Abstract

The mass recruitment to the midgut contents of lysosomal proteolytic enzymes occurred in insects under three major selective pressures. Hemipteran (true bugs, aphids, and cicadas) ancestors lost their serine peptidases (SP) on adapting to feed on protein-free plant sap. When they returned to protein diets, their cathepsins L and B were recruited to replace their lost SP. Among beetles of the series Cucujiformia, cathepsins L were recruited to hydrolyze ingested plant inhibitors that affect their major SP and/or to deal with special seed proteins, such as prolamins. Larval flies have a very acid middle midgut and use cathepsin D to digest bacteria from their infected food. All the recruited enzymes originated from duplicated genes. The recruited digestive enzymes differ from their lysosomal counterparts in critical regions of their amino acid sequences that resulted in changes in substrate specificities and other kinetic properties. The discharge of digestive cathepsins in the midgut contents, instead of lysosomes, seems to be a consequence of their overexpression or the existence of new targeting signals. Their activation at the midgut contents occurs by an autoactivation mechanism or with the help of other enzymes or by a combination of both. The targeting to lysosomes of the insect lysosomal enzymes does not follow the mammalian mannose 6-phosphate route, but an incompletely known mechanism.

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