@article{fdi:010064913,
  title = {{E}ffects of the {P}20 protein from {B}acillus thuringiensis israelensis on insecticidal crystal protein {C}ry4{B}a},
  author = {{E}lleuch, {J}. and {Z}ghal, {R}. {Z}. and {B}en {F}guira, {I}. and {L}acroix, {M}. {N}. and {S}uissi, {J}. and {C}handre, {F}abrice and {T}ounsi, {S}. and {J}aoua, {S}.},
  editor = {},
  language = {{ENG}},
  abstract = {{T}he accessory protein {P}20 from {B}acillus thuringiensis israelensis has been defined as an important molecular chaperone for forming crystal {C}yt1{A}a, and enhancing {C}ry11{A}a and {C}ry4{A}a expression. {T}o investigate its putative role in {C}ry4{B}a delta-endotoxin production and toxicity, a p20 gene was cloned and introduced into {B}. thuringiensis recombinant strain expressing cry4{B}a type gene (cry4{BLB}). {T}he delta-endotoxin synthesis was enhanced by 262%. {T}he generated inclusions were assayed against third instar larvae of {A}edes aegypti. {T}he combination of {P}20 protein with {C}ry4{BLB} delta-endotoxin led to a stable mortality rate of 25% with doses ranging from 0.2 mg l(-1) to 0.6 mg l(-1). {C}ry4{BLB} crystals produced in the presence of {P}20 were much less soluble than those produced by the control strain lacking {P}20 at p{H} lower than or equal to 10.5. {T}he observed toxicity perturbation correlates with a decrease of {C}ry4{BLB} inclusions solubility. {T}he presence of {P}20 protein has affected {C}ry4{BLB} crystallization and altered greatly its solubility properties. {C}ry4{B}a effectiveness against {A}. aegypti larvae is related to the solubilization step in larval guts environment.},
  keywords = {20-k{D}a chaperone-like protein ; {C}ry4{BLB} larvicidal activity ; {T}oxin ; solubilization},
  booktitle = {},
  journal = {{I}nternational {J}ournal of {B}iological {M}acromolecules},
  volume = {79},
  numero = {},
  pages = {174--179},
  ISSN = {0141-8130},
  year = {2015},
  DOI = {10.1016/j.ijbiomac.2015.04.035},
  URL = {https://www.documentation.ird.fr/hor/fdi:010064913},
}