@article{fdi:010065326,
  title = {{C}ry4{B}a and {C}yt1{A}a proteins from {B}acillus thuringiensis israelensis : interactions and toxicity mechanism against {A}edes aegypti},
  author = {{E}lleuch, {J}. and {J}acca, {S}. and {D}arriet, {F}r{\'e}d{\'e}ric and {C}handre, {F}abrice and {T}ounsi, {S}. and {Z}ghal, {R}. {Z}.},
  editor = {},
  language = {{ENG}},
  abstract = {{I}ndividual crystal proteins from {B}acillus thuringiensis israelensis exhibit variable levels of insecticidal activities against mosquito larvae. {I}n all cases, they are much less active compared to the whole crystal proteins due to described complex synergistic interactions among them. {I}n the present study we investigated the effects of {C}yt1{A}98 (a {C}yt1{A}a type protein) on {C}ry4{BLB} (a {C}ry4{B}a type toxin) insecticidal activity toward the dengue vector {A}edes aegypti. {T}he bioassay analyses demonstrated the ability of {C}yt1{A}98 protein to enhance {C}ry4{BLB} toxin larvicidal activity even at a low proportion in the mixture (1%). {I}n vitro interaction assays showed that {C}yt1{A}98 provides supplementary binding sites for {C}ry4{BLB} in {A}. aegypti {BBMV}s. {M}oreover, it enhances the formation of {C}ry4{BLB} oligomeric structure. {T}hese results support that {C}yt1{A}98 protein could act as a membrane-bound receptor fixing {C}ry4{BLB} delta-endotoxins and promoting its oligomerization.},
  keywords = {{B}acillus thuringiensis israelensis ; {C}ytolytic protein {C}yt1{A}98 ; {C}ry4{BLB} ; toxin ; {S}ynergism ; {A}edes aegypti},
  booktitle = {},
  journal = {{T}oxicon},
  volume = {104},
  numero = {},
  pages = {83--90},
  ISSN = {0041-0101},
  year = {2015},
  DOI = {10.1016/j.toxicon.2015.07.337},
  URL = {https://www.documentation.ird.fr/hor/fdi:010065326},
}