MON 95379 corn contains the cry1Da1_7 gene, which encodes the Cry1Da_7 protein, and the cry1B.868 gene, which encodes the Cry1B.868 protein, a chimeric protein constituted by the fusion of Domains I and II of the Cry1Be (Bt) protein, from the III of the Cry1Ca protein (Bt subsp. aizawai) and the C-terminal domain of Cry1Ab protein protoxin (Bt subsp. kurstaki). Ingestion of proteins by the target insect exposes them to alkaline conditions and proteases in its midgut, resulting in proteolytic cleavage of the protoxin domains of the proteins, converting the proteins into insecticidal active toxins. The Cry1Da_7 protein is the modified version of the Cry1Da protein and has approximately 99.7% (4 altered amino acids) sequence similarity to the native Bacillus thuringiensis Cry1Da protein. These changes were made to increase activity against the Helicoverpa zea pest while maintaining the spectrum ofactivity for Spodoptera frugiperda, both insects targeted by the technology present in MON 95379 corn. The Cry1B.868 protein is chimeric, having Domains I and II of the Cry1Be protein, Domain III of the Cry1Ca protein and the C-terminal Domain of the protein's protoxin Cry1Ab. The amino acid sequences of each domain in the Cry1B.868 protein are 100% identical to their respective domains in the donor proteins. The domain switch strategy aims to achieve high levels of activity against target lepidopteran insects.