Acta Scientific Microbiology

Review Article Volume 7 Issue 6

Biocidal Activity of the Bacillus thuringiensis 3D Cry Toxins, Molecular Crosstalk at the Insect Midgut with Implication in Insect Resistance Development

Gloria G Guerrero M*

Universidad Autónoma de Zacatecas, Campus II, Unidad Académica de Ciencias Biológicas, Zacatecas, Zac, México

*Corresponding Author: Gloria G Guerrero M, Universidad Autónoma de Zacatecas, Campus II, Unidad Académica de Ciencias Biológicas, Zacatecas, Zac, México.

Received: March 13, 2024; Published: May 26, 2024


Bacillus thuringiensis (Bt) is a Gram-positive bacteria characterized by the production of parasporal crystalline proteins toxic to a wide range of insect orders. Cry toxins targeted pests of crops of economic importance. Nowadays, around 600 genes encode crystalline proteins with a range of molecular weight of 50 to 130 kDa. Cry proteins are comprised of three domains and their tridimensional structures have been elucidated by X-rays. Their mode of action remains to be defined and understood. However, most of these proteins follow a basic program for their biocidal activity. A critical step in the mode of action of the 3D Cry toxins is the specific binding to the receptors present in the midgut epithelial. These receptors are determinants of the specificity and susceptibility of targeted insects. Among them are the classical glycosyl phosphate inositol (GPI)-anchored membrane receptors, such as N-aminopeptidase, Alkaline Phosphatase, and classical epithelial cadherins DE-Cadherins. The second group of binding proteins includes ABC transporters, V-ATPase, and other lipid rafts-associated proteins. The hallmark of this molecular crosstalk at the insect midgut is that it is conserved between different Cry 3D toxins with diverse targets of insects. Moreover, the receptors in this tissue are also common resulting in a common mode of action that comprises the insect response to entomopathogens, which potentially can guide a design of safe and integrated management of crop pests.

Keywords: Crystalline Proteins (Cry); BTR1 Receptors; REPAT; G Proteins; PKA; ERK; MAPK p38


  1. Höfte H and Whiteley HR. “Insecticidal crystal proteins of Bacillus thuringiensis”. Microbiological Review 53 (1989): 242-255.
  2. Ibrahim M., et al. “Bacillus thuringiensis a genomic and proteomics perspective”. Bioengineered Bugs 1 (2019): 31-50.
  3. Estruch JJ., et al. “Vip3A, a novel Bacillus thuringiensis vegetative insecticidal protein with a wide spectrum of activities against Lepidopteran insects”. Proceedings of the National Academy of Sciences of the United States of America 93 (1996): 5389-5394.
  4. Bravo A., et al. “Bacillus thuringiensis mechanisms and use”. In: Gilbert, LI.; Iatrou, K.; Gill, SS., editors. Comprehensive Molecular Insect Science. Elsevier BV; (2005): 175-206.
  5. Bel Y., et al. “Comprehensive analysis of gene expression profiles of the beet armyworm larvae Spodoptera exigua (Lepidoptera Noctuidae) challenged with Bacillus thuringiensis Vip3Aa toxin”. PLoS One 8 (2013): e81927.
  6. Verma P., et al. “Pore-formingtoxins in infection and immunity”. Biochemical Society Transactions 49 (2021): 455-465.
  7. Ulhuq FR and Mariano G. “Bacterialpore-forming toxins”. Microbiology 168 (2022):
  8. Cramer WA., et al. “On mechanisms of colicinimport: the outer membrane quandary”. Biochemical Journal 475 (2018): 3903-3915.
  9. Budiardjo SJ., et al. “ColicinE1 opens its hinge to plug TolC”. Elife11 (2022): e73297.
  10. Lycke N., et al. “ADP-ribosylating enterotoxins as vaccine adjuvants”. Current Opinion on Pharmacology 41 (2018): 42-51.
  11. Spangler BD. “Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin”. Microbiology Review56 (1992): 622-647.
  12. Escartín-Gutiérrez JR., et al. “Transcriptional Activation of a Pro-Inflammatory Response (NF-κB, AP-1, IL-1β) by the Vibrio cholerae Cytotoxin (VCC) Monomer through the MAPK Signaling Pathway in the THP-1 Human Macrophage Cell Line”. International Journal of Molecular Sciences 24 (2023):
  13. Lacomel CJ., et al. “Branching out the aerolysin, ETX/MTX-2 and Toxin_10 family of poreforming proteins”. Journal of Invertebrate Pathology 186 (2021):
  14. Thapa R and Keyel PA. “Patch repair protects cells from the small pore-formingtoxin aerolysin”. Journal of Cell Science 136 (2023):
  15. Bravo A. “Phylogenetic relationships of Bacillus thuringiensis d-endotoxin family proteins and their functional domains”. Journal of Bacteriology 179 (1997): 2793-2801.
  16. De Maagd RA., et al. “Structure, diversity, and evolution of proteins toxins from spore-forming entomopathogenic bacteria”. Annual Review of Genetics 37 (2003): 409-433.
  17. Bravo A., et al. “Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect control”. Toxicon 49 (2007): 423-435.
  18. Jurat-Fuentes JL., et al. “Specificity determinants for Cryinsecticidal proteins: Insights from their mode of action”. Journal of Invertebrate Pathology 142 (2017): 5-10.
  19. Bel Y., et al. “Bacillus thuringiensis toxins: functional characterization and mechanism of action”. Toxins (Basel) 12 (2020):
  20. Grochulski P., et al. “Bacillus thuringiensis CryIAa insecticidal toxin: crystal structure and channel formation”. Journal of Molecular Biology 254 (1995): 447-464.
  21. Derbyshire DJ., et al. “Crystallization of the Bacillus thuringiensis toxin Cry2Ac and its complex with the receptor ligand N-acetylgalactosamine”. Acta Crystallography Section D 57 (2001): 1938-1944.
  22. Morse RJ., et al. “Structure of Cry2Aa suggests an unexpected receptor binding epitope”. Structure 9 (2001): 409-417.
  23. Cohen S., et al. “High-resolution crystal of activated Cyt2Ba monomer from Bacillus thuringiensis var israelensis”. Journal of Molecular Biology 380 (2008): 820-827.
  24. Li J., et al. “Crystal structure of insecticidal d-endotoxin from Bacillus thuringiensis at 2.5Å resolution”. Nature 353 (1991): 815-821.
  25. Galitsky N., et al. “Structure of the insecticidal bacterial d-endotoxin Cry3Bb1 of Bacillus thuringiensis”. Acta Crystal D 57 (2001): 1101-1109.
  26. Boonserm P., et al. “Structure of the functional form of the mosquito larvicidal Cry4Aa toxin from Bacillus thuringiensis at a 2.8-Å resolution”. Journal of Bacteriology 188 (2006): 3391-3401.
  27. Boonserm P., et al. “Crystal Structure of the Mosquito larvicidal Toxin Cry4Ba and Its biological implications”. Journal of Molecular Biology 348 (2005): 363-382.
  28. Pardo-López L., et al. “Bacillus thuringiensis insecticidal thee-domain Cry toxins: mode of action, insect resistance and consequences for crop protection”. FEMS Microbiology Review 37 (2013): 3-22.
  29. Burton SL., et al. “N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognized by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin”. Journal of Molecular Biology 287 (1999): 1011-1022.
  30. Walters FS., et al. “Lepidopteran-active variable-region sequence imparts coleopteran activity in eCry3.Cry1Ab, an engineered Bacillus thuringiensis hybrid insecticidal protein”. Applied and Environmental Microbiology 76 (2010): 3082-3088.
  31. Xiao Y and Wu K. “Recent progress on the interaction between insects and Bacillus thuringiensis crops”. Philosophical Transactions of the Royal Society B 374 (2019):
  32. Jiang H., et al. “Immunity in lepidopteran insects”. Advances in Experimental Medicine and Biology 708 (2010): 181-204.
  33. Castagnola A and Jurat-Fuentes JL. “Intestinal regeneration as an insect resistance mechanism to entomopathogenic bacteria”. Current Opinion in Insect Science 15 (2016): 110.
  34. Herrero S., et al. “Insect REPAT, an new family of proteins induced by bacterial toxins and baculovirus infection in Spodoptera exigua”. Biochem Mol Biol. 37 (2007): 1109-18.
  35. Navarro-Cerrillo G., et al. “Functional interactions between members of the REPATfamily of insect pathogen-induced proteins”. Insect Molecular Biology 21 (2012): 335-342.
  36. Zhou CY., et al. “Identification of MBF2 family genesin Bombyx mori and their expression in different tissues and stages and in response to Bacillus Bomby septicus infection and starvation”. Insect Science 23 (2016): 502-512.
  37. Pinos D., et al. “Response Mechanisms of Invertebrates to Bacillus thuringiensis and Its Pesticidal Proteins”. Microbiology and Molecular Biology Reviews 85 (2021): e00007-20.
  38. Knowles BH., et al. “Colloid-osmotic lysis is a general feature of the mechanism of action of Bacillus thuringiensis delta-endotoxins with different insect specificity”. BBA Gen. Subj. 924 (1987): 509-518.
  39. Zhang X., et al. “Cytotoxicity of Bacillus thuringiensis Cry1Ab toxin depends on specific binding of the toxin to the cadherin receptor BT-R1 expressed in insect cells”. Cell Death Dier 12 (2005): 1407-1416.
  40. Khorramnejad A., et al. “Study of the Bacillus thuringiensis Cry1Ia protein oligomerization promoted by midgut brush border membrane vesicles of lepidopteran and coleopteran insects, or cultured insect cells”. Toxins (Basel) 12 (2020):
  41. Liu L., et al. “Which Is Stronger? A Continuing Battle between Cry Toxins and Insects”. Frontiers in Microbiology 12 (2021): 1-13.
  42. Endo H., et al. “Extracellular loop structures in silk-worm ABCC transporters determine their specificities for Bacillus thuringiensis Cry toxins”. Journal of Biological Chemistry 293 (2018): 8569-8577.
  43. Palma L., et al. “Bacillus thuringiensis toxins: an overview of their biocidal activity”. Toxins (Basel). 6 (2014): 3296-3325.
  44. Jiménez-Juárez A., et al. “Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae”. Journal of Biological Chemistry 282 (2007): 21222-21229.
  45. Fu Y., et al. “C-di-GMP regulates various phenotypes and insecticidal activity of Gram-positive Bacillus thuringiensis”. Frontiers in Microbiology 9 (2018): 45.
  46. Zhang XB., et al. “A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis”. Proceedings of the National Academy of Sciences of the United States of America 103 (2006): 9897-9902.
  47. Xu C., et al. “Structural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxins”. Toxins (Basel) 6 (2014): 2732-2770.
  48. Zalem D., et al. “Biochemical and structural characterization of the novel sialic acid-binding site of Escherichia coli heat-labile enterotoxin LT-IIb”. Biochemical Journal 473 (2016): 3923-3936.
  49. Berenson CS., et al. “Ganglioside-binding specificities of coli enterotoxin LT-IIc: Importance of long-chain fatty acyl ceramide”. Glycobiology 23 (2013): 23-31.
  50. Liu L., et al. “The defined toxin-binding region of the cadherin G-protein coupled receptor Bt-R1 for the active Cry1Ab of Bacillus thuringiensis”. Journal of Proteom Bioinform 11 (2018): 201-210.
  51. Huffman DL., et al. “Mitogen-activated protein kinase pathways defend against bacterial pore forming toxins”. Proceedings of the National Academy of Sciences of the United States of America 101 (2004): 10995-11000.
  52. Bischof LJ., et al. “Activation of the unfolded protein response is required for defenses against bacterial pore-forming toxin in vivo”. PLoS Pathogens 4 (2008): e1000176.
  53. Rubio-Infante N., et al. “The Macrophage Activation Induced by Bacillus thuringiensis Cry1Ac Protoxin Involves ERK1/2 and p38 Pathways and the Interaction with Cell-Surface-HSP70”. Journal of Cell Biochemistry 119 (2018): 580-598.
  54. Cancino-Rodezno A., et al. “The mitogen-activated protein kinase p38 p.thway is involved in insect defense against Cry toxins from Bacillus thuringiensis”. Insect Biochemistry and Molecular Biology 40 (2010): 58-63.
  55. Zhang H., et al. “Intra-and-extracellular domains of the Helicoverpa armiguera cadherin mediate Cry1Ac cytotoxicity”. Insect Biochemistry and Molecular Biology 86 (2017): 41-49.
  56. Jurat-Fuentes JL., et al. “The HevCaLP protein mediates binding specificity of the Cry1A class of Bacillus thuringiensis toxins in Heliothis virescens”. Biochemistry 43 (2004): 14299-14305.
  57. Pigott CR and Ellar DJ. “Role of receptors in Bacillus thuringiensis crystal toxin activity”. Microbiology and Molecular Biology Reviews 71 (2007): 255-281.
  58. Fabrick J., et al. “A novel Tenebrio molitor cadherin is a functional receptor for Bacillus thuringiensis Cry3Aa toxin”. Journal of Biological Chemistry 284 (2009): 18401-18410.
  59. Adang MJ., et al. “Diversity of Bacillus thuringiensis crystal toxins and mechanism of action”. Advances in Insect Physiology 47 (2014): 39-87.
  60. Arenas I., et al. “Role of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxin”. Journal of Biological Chemistry 285 (2010): 12497-12503.
  61. Xie R., et al. “Single amino acid mutations in the cadherin receptor from Heliothis virescens affect its toxin binding ability to Cry1A toxins”. Journal of Biological Chemistry 280 (2005): 8416-8425.
  62. Atsumi S., et al. “Location of the Bombyx mori 175kDa cadherin-like protein-binding site on Bacillus thuringiensis Cry1Aa toxin”. FEBS Journal 275 (2008): 4913-4926.
  63. Du L., et al. “Cadherin CsCad plays differential functional roles in Cry1Ab and Cry1C intoxication in Chilo suppressalis”. Science Report 9 (2019): 8507-8522.
  64. Pacheco S., et al. “Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation”. Peptides 30 (2009a): 583-588.
  65. Chen J., et al. “Aedes aegypti cadherin serves as a putative receptor of the Cry11Aa toxin from Bacillus thuringiensis var israelensis”. Biochemical Journal 424 (2009b): 191-200.
  66. Chen J., et al. “Identification and characterization of Aedes aegypti aminopeptidase N as a putative receptor of Bacillus thuringiensis Cry11A toxin”. Insect Biochemistry and Molecular Biology 39 (2009a): 688-696.
  67. Likitvivatanavong S., et al. “Cadherin, alkaline phosphatase and aminopeptidase N as receptors of Cry11Ba toxin from Bacillus thuringiensis jegathesan in Aedes aegypti”. Applied and Environmental Microbiology 77 (2011): 24-31.
  68. Fernández LE., et al. “Cry11Aa toxin from Bacillus thuringiensis binds its receptor in Aedes aegypti mosquito larvae through loop a-8of domain II”. FEBS Letter 579 (2005): 3508-3514.
  69. Lu Q., et al. “A fragment of cadherin-like protein enhances Bacillus thuringiensis Cry1B and Cry1C toxicity to Spodoptera exigua (Lepidoptera: Noctuidae)”. Journal of Integrative Agriculture 11 (2012): 628-638.
  70. Contreras E., et al. “Sodium solute symporter and cadherin proteins act as Bacillus thuringiensis Cry3Ba toxin functional receptor in Tribolium castancum”. Journal of Biological Chemistry 288 (2013): 18013-18021.
  71. Khasdan V., et al. “Toxicity and synergism in transgenic Escherichia coli expressing four genes from Bacillus thuringiensis subsp israeliensis”. Environment Microbiology 3 (2001): 798-806.
  72. Cantón PE., et al. “Binding of Bacillus thuringiensis israelensis Cry4Ba to Cyt1Aa has an important role in synergism”. Peptides 32 (2011): 595-600.
  73. Fabrick J., et al. “A novel Tenebrio molitor cadherin is a functional receptor for Bacillus thuringiensis Cry3A toxin”. Journal of Biological Chemistry 284 (2009): 18401-18410.
  74. Martins ES., et al. “Midgut GPI-anchored proteins with alkaline phosphatase activity from the cotton boll weevil (Anthonomus grandis) are putative receptors for the Cry1B protein of Bacillus thuringiensis”. Insect Biochemistry and Molecular Biology 40 (2010): 138-145.
  75. Nollet F., et al. “Phylogenetic analysis of the cadherin superfamily allows identification of six major subfamilies besides several solitary members”. Journal of Molecular Biology299 (2009): 551-572.
  76. Shapiro L and Weiss WI. “Structure and biochemistry of cadherins and catenin”. Cold Spring Harbor Perspectives in Biology 1 (2009): a003053.
  77. Tepass U and Harris KP. “Adherens junctions in Drosophila retinal morphogenesis”. Trends Cell Biology 17 (2007): 26-35.
  78. Chen J., et al. “Aedes cadherin receptor that mediates Bacillus thuringiensis Cry11A toxicity is essential for mosquito development”. PLOS Neglected Tropical Diseases 14 (2020):
  79. Lefebre JL., et al. “Protocadherins mediate dendritic self-avoidance in the mammalian nervous system”. Nature 488 (2012): 517-521.
  80. Sasaki M., et al. “Evolutionary origin of type IV classical cadherins in arthropods”. BMC Evolutionary Biology 17 (2017): 142-165.
  81. Jin W., et al. “Cadherin Protein is Involved in the Action of Bacillus thuringiensis Cry1Ac toxin in Ostrinia furnacalis”. Toxins 13 (2021): 658-672.
  82. Pandian NG., et al. “Bombyx mori midgut membrane protein P252 which binds to Cry1A of Bacillus thuringiensis is a chlorophyllide binding protein and its resulting complex has antimicrobial activity”. Applied and Environmental Microbiology 74 (2008): 1324-1331.
  83. Bayyareddy K., et al. “Proteomic identification of Bacillus thuringiensis israelensis toxin Cry4Ba binding proteins in midgut membranes from Aedes (Stegomyia) aegypti Linnaeus (Diptera, Culicidae) larvae”. Insect Biochemistry and Molecular Biology 39 (2009): 279-286.
  84. Griffitts JS., et al. “Glycolipids as receptors for Bacillus thuringiensis crystal toxin”. Science 307 (2005): 922-992.
  85. Fernández-Luna MT., et al. “An alpha-amylase a novel receptor for Bacillus thuringiensis israelensis Cry4Ba and Cry11Aa toxins in the malaria vector mosquito Anopheles albimanus (Diptera: Culicidae)”. Environmental Microbiology 12 (2010): 746-757.
  86. Ochoa-Campuzano C., et al. “An ADAM metalloprotease is a Cry3Aa Bacillus thuringiensis toxin receptor”. Biochemical and Biophysical Research Communications 362 (2007): 437-442.
  87. Liu X. “ABC Family Transporters”. Advances in Experimental Medicine and Biology 1141 (2019): 13-100.
  88. Sato R., et al. “Function and Role of the ATP-binding Cassette Transporters as Receptors for 3D-Cry Toxins”. Toxins 11 (2019): 124-141.
  89. Xiao Y., et al. “Mis-splicing of the ABCC2 gene linked with Bt toxin resistance in Helicoverpa armiguera”. Scientific Report 4 (2014): 618.
  90. Baxter SW., et al. “Parallel evolution of Bt toxin resistance in Lepidoptera”. Genetics 189 (2011): 1-19.
  91. Atsumi S., et al. “Single aminoacid mutation in an ATP-binding casette transporter gene causes resistance to Bt roxin Cry1Ab to the silkworm. Bombyx mori”. Proceedings of the National Academy of Sciences of the United States of America 109 (2012): E1591-1598.
  92. Adewaga S., et al. “The domain II loops of Bacillus thuringiensis Cry1Aa form an overlapping interaction site for two Bombyx mori larvae functional receptors, ABC transporter C2 and cadherin-like receptor”. BBVA Proteins Proteome 1868 (2007): 220-231.
  93. Oppert B., et al. “Proteinase-mediated insect resistance to Bacillus thuringiensis toxins”. Journal of Biological Chemistry 272 (1997): 23473-23476.
  94. Griffitts J., et al. “Many roads to resistance: how invertebrates adapt to Bt toxins”. BioEssays 27 (2005): 614-624.
  95. Bravo A and Soberón M. “How to cope with resistance to Bt toxins?” Trends in Biotechnology 26 (2008): 573-579.
  96. Tabashnik BE., et al. “Insect resistance to Bt crops: evidence versus theory”. Nature Biotechnology 26 (2008): 199-202.
  97. Jurat-Fuentes JI., et al. “Mechanism of resistance to insecticidal proteins from Bacillus thuringiensis”. Annual Review of Entomology 66 (2021): 121-146.
  98. Zhu B., et al. “MicroRNA-9983p contributes to Cry1Ac-resistance by targeting ABCC2 in lepidopteran insects”. Insect Biochemistry and Molecular Biology 117 (2020):
  99. Xu X., et al. “Disruption of a cadherin gene associated with resistance to Cry1Ac delta-endoxtin of Bacillus thuringiensis in Helicoverpa armiguera”. Applied and Environmental Microbiology 71 (2005): 946-954.
  100. Gahan LJ., et al. “An ABC transporter mutation is correlated with insect resistance to Bacillus thuringiensis Cry1Ac toxin”. PLoS Genetics 6 (2010):
  101. Morin S., et al. “Three cadherin alleles associated with resistance to Bacillus thuringiensis in pink bollworm”. Proceedings of the National Academy of Sciences of the United States of America 100 (2003): 5004-5009.
  102. Caccia S., et al. “Association of Cry1Ac toxin resistance in Helicoverpa zea (Boddie) with increased alkaline phosphatase level in the midgut lumen”. Applied and Environmental Microbiology 78 (2012): 5690-5698.
  103. Tabashnik BE., et al. “Supressing resistance to Bacillus thuringiensis cotton with sterile insect releases”. Nature Biotechnology 28 (2010): 1304-1307.
  104. Soberón M., et al. “Engineering modified Bacillus thuringiensis toxins to counter insect resistance”. Science 318 (2007): 1640-1642.
  105. Chen G., et al. “Differences in midgut transcriptomes between resistant and susceptible strains of Chilo suppressalis to Cry1C toxin”. BMC Genomics 21 (2020):
  106. Kwong WK., et al. “Immune system stimulation by the native gut microbiota of honey bees”. Royal Society Open Science 4 (2017):
  107. Shao Y., et al. “Symbiont-derived antimicrobials contribute to the control of the lepidopteran gut microbiota”. Cell Chemical Biology 24 (2017): 66-75.
  108. Van Rensburg JBJ. “First report of field resistance by stem borer Busseola fusca (Fuller) to Bacillus thuringiensist transgenic maize”. South African Journal of Plant and Soil 24 (2007): 147-151.
  109. Gómez-Díaz E., et al. “Epigenetics of host-pathogen interactions: the road ahead and the road behind”. PLoS Pathogen 8 (2012):
  110. Laland K., et al. “Does evolutionary theory need a rethink?” Nature 514 (2014): 161-164.
  111. Skinner MK. “Environmental epigenetics and a unified theory of the molecular aspects of evolution: a neo-Lamarckian concept that facilitates neoDarwinian evolution”. Genome Biological Ecology 7 (2015): 1296-1302.
  112. Eggert H., et al. “Different effects of paternal trans-generational immune priming on survival and immunity in step and genetic offspring”. Proceedings B is the Royal Society 281 (2014): 20142089.
  113. Schulz NKE., et al. “Transgenerational developmental effects of immune priming in the red flour beetle Tribolium castaneum”. Frontiers in Physiology 10 (2019):
  114. Vilcinskas A. “The role of epigenetics in host-parasite coevolution: lessons from the model host insects Galleria mellonella and Tribolium castaneum”. Zoology (Jena) 119 (2016): 273-280.
  115. Mukherjee K., et al. “Histone acetylation mediates epigenetic regulation of transcriptional reprogramming in insects during metamorphosis, wounding and infection’. Frontiers in Zoology 9 (2012):
  116. Jones CM., et al. “Genome-wide characterization of DNA methylation in an invasive lepidopteran pest, the cotton bollworm Helicoverpa armigera”. G3 (Bethesda) 8 (2018): 779-787.
  117. Peterson B., et al. “An overview of mechanisms of Cry toxin resistance in lepidopteran insects”. Journal of Economic Entomology 110 (2017): 362-377.
  118. Guo Z., et al. “MAPK signaling pathway alters expression of midgut ALP and ABCC genes and causes resistance to Bacillus thuringiensis Cry1Ac toxin in diamondback moth”. PLoS Genetics 11 (2015):
  119. Li H., et al. “Interaction of the Bacillus thuringiensis delta endotoxins Cry1Ac and Cry3Aa with the gut of the pea aphid, Acyrthosiphon pisum (Harris)”. Journal of Invertebrate Pathology 107 (2011): 69-78.
  120. Wang YY., et al. “Toxicological, biochemical, and histopathological analyses demonstrating that Cry1C and Cry2A are not toxic to larvae of the honeybee, Apis mellifera”. Journal of Agricultural and Food Chemistry 63 (2015): 6126-6132.
  121. Emery O., et al. “Immune system stimulation by the gut symbiont Frischella perrara in the honey bee, Apis mellifera”. Molecular Ecology 26 (2017): 2576-2590.
  122. Boyer S., et al. “Influence of insecticide Bacillus thuringiensis subsp israelensis treatments on resistance and enzyme activities in Aedes rusticus larvae (Diptera: Culicidae)”. Biological Control 62 (2012): 75-81.
  123. Zhao Z., et al. “Differential gene expression in response to eCry3.1Ab ingestion in an unselected and eCry3.1Ab-selected western corn rootworm Diabrotica virgifera virgifera LeConte population”. Scientific Report 9 (2019):


Citation: Gloria G Guerrero M. “Biocidal Activity of the Bacillus thuringiensis 3D Cry Toxins, Molecular Crosstalk at the Insect Midgut with Implication in Insect Resistance Development".Acta Scientific Microbiology 7.6 (2024): 37-51.


Copyright: © 2024 Gloria G Guerrero M. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


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