ABSTRACT: This dataset derives from a comparative quantitative proteomics study designed to elucidate stage-specific molecular responses to heme-induced oxidative stress in Aedes aegypti, a major vector of dengue, Zika, and chikungunya viruses. During blood digestion in hematophagous insects, the release of free heme represents a significant physiological challenge, as this molecule acts as a strong pro-oxidant capable of catalyzing the formation of reactive oxygen species (ROS) and promoting widespread oxidative damage. In mosquitoes, the maintenance of redox homeostasis is essential not only for survival and development but also for vector competence, given that mitochondrial performance, antioxidant capacity, and immune signaling are tightly linked to arboviral replication and transmission dynamics. Whole-body samples from fourth-instar larvae (L4) and 3–5-day-old adult females were exposed to 10 mM hemin for 24 h, alongside unexposed control groups processed in parallel. Proteomic profiles were generated using label-free liquid chromatography–tandem mass spectrometry (LC–MS/MS) in data-dependent acquisition mode, resulting in the identification of 948 proteins across all experimental conditions. Comparative analyses of protein abundance revealed pronounced and divergent stage-specific proteomic signatures in response to heme exposure. In larvae, heme treatment led to a general downregulation of metabolic proteins, accompanied by the selective upregulation of antioxidant enzymes (such as glutathione S-transferases and glutamate–cysteine ligase), iron-binding proteins (including ferritin and transferrin), cytoskeletal components, and cuticle-associated proteins. This profile is consistent with a physiological strategy centered on energy conservation, coupled with targeted investment in detoxification pathways and structural reinforcement. In contrast, adult females displayed a proteomic response characterized by the maintenance of mitochondrial and proteostatic functions, with selective upregulation of proteins involved in energy metabolism (ATP synthase, succinate dehydrogenase, and malate dehydrogenase), molecular chaperones (heat shock proteins and prohibitin), and components of the contractile machinery (myosin and troponin), highlighting a close integration between bioenergetic capacity and functional resilience. Notably, both developmental stages exhibited enrichment of cuticle-related proteins, suggesting that heme-induced structural remodeling constitutes a conserved adaptive response across the mosquito life cycle. These findings illuminate developmental stage-dependent strategies for coping with heme-induced oxidative stress and provide mechanistic insights into mosquito redox biology, proteostasis networks, and potential vulnerabilities exploitable for innovative vector control strategies.
Felipe Almeida 
