In GSK-3-silenced A.fluviatilis, embryonic developmental was delayed, compared to control embryos. Similarly, Dedeine et al. observed that vitellogenesis was blocked in the wasp Asobara tabida without Wolbachia, suggesting the involvement of Wolbachia in oocyte differentiation, yolk production and germ cell division. GSK-3 silencing also decreased in Rhipicephalus microplus oviposition, as well as egg hatching, proposing that enzyme as an essential protein for embryo formation. Syncytial blastoderm was observed within 6 HAO, and the germ band extension started at 12 HAO. Around 24 HAO, germ band retraction begins, similarly to what was observed for A. aegypti and Anopheles albitarsis. Embryo development is complete within 48 HAO, and larvae are ready to hatch. Previously, germ band retraction was correlated with increased glycolysis during A. aegypti embryogenesis. In the present work, hexokinase and pyruvate kinase activities were measured during A. fluviatilis embryogenesis in order to investigate glycolysis. Both enzymes in W2 and W+ embryos increased activity after 6 HAO, coinciding with syncytial blastoderm formation. In A. aegypti mosquitoes, ILP3 stimulates egg maturation, suggesting that an endogenous ILP stimulates egg maturation by activating the insulin signaling pathway in the ovaries. Activation of insulin signaling pathway promotes GSK-3 inhibition by phosphorylation via AKT, contributing to glycogen and protein synthesis. Wolbachia interferes in this process, increasing the insulin signaling pathway flux in Drosophila melanogaster. The amount of Wolbachia is linked to embryo growth and development in Drosophila simulans, interacting with the microtubules and cell divisions of these flies. Wolbachia may affect glycogen metabolism in A. fluviatilis embryos due to a drastic change in glucose metabolism observed in W+ embryos. The enzymes involved in the synthesis and degradation of glycogen are absent in the Wolbachia genome, as well as the enzymes of the glycolytic preparatory phase. This suggests that Wolbachia may be able to internalize host pyruvate, which would be further processed by the pyruvate phosphate dikinase identified in the Wolbachia genome. Pyruvate phosphate dikinase uses pyruvate to produce fructose 6-phosphate and acetyl-CoA, as described by Foster et al.. Pyruvate is the final product of glycolysis and represents the major substrate of the tricarboxylic acid cycle in mitochondria, playing a central role in carbon metabolism regulation. Additionally, pyruvate participates in the catabolic and anabolic pathways, consuming or synthetizing glucose. The hypothesis of pyruvate internalization by the bacterium is corroborated by the identification of an enzyme linked to lipid degradation in the Wolbachia genome, indicating a pyruvate dependence to obtain energy. Despite this finding, the endosymbiont Wigglesworthia may oxidize amino acids derived from the host to obtain energy.