# Delta endotoxins

> Mediated Wiki article. Canonical URL: https://mediated.wiki/source/Delta_endotoxins
> Markdown URL: https://mediated.wiki/source/Delta_endotoxins.md
> Source: https://en.wikipedia.org/wiki/Delta_endotoxins
> Source revision: 1355627740
> License: Creative Commons Attribution-ShareAlike 4.0 International (https://creativecommons.org/licenses/by-sa/4.0/)

Insecticide

Protein domain

Delta endotoxin, N-terminal domain crystal structure of the insecticidal bacterial del endotoxin Cry3Bb1 Bacillus thuringiensis[1] Identifiers Symbol Endotoxin_N Pfam PF03945 InterPro IPR005639 SCOP2 1dlc / SCOPe / SUPFAM TCDB 1.C.2 Available protein structures: PDB IPR005639 PF03945 (ECOD; PDBsum) AlphaFold IPR005639 PF03945

Protein domain

Delta endotoxin, middle domain Identifiers Symbol Endotoxin_M Pfam PF00555 Pfam clan CL0568 InterPro IPR015790 SCOP2 1dlc / SCOPe / SUPFAM TCDB 1.C.2 Available protein structures: PDB IPR015790 PF00555 (ECOD; PDBsum) AlphaFold IPR015790 PF00555

Protein domain

Delta endotoxin, middle domain, Cry2A and Cry18 insecticidal crystal protein cry2aa Identifiers Symbol Endotoxin_mid Pfam PF09131 InterPro IPR015214 SCOP2 1i5p / SCOPe / SUPFAM Available protein structures: PDB IPR015214 PF09131 (ECOD; PDBsum) AlphaFold IPR015214 PF09131

Protein family

Delta endotoxin, C-terminal Identifiers Symbol Endotoxin_C Pfam PF03944 Pfam clan CL0202 InterPro IPR005638 SCOP2 1dlc / SCOPe / SUPFAM TCDB 1.C.2 CDD cd04085 Available protein structures: PDB IPR005638 PF03944 (ECOD; PDBsum) AlphaFold IPR005638 PF03944

Protein family

Cytolytic delta-endotoxin Cyt1/2 Identifiers Symbol CytB Pfam PF01338 InterPro IPR001615 SCOP2 1cby / SCOPe / SUPFAM TCDB 1.C.71 Available protein structures: PDB IPR001615 PF01338 (ECOD; PDBsum) AlphaFold IPR001615 PF01338

**Delta endotoxins** (**δ-endotoxins**) are a family of [pore-forming toxins](/source/Pore-forming_toxin) produced by *[Bacillus thuringiensis](/source/Bacillus_thuringiensis)* species of bacteria. They are useful for their [insecticidal](/source/Insecticide) action and are the primary toxin produced by the genetically modified (GM) [Bt maize/corn](/source/Bt_maize) and other GM crops. During [spore](/source/Spore) formation the bacteria produce crystals of such proteins (hence the name **Cry** toxins) that are also known as **parasporal bodies**, next to the [endospores](/source/Endospore); as a result some members are known as a **parasporin**. The **Cyt** (cytolytic) toxin group is another group of delta-endotoxins formed in the cytoplasm. **VIP toxins** (vegetative insecticidal proteins) are formed at other stages of the life cycle.[2]

## Mechanism of action

When an [insect](/source/Insect) ingests these proteins, they are activated by [proteolytic cleavage](/source/Proteolytic_cleavage). The N-terminus is cleaved in all of the proteins and a [C-terminal](/source/C-terminal) extension is cleaved in some members. Once activated, the endotoxin binds to the gut [epithelium](/source/Epithelium) and causes [cell lysis](/source/Cell_lysis) by the formation of [cation-selective channels](/source/Ion_channel), which leads to death.[3][1]

For many years there was no clarity as to the relationship between [aminopeptidase N](/source/Aminopeptidase_N) and Bt toxins. Although AP-N does bind Cry proteins in vitro[4] (reviewed by Soberón et al. 2009[5] and Pigott & Ellar 2007[6]),[7] no cases of [resistance](/source/Bt_resistance) – or even reduced in vitro binding – due to AP-N structure alteration were known through 2002, and there was some doubt that the resistance mechanism was so straight forward. Indeed, Luo et al. 1997, Mohammed et al. 1996, and Zhu et al. 2000 *positively* found this to *not* occur in [Lepidoptera](/source/Lepidoptera) examples.[4] Subsequently, however Herrero et al. 2005 showed correlation between nonexpression and Bt resistance,[7] and actual resistance was found in *[Helicoverpa armigera](/source/Helicoverpa_armigera)* by Zhang et al. 2009,[7][8] in *[Ostrinia nubilalis](/source/Ostrinia_nubilalis)* by Khajuria et al. 2011, and in *[Trichoplusia ni](/source/Trichoplusia_ni)* by Baxter et al. 2011 and Tiewsiri & Wang 2011 (also all Lepidoptera).[7] There continues to be confirmation that AP-Ns do not by themselves affect resistance in some cases, possibly due to sequential binding by the toxin being required to produce its effect. In this sequence each binding step is theoretically not indispensable, but if it occurs does contribute to the final pore formation result.[8]

## Structure

The activated region of the delta toxin is composed of three distinct [structural domains](/source/Structural_domain): an [N-terminal](/source/N-terminal) [helical bundle](/source/Helical_bundle) domain ([InterPro](/source/InterPro): *[IPR005639](https://www.ebi.ac.uk/interpro/entry/IPR005639)*) involved in membrane insertion and pore formation; a [beta-sheet](/source/Beta-sheet) central domain involved in receptor binding; and a C-terminal [beta-sandwich](/source/Beta-sandwich) domain ([InterPro](/source/InterPro): *[IPR005638](https://www.ebi.ac.uk/interpro/entry/IPR005638)*) that interacts with the N-terminal domain to form a channel.[1][3]

## Types

*B. thuringiensis* encodes many proteins of the delta endotoxin family ([InterPro](/source/InterPro): *[IPR038979](https://www.ebi.ac.uk/interpro/entry/IPR038979)*), with some strains encoding multiple types simultaneously.[9] A gene mostly found on [plasmids](/source/Plasmid),[10] delta-entotoxins sometimes show up in genomes of other species, albeit at a lower proportion than those found in *B. thuringiensis*.[11] The gene names look like Cry3Bb, which in this case indicates a Cry toxin of superfamily 3 family B subfamily b.[12]

*Cry* proteins that are interesting to cancer research are listed under a parasporin (PS) nomenclature in addition to the Cry nomenclature. They do not kill insects, but instead kill [leukemia](/source/Leukemia) cells.[13][14][15] The Cyt toxins tend to form their own group distinct from Cry toxins.[16] Not all *Cry* — crystal-form — toxins directly share a common root.[17] Examples of non-three-domain toxins that nevertheless have a *Cry* name include [Cry34/35Ab1](/source/Cry34Ab1) and related beta-sandwich binary (*Bin*-like) toxins, [Cry6Aa](/source/Cry6Aa), and many beta-sandwich parasporins.[18]

Specific delta-endotoxins that have been inserted with [genetic engineering](/source/Genetic_engineering) include Cry3Bb1 found in [MON 863](/source/MON_863) and Cry1Ab found in [MON 810](/source/MON_810), both of which are [maize/corn cultivars](https://en.wikipedia.org/w/index.php?title=Maize_cultivar&action=edit&redlink=1). Cry3Bb1 is particularly useful because it kills Coleopteran insects such as the [corn rootworm](/source/Corn_rootworm), an activity not seen in other Cry proteins.[1] Other common toxins include [Cry2Ab](/source/Cry2Ab) and [Cry1F](/source/Cry1F) in [cotton](/source/Transgenic_cotton) and [maize/corn](/source/Transgenic_maize).[19] In addition, [Cry1Ac](/source/Cry1Ac) is effective as a vaccine adjuvant in humans.[20]

Some insect populations have started to develop resistance towards delta endotoxin, with five resistant species found as of 2013. Plants with two kinds of delta endotoxins tend to make resistance happen slower, as the insects have to evolve to overcome both toxins at once. Planting non-Bt plants with the resistant plants will reduce the selection pressure for developing the toxin. Finally, two-toxin plants should not be planted with one-toxin plants, as one-toxin plants act as a stepping stone for adaption in this case.[19]

## References

1. ^ [***a***](#cite_ref-Galitsky_2001_1-0) [***b***](#cite_ref-Galitsky_2001_1-1) [***c***](#cite_ref-Galitsky_2001_1-2) [***d***](#cite_ref-Galitsky_2001_1-3) Galitsky N, Cody V, Wojtczak A, Ghosh D, Luft JR, Pangborn W, English L (August 2001). "Structure of the insecticidal bacterial delta-endotoxin Cry3Bb1 of *Bacillus thuringiensis*". *Acta Crystallographica. Section D, Biological Crystallography*. **57** (Pt 8): 1101–1109. [Bibcode](/source/Bibcode_(identifier)):[2001AcCrD..57.1101G](https://ui.adsabs.harvard.edu/abs/2001AcCrD..57.1101G). [doi](/source/Doi_(identifier)):[10.1107/S0907444901008186](https://doi.org/10.1107%2FS0907444901008186). [PMID](/source/PMID_(identifier)) [11468393](https://pubmed.ncbi.nlm.nih.gov/11468393).

1. **[^](#cite_ref-2)** Roger Hull; et al. (2021). "Risk assessment and management—Environment". *Genetically Modified Plants* (second ed.). Upon sporulation, *B. thuringiesis* forms proteinaceous insecticidal δ-endotoxins either in crystals (Cry toxins) or cytoplasmically (Cyt toxins), which are encoded by cry or cyt genes, respectively. When insects ingest toxin crystals, the enzymes in their digestive tract cause the toxin to become activated. The toxin binds to the insect's gut membranes, forming a pore that results in swelling, cell lysis, and eventually killing the insect. *B. thuringiesis* also produces insecticidal proteins at other stages in its lifecycle, specifically the vegetative insecticidal proteins (VIPs).

1. ^ [***a***](#cite_ref-Grochulski_1995_3-0) [***b***](#cite_ref-Grochulski_1995_3-1) Grochulski P, Masson L, Borisova S, Pusztai-Carey M, Schwartz JL, Brousseau R, Cygler M (December 1995). "*Bacillus thuringiensis* CryIA(a) insecticidal toxin: crystal structure and channel formation". *Journal of Molecular Biology*. **254** (3): 447–464. [doi](/source/Doi_(identifier)):[10.1006/jmbi.1995.0630](https://doi.org/10.1006%2Fjmbi.1995.0630). [PMID](/source/PMID_(identifier)) [7490762](https://pubmed.ncbi.nlm.nih.gov/7490762).

1. ^ [***a***](#cite_ref-Ferre-Rie-2002_4-0) [***b***](#cite_ref-Ferre-Rie-2002_4-1) Ferré J, Van Rie J (2002). "Biochemistry and genetics of insect resistance to *Bacillus thuringiensis*". *Annual Review of Entomology*. **47** (1). [Annual Reviews](/source/Annual_Reviews_(publisher)): 501–533. [doi](/source/Doi_(identifier)):[10.1146/annurev.ento.47.091201.145234](https://doi.org/10.1146%2Fannurev.ento.47.091201.145234). [PMID](/source/PMID_(identifier)) [11729083](https://pubmed.ncbi.nlm.nih.gov/11729083).

1. **[^](#cite_ref-Soberon-et-al-2009_5-0)** Soberón M, Gill SS, Bravo A (April 2009). ["Signaling versus punching hole: How do *Bacillus thuringiensis* toxins kill insect midgut cells?"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11131463). *Cellular and Molecular Life Sciences*. **66** (8). [Springer](/source/Springer_Science%2BBusiness_Media): 1337–1349. [doi](/source/Doi_(identifier)):[10.1007/s00018-008-8330-9](https://doi.org/10.1007%2Fs00018-008-8330-9). [PMC](/source/PMC_(identifier)) [11131463](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11131463). [PMID](/source/PMID_(identifier)) [19132293](https://pubmed.ncbi.nlm.nih.gov/19132293). [S2CID](/source/S2CID_(identifier)) [5928827](https://api.semanticscholar.org/CorpusID:5928827).

1. **[^](#cite_ref-Pigott-Ellar-2007_6-0)** Pigott CR, Ellar DJ (June 2007). ["Role of receptors in *Bacillus thuringiensis* crystal toxin activity"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1899880). *Microbiology and Molecular Biology Reviews*. **71** (2). [American Society for Microbiology](/source/American_Society_for_Microbiology): 255–281. [doi](/source/Doi_(identifier)):[10.1128/mmbr.00034-06](https://doi.org/10.1128%2Fmmbr.00034-06). [PMC](/source/PMC_(identifier)) [1899880](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1899880). [PMID](/source/PMID_(identifier)) [17554045](https://pubmed.ncbi.nlm.nih.gov/17554045). [S2CID](/source/S2CID_(identifier)) [13982571](https://api.semanticscholar.org/CorpusID:13982571).

1. ^ [***a***](#cite_ref-Lopez-et-al-2013_7-0) [***b***](#cite_ref-Lopez-et-al-2013_7-1) [***c***](#cite_ref-Lopez-et-al-2013_7-2) [***d***](#cite_ref-Lopez-et-al-2013_7-3) Pardo-López L, Soberón M, Bravo A (January 2013). ["*Bacillus thuringiensis* insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection"](https://doi.org/10.1111%2Fj.1574-6976.2012.00341.x). *FEMS Microbiology Reviews*. **37** (1). [Federation of European Microbiological Societies](/source/Federation_of_European_Microbiological_Societies) ([OUP](/source/Oxford_University_Press)): 3–22. [doi](/source/Doi_(identifier)):[10.1111/j.1574-6976.2012.00341.x](https://doi.org/10.1111%2Fj.1574-6976.2012.00341.x). [PMID](/source/PMID_(identifier)) [22540421](https://pubmed.ncbi.nlm.nih.gov/22540421).

1. ^ [***a***](#cite_ref-Vachon-et-al-2012_8-0) [***b***](#cite_ref-Vachon-et-al-2012_8-1) Vachon V, Laprade R, Schwartz JL (September 2012). "Current models of the mode of action of *Bacillus thuringiensis* insecticidal crystal proteins: a critical review". *Journal of Invertebrate Pathology*. **111** (1). [Academic Press](/source/Academic_Press) ([Elsevier](/source/Elsevier)): 1–12. [Bibcode](/source/Bibcode_(identifier)):[2012JInvP.111....1V](https://ui.adsabs.harvard.edu/abs/2012JInvP.111....1V). [doi](/source/Doi_(identifier)):[10.1016/j.jip.2012.05.001](https://doi.org/10.1016%2Fj.jip.2012.05.001). [PMID](/source/PMID_(identifier)) [22617276](https://pubmed.ncbi.nlm.nih.gov/22617276).

1. **[^](#cite_ref-9)** ["Pesticidal crystal protein (IPR038979)"](http://www.ebi.ac.uk/interpro/entry/IPR038979/). *InterPro*. Retrieved 12 April 2019.

1. **[^](#cite_ref-Dean_1984_10-0)** Dean DH (1984). ["Biochemical genetics of the bacterial insect-control agent *Bacillus thuringiensis*: basic principles and prospects for genetic engineering"](https://doi.org/10.1080%2F02648725.1984.10647804). *Biotechnology & Genetic Engineering Reviews*. **2**: 341–363. [doi](/source/Doi_(identifier)):[10.1080/02648725.1984.10647804](https://doi.org/10.1080%2F02648725.1984.10647804). [PMID](/source/PMID_(identifier)) [6443645](https://pubmed.ncbi.nlm.nih.gov/6443645).

1. **[^](#cite_ref-11)** ["Species: Pesticidal crystal protein (IPR038979)"](http://www.ebi.ac.uk/interpro/entry/IPR038979/taxonomy). *InterPro*.

1. **[^](#cite_ref-12)** ["*Bacillus thuringiensis* Toxin Nomenclature"](http://www.btnomenclature.info/). *Bt toxin specificity database*. Retrieved 12 April 2019.

1. **[^](#cite_ref-13)** Mizuki E, Park YS, Saitoh H, Yamashita S, Akao T, Higuchi K, Ohba M (July 2000). ["Parasporin, a human leukemic cell-recognizing parasporal protein of *Bacillus thuringiensis*"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC95925). *Clinical and Diagnostic Laboratory Immunology*. **7** (4): 625–634. [doi](/source/Doi_(identifier)):[10.1128/CDLI.7.4.625-634.2000](https://doi.org/10.1128%2FCDLI.7.4.625-634.2000). [PMC](/source/PMC_(identifier)) [95925](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC95925). [PMID](/source/PMID_(identifier)) [10882663](https://pubmed.ncbi.nlm.nih.gov/10882663).

1. **[^](#cite_ref-14)** Ohba M, Mizuki E, Uemori A (January 2009). ["Parasporin, a new anticancer protein group from *Bacillus thuringiensis*"](http://ar.iiarjournals.org/cgi/pmidlookup?view=long&pmid=19331182). *Anticancer Research*. **29** (1): 427–433. [PMID](/source/PMID_(identifier)) [19331182](https://pubmed.ncbi.nlm.nih.gov/19331182).

1. **[^](#cite_ref-15)** ["List of Parasporins"](http://parasporin.fitc.pref.fukuoka.jp/list.html). *Committee of Parasporin Classification and Nomenclature*. Accessed Jan 4, 2013

1. **[^](#cite_ref-16)** Crickmore N. ["Other Cry Sequences"](http://www.lifesci.susx.ac.uk/home/Neil_Crickmore/Bt/othercry.pdf) (PDF). Retrieved 12 April 2019.

1. **[^](#cite_ref-17)** Crickmore N, Zeigler DR, Feitelson J, Schnepf E, Van Rie J, Lereclus D, et al. (September 1998). ["Revision of the nomenclature for the *Bacillus thuringiensis* pesticidal crystal proteins"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC98935). *Microbiology and Molecular Biology Reviews*. **62** (3): 807–813. [doi](/source/Doi_(identifier)):[10.1128/MMBR.62.3.807-813.1998](https://doi.org/10.1128%2FMMBR.62.3.807-813.1998). [PMC](/source/PMC_(identifier)) [98935](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC98935). [PMID](/source/PMID_(identifier)) [9729610](https://pubmed.ncbi.nlm.nih.gov/9729610).

1. **[^](#cite_ref-Kelker2014_18-0)** Kelker MS, Berry C, Evans SL, Pai R, McCaskill DG, Wang NX, et al. (2014-11-12). ["Structural and biophysical characterization of *Bacillus thuringiensis* insecticidal proteins Cry34Ab1 and Cry35Ab1"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4229197). *PLOS ONE*. **9** (11) e112555. [Bibcode](/source/Bibcode_(identifier)):[2014PLoSO...9k2555K](https://ui.adsabs.harvard.edu/abs/2014PLoSO...9k2555K). [doi](/source/Doi_(identifier)):[10.1371/journal.pone.0112555](https://doi.org/10.1371%2Fjournal.pone.0112555). [PMC](/source/PMC_(identifier)) [4229197](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4229197). [PMID](/source/PMID_(identifier)) [25390338](https://pubmed.ncbi.nlm.nih.gov/25390338).

1. ^ [***a***](#cite_ref-Tabashnik_2013_19-0) [***b***](#cite_ref-Tabashnik_2013_19-1) Tabashnik BE, Brévault T, Carrière Y (June 2013). "Insect resistance to Bt crops: lessons from the first billion acres". *Nature Biotechnology*. **31** (6): 510–521. [doi](/source/Doi_(identifier)):[10.1038/nbt.2597](https://doi.org/10.1038%2Fnbt.2597). [PMID](/source/PMID_(identifier)) [23752438](https://pubmed.ncbi.nlm.nih.gov/23752438). [S2CID](/source/S2CID_(identifier)) [205278530](https://api.semanticscholar.org/CorpusID:205278530).

1. **[^](#cite_ref-Rodriguez-Monroy2010_20-0)** Rodriguez-Monroy MA, Moreno-Fierros L (March 2010). ["Striking activation of NALT and nasal passages lymphocytes induced by intranasal immunization with Cry1Ac protoxin"](https://doi.org/10.1111%2Fj.1365-3083.2009.02358.x). *Scandinavian Journal of Immunology*. **71** (3): 159–168. [doi](/source/Doi_(identifier)):[10.1111/j.1365-3083.2009.02358.x](https://doi.org/10.1111%2Fj.1365-3083.2009.02358.x). [PMID](/source/PMID_(identifier)) [20415781](https://pubmed.ncbi.nlm.nih.gov/20415781).

## Further reading

- Bravo A, Gill SS, Soberón M (March 2007). ["Mode of action of *Bacillus thuringiensis* Cry and Cyt toxins and their potential for insect control"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1857359). *Toxicon*. **49** (4): 423–435. [Bibcode](/source/Bibcode_(identifier)):[2007Txcn...49..423B](https://ui.adsabs.harvard.edu/abs/2007Txcn...49..423B). [doi](/source/Doi_(identifier)):[10.1016/j.toxicon.2006.11.022](https://doi.org/10.1016%2Fj.toxicon.2006.11.022). [PMC](/source/PMC_(identifier)) [1857359](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1857359). [PMID](/source/PMID_(identifier)) [17198720](https://pubmed.ncbi.nlm.nih.gov/17198720).

- Pigott CR, Ellar DJ (June 2007). ["Role of receptors in *Bacillus thuringiensis* crystal toxin activity"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1899880). *Microbiology and Molecular Biology Reviews*. **71** (2): 255–281. [doi](/source/Doi_(identifier)):[10.1128/MMBR.00034-06](https://doi.org/10.1128%2FMMBR.00034-06). [PMC](/source/PMC_(identifier)) [1899880](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1899880). [PMID](/source/PMID_(identifier)) [17554045](https://pubmed.ncbi.nlm.nih.gov/17554045).

- Palma L, Muñoz D, Berry C, Murillo J, Caballero P (December 2014). ["*Bacillus thuringiensis* toxins: an overview of their biocidal activity"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4280536). *Toxins*. **6** (12): 3296–3325. [doi](/source/Doi_(identifier)):[10.3390/toxins6123296](https://doi.org/10.3390%2Ftoxins6123296). [PMC](/source/PMC_(identifier)) [4280536](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4280536). [PMID](/source/PMID_(identifier)) [25514092](https://pubmed.ncbi.nlm.nih.gov/25514092).

## External links

- [Cry3Bb1](https://web.archive.org/web/20040908235342/http://www.epa.gov/oppbppd1/biopesticides/ingredients/factsheets/factsheet_006484.htm) at the *[United States Environmental Protection Agency](/source/United_States_Environmental_Protection_Agency)*

v t e Toxins cardiotoxin cytotoxin enterotoxin hemotoxin hepatotoxin neurotoxin phototoxin Bacterial toxins Exotoxin Gram positive Bacilli Clostridium: tetani Tetanospasmin Tetanolysin perfringens Alpha toxin Enterotoxin difficile A B botulinum Botox Other: Anthrax toxin Listeriolysin O Cocci Streptolysin Leukocidin Panton–Valentine leukocidin Staphylococcus Staphylococcus aureus alpha/beta/delta Exfoliatin Toxic shock syndrome toxin Staphylococcal Enterotoxin B (SEB) Actinomycetota Cord factor Diphtheria toxin Gram negative Shiga toxin/Verotoxin E. coli heat-stable enterotoxin Cholera toxin/Heat-labile enterotoxin Pertussis toxin Pseudomonas exotoxin Extracellular adenylate cyclase Mechanisms type I Superantigen type II Pore-forming toxin type III AB toxin/AB5 Endotoxin Lipopolysaccharide Lipid A Bacillus thuringiensis delta endotoxin Cry1Ac Cry3Bb1 Other B. thuringiensis toxins Cry6Aa Cry34Ab1 Virulence factor Clumping factor A Fibronectin binding protein A Mycotoxins Aflatoxin Amatoxin (alpha-amanitin, beta-amanitin, gamma-amanitin, epsilon-amanitin, Amanullin, Amanullinic acid, Amaninamide, Amanin, Proamanullin) beta-Nitropropionic acid Citrinin Cytochalasin Ergotamine Fumonisin (Fumonisin B1, Fumonisin B2, Fumonisin B3, Fumonisin B4) Gliotoxin Ibotenic acid Lolitrem B Muscarine Muscimol Orellanine Ochratoxin Patulin Phallotoxin (Phalloidin) Satratoxin-H Sterigmatocystin T-2 mycotoxin Trichothecene Vomitoxin Zeranol Zearalenone Plant toxins Amygdalin Anisatin Antiarin Brucine Chaconine Cicutoxin Coniine Daphnin Delphinine Divicine Djenkolic acid Falcarinol Gossypol Helenalin Ledol Linamarin Lotaustralin Mimosine Oenanthotoxin Oleandrin Persin Protoanemonin Pseudaconitine Retronecine Resiniferatoxin Scopolamine Solamargine Solanidine Solanine Solasodamine Solasodine Solasonine Solauricidine Solauricine Strychnine Swainsonine Tagetitoxin Tinyatoxin Tomatine Toxalbumin Abrin Ricin Tutin Invertebrate toxins Scorpion: Androctonus australis hector insect toxin Charybdotoxin Maurotoxin Agitoxin Margatoxin Slotoxin Scyllatoxin Hefutoxin HgeTx1 HsTx1 Kaliotoxin Lq2 Birtoxin Bestoxin BmKAEP Phaiodotoxin Imperatoxin Pi3 Spider: Latrotoxin Alpha-latrotoxin CSTX Cupiennins PhTx3 Stromatoxin Vanillotoxin Huwentoxin Mollusca: Conotoxin Eledoisin Onchidal Saxitoxin Tetrodotoxin Vertebrate toxins Fish: Ciguatoxin Tetrodotoxin Amphibian: (+)-Allopumiliotoxin 267A Batrachotoxin Bufotoxins Arenobufagin Bufotalin Bufotenin Cinobufagin Marinobufagin Epibatidine Histrionicotoxin Pumiliotoxin 251D Samandarin Samandaridine Tarichatoxin Zetekitoxin AB Reptile/ Snake venom: Bungarotoxin α-Bungarotoxin β-Bungarotoxin κ-Bungarotoxin Calciseptine Taicatoxin Calcicludine Cardiotoxin III note: some toxins are produced by lower species and pass through intermediate species Category

This article incorporates text from the public domain [Pfam](/source/Pfam) and [InterPro](/source/InterPro): [IPR015790](https://www.ebi.ac.uk/interpro/entry/IPR015790)

---
Adapted from the Wikipedia article [Delta endotoxins](https://en.wikipedia.org/wiki/Delta_endotoxins) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Delta_endotoxins?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.