The insecticidal activity of Bacillus thuringiensis subsp. israelensis (Bti) is due to synergistic interactions among its four major proteins (Cry4Aa, Cry4Ba, Cry11Aa, Cyt1Aa), while the activity of Lysinibacillus sphaericus (Ls) is due to a binary toxin (Bin) consisting of a toxin domain, BinA, and a midgut receptor-binding domain, BinB. Although used commercially for almost three decades, reports of mosquito resistance to Bti have been rare. However, levels of resistance greater than 10,000-fold to Bin have been reported where Ls has been used intensively for mosquito control. Cyt1Aa is a lipophilic protein, and in previous studies we showed it delays the evolution of resistance to the Cry proteins of Bti, and can overcome high levels of resistance Bin. In a previous study, we fused Cyt1Aa to BinA, using the lipophile as a broad-spectrum binding domain and showed that the Cyt1Aa-BinA chimera was remarkably toxic to five major vector species of mosquitoes, Anopheles gambiae, An. stephensi, An. quadrimaculatus, Bin-sensitive and Bin-resistant strains of Culex quinquifasciatus, and Aedes aegypti, the latter not normally sensitive to Ls. However, toxicity against Aedes aegypti was not as high as against other mosquito species. Here we show that introducing another highly mosquitocidal protein, Cry11B from B. thuringiensis subsp. jegathesan, enhances the chimera’s toxicity against Ae. aegypti significantly but not against Cx. quinquefasciatus.