Abstract
Royal jelly (RJ) is produced by honeybees (Apis mellifera) as nutrition during larval development. The high viscosity of RJ originates from high concentrations of long lipoprotein filaments that include the glycosylated major royal jelly protein 1 (MRJP1), the small protein apisimin and insect lipids. Using cryo-electron microscopy we reveal the architecture and the composition of RJ filaments, in which the MRJP1 forms the outer shell of the assembly, surrounding stacked apisimin tetramers harbouring tightly packed lipids in the centre. The structural data rationalize the pH-dependent disassembly of RJ filaments in the gut of the larvae.
Highlights
Royal jelly (RJ) is produced by honeybees (Apis mellifera) as nutrition during larval development
We present the structure of native RJ filaments using a combination of cryogenic electron microscopy approaches based on tomography and helical reconstruction methods
SDSPAGE and mass spectrometry analysis confirmed that major royal jelly protein 1 (MRJP1) was the most abundant protein component of the filaments (Supplementary Fig. 1), which eluted at a size exclusion chromatography (SEC) volume corresponding to a molecular mass above 500 kDa
Summary
Royal jelly (RJ) is produced by honeybees (Apis mellifera) as nutrition during larval development. Purified RJ filaments were vitrified and imaged to acquire 11 dose-symmetric tilt series (Supplementary Fig. 2).
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