α-1,6-fucosyltransferase plays a critical role during embryogenesis of the hemimetabolous insect Nilaparvata lugens.

Protein glycosylation is one of the most important post-translational modifications, modulating the properties of proteins. In insects, α-1,6-fucosyltransferase (FucT6) is an important enzyme in the glycosylation pathway, modifying the core structure of N-glycans on glycoproteins with the addition of a fucose residue. In our previous study, RNAi-mediated silencing of FucT6 in the third-instar nymphs of Nilaparvata lugens caused a failure of the ecdysis process during nymphal development, leading to high mortality. These results suggested the requirement of FucT6 during nymphal development in N. lugens. In this study, RNAi-mediated gene silencing of FucT6 in adults did not cause lethality. However, parental RNAi of FucT6 led to full failure in the hatching of eggs, and this effect was maternally mediated. Interestingly, gene expression levels of FucT6 in the eggs peaked at the katatrepsis event, where the embryo rotates 180° resulting in the head pointing towards the anterior side of the egg. Proteome analysis showed significant differences in the abundance of proteins between different embryonal developmental stages, suggesting the crucial role of FucT6 mediated core N-fucosylation in embryonal development. Therefore, correct α-1,6-fucosylation of glycoproteins is important for N. lugens during embryonic development and this study provides new insights into the role of N-glycosylation in embryogenesis in insects.