [5]
The amino acid sequence of CytK-2 does actually show 30% similarity with α-hemolysin of S. aureus which lead to believe that CytK-2 falls in the same group of β-barrel channel-forming toxins[6] which may explain the idea that CytK plays a role in a similar disease pattern as HBL and Nhe. The glycine-rich part of CytK, which aligns the most with the stem region of α-hemolysin (64%) and may adopt a similar structure.
This α-hemolysin of S. aureus synthesis which really does have much similarities with CytK-2 depends on different pairs of histidine kinases and response regulators, it is therefore tempting to suggest the possibility that a two-component system with a histidine kinase and a response regulator is also involved in regulation of the transcription of CytK, in addition to PlcR' at least on behalf of and on behalf of [5] who showed this recognition site in the promotor region of CytK-2.
Mechanism of toxicity
Cytotoxin-K (CytK) is excreted via de Sec translocation pathway.[7] and has shown to be hemolytic dermonecrotic and highly toxic towards human epithelial cells by inducing pyroptosis.[8][9] Cytotoxin K induces this inflammatory cell death by interacting with phosphatidic acid (PA) and to a lesser extent PtdIns(4)P, PtdIns(4,5)P2, and PtdIns(3,4,5)P3 which are membrane lipids [9] . By binding to the cellular membrane and oligomerization of cytotoxin K the protein forms pores that have a predicted opening size of 7 Armstrong[1]. These pores cause changes the integrity of the membrane. As a result of this potassium ions efflux out of the cells while calcium ions accumulate disrupting the cellular homeostasis [9]. The change in intercellular ion concentrations results in the activation of NLRP3 [9] . NLRP3 activation results in the formation of the inflammasome which in turn activates Gasdermin D and interleukin 1B [9]. Gasdermin D then forms pores in the membrane and releases the interleukins and causes swelling and eventually bursting of the cell [10]. The pore forming mechanisms of the two variants CytK1 and CytK2 haven’t been fully investigated but are deducted from close protein families such as S. aureus α- and γ-hemolysin, C. perfringens β-toxin, and B. cereus hemolysin II which share significant homology.[1] Thus, CytK is classified as member of the family of β-barrel pore-forming toxins[1]
Indications
CytK toxin is produced by certain strains of Bacillus cereus, a type of bacteria commonly found in soil, water, and food. Like other toxins produced by this bacteria, such as HBL and Nhe, consuming CytK toxin can cause diarrhea and other gastrointestinal symptoms (9).
If you suspect that you may have consumed CytK toxin, here are some indications to look out for:
- Diarrhea: This is one of the most common symptoms of CytK toxin poisoning. The diarrhea may be watery or bloody and can occur several times a day;
- Abdominal cramps: You may experience severe abdominal cramps or stomach pain;
- Nausea and vomiting: You may feel nauseous and may vomit;
- Fever: You may develop a fever along with other symptoms like a common cold;
- Dehydration: Diarrhea and vomiting can lead to dehydration. Signs of dehydration include dry mouth and throat, dark urine, and feeling lightheaded.
If you experience any of these symptoms after eating food contaminated with CytK toxin, seek medical attention immediately if after 24 hours the symptoms did not diminish, there are some cases of really worse seizures due to the intoxication (10). It's important to stay hydrated by drinking plenty of fluids, especially water or oral rehydration solutions, to replace lost fluids and electrolytes.
References
- ^ a b c d e f g h Dietrich, Richard; Jessberger, Nadja; Ehling-Schulz, Monika; Märtlbauer, Erwin; Granum, Per Einar (February 2021). "The Food Poisoning Toxins of Bacillus cereus". Toxins. 13 (2): 98. doi:10.3390/toxins13020098. ISSN 2072-6651. PMC 7911051. PMID 33525722.
- ^ a b Koné, Klèma Marcel; Hinnekens, Pauline; Jovanovic, Jelena; Rajkovic, Andreja; Mahillon, Jacques (2021-10-01). "New Insights into the Potential Cytotoxic Role of Bacillus cytotoxicus Cytotoxin K-1". Toxins. 13 (10): 698. doi:10.3390/toxins13100698. ISSN 2072-6651. PMC 8540763. PMID 34678991.
- ^ Tallent, S.M.; Hait, J.M.; Bennett, R.W. (April 2015). "Analysis of Bacillus cereus toxicity using PCR, ELISA and a lateral flow device". Journal of Applied Microbiology. 118 (4): 1068–1075. doi:10.1111/jam.12766. PMID 25627167. S2CID 25638015.
- ^ Fagerlund, Annette; Ween, Ola; Lund, Terje; Hardy, Simon P.; Granum, Per E.YR 2004 (2004). "Genetic and functional analysis of the cytK family of genes in Bacillus cereus". Microbiology. 150 (8): 2689–2697. doi:10.1099/mic.0.26975-0. ISSN 1465-2080. PMID 15289565.
{{cite journal}}: CS1 maint: numeric names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ a b c d Lund, Terje; De Buyser, Marie-Laure; Granum, Per Einar (October 2000). "A new cytotoxin from Bacillus cereus that may cause necrotic enteritis". Molecular Microbiology. 38 (2): 254–261. doi:10.1046/j.1365-2958.2000.02147.x. ISSN 0950-382X. PMID 11069652. S2CID 5729364.
- ^ Song, Langzhou; Hobaugh, Michael R.; Shustak, Christopher; Cheley, Stephen; Bayley, Hagan; Gouaux, J. Eric (1996-12-13). "Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore". Science. 274 (5294): 1859–1865. Bibcode:1996Sci...274.1859S. doi:10.1126/science.274.5294.1859. ISSN 0036-8075. PMID 8943190. S2CID 45663016.
- ^ Desvaux, Mickaël; Hébraud, Michel (September 2006). "The protein secretion systems in Listeria : inside out bacterial virulence". FEMS Microbiology Reviews. 30 (5): 774–805. doi:10.1111/j.1574-6976.2006.00035.x. ISSN 1574-6976. PMID 16911044.
- ^ Desvaux, Mickaël; Hébraud, Michel (September 2006). "The protein secretion systems in Listeria : inside out bacterial virulence". FEMS Microbiology Reviews. 30 (5): 774–805. doi:10.1111/j.1574-6976.2006.00035.x. ISSN 1574-6976. PMID 16911044.
- ^ a b c d e Zhao, Yan; Sun, Li (4 July 2022). "Bacillus cereus cytotoxin K triggers gasdermin D-dependent pyroptosis". Cell Death Discovery. 8 (1): 1–8. doi:10.1038/s41420-022-01091-5. S2CID 256605262.
- ^ Shao, Bo-Zong; Xu, Zhe-Qi; Han, Bin-Ze; Su, Ding-Feng; Liu, Chong (2015). "NLRP3 inflammasome and its inhibitors: a review". Frontiers in Pharmacology. 6. doi:10.3389/fphar.2015.00262. ISSN 1663-9812. PMC 4633676. PMID 26594174.