Metarhizium anisopliae is an entomopathogenic
fungus that has evolved specialized strategies to infect insect hosts.
Here we analyzed secreted proteins related to Dysdercus peruvianus infection. Using shotgun proteomics, abundance changes in 71 proteins
were identified after exposure to host cuticle. Among these proteins
were classical fungal effectors secreted by pathogens to degrade physical
barriers and alter host physiology. These include lipolytic enzymes,
Pr1A, B, C, I, and J proteases, ROS-related proteins, oxidorreductases,
and signaling proteins. Protein interaction networks were generated
postulating interesting candidates for further studies, including
Pr1C, based on possible functional interactions. On the basis of these
results, we propose that M. anisopliae is degrading
host components and actively secreting proteins to manage the physiology
of the host. Interestingly, the secretion of these factors occurs
in the absence of a host response. The findings presented here are
an important step in understanding the host–pathogen interaction
and developing more efficient biocontrol of D. peruvianus by M. anisopliae.