Informace o publikaci
From Interactions to Function: Investigating the Honey Bee Apolipophorin-1
| Autoři | |
|---|---|
| Rok publikování | 2026 |
| Druh | Další prezentace na konferencích |
| Fakulta / Pracoviště MU | |
| Citace | |
| Popis | Apolipophorin-1 (Apolp1) belongs to the large lipid transfer protein superfamily. This group of insect proteins is known for its role in the transport of lipids and other hydrophobic compounds, but there is an increasing amount of evidence suggesting that they have other functions, e.g. participation in the immune system or redox homeostasis. Despite its regular appearance in honey bee omics study datasets, and its sharing of several conserved domains with the highly studied, multifunctional protein vitellogenin, honey bee Apolp1 remains severely understudied. In our research, we explored the conserved domains of Apolp1, monitored its seasonal variations, and localised it in several tissue types using in-house monoclonal antibodies. We also employed immunoprecipitation, followed by tandem mass spectrometry, to identify its protein interactors. Our results revealed a distinct expression pattern for Apolp1 that was negatively correlated with that of the key regulatory protein vitellogenin. This suggests that Apolp1 may play a pivotal role in the seasonal adaptations of honey bees. Interactome analysis identified 183 interacting proteins that participate in various biological processes, suggesting that Apolp1 has a plethora of roles beyond lipid metabolism. These results provide new hypotheses that we plan to corroborate using confocal microscopy and in vivo knock-down experiments. This research is supported by the Ministry of Agriculture of the Czech Republic (project no. QK21010088) in collaboration with the CEITEC Proteomics Core Facility, part of the CIISB, Instruct-CZ Centre, supported by the Ministry of Education, Youth and Sports of the Czech Republic (project no. LM2023042). |
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