Abstract
With age, worker honey bees normally proceed from performing activities inside the nest to foraging in the field, creating an age-related division of labor. We previously established that the whole-body protein profiles of nest workers and foragers are different, and proposed that this proteomic divergence in part is explained by a shift in metabolic requirements as worker bees initiate intense flight. The unique plasticity of honey bee worker ontogeny, however, provides further opportunities to investigate if such changes in the proteome are dynamic or, alternatively, are permanently induced. Through manipulation of the social structure of colonies, foragers can be forced to revert to nest tasks, and in the current study we investigate how protein profiles respond to such reverse development. By using a quantitative LC-MS/MS-based approach in conjunction with robust statistical validation we show that after reversal from foraging to nest activities, subsets of proteins are detected at relative concentrations that characterize nest bees, whereas other proteins remain unchanged at relative concentrations normally found in foragers. In all, we quantified the levels of 81 proteins, and for 22 of these we found significant differences between worker groups before and after reversion. We interpret these patterns as examples of plasticity and robustness at the proteome level that are linked to characteristics of behavior and aging in Apis mellifera.
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Acknowledgements
We thank Nick Baker and M. Kim Fondrk for help with bees. GVA was supported by NFR #171958, #175413, NSF #0615502 and the PEW foundation, and FW by a Feodor Lynen stipend provided by the Humboldt foundation. We are grateful for helpful comments and access to the LTQ provided by Zhengping Yi and Lawrence Mandarino.
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Wolschin, F., Amdam, G.V. Plasticity and robustness of protein patterns during reversible development in the honey bee (Apis mellifera). Anal Bioanal Chem 389, 1095–1100 (2007). https://doi.org/10.1007/s00216-007-1523-5
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DOI: https://doi.org/10.1007/s00216-007-1523-5