Structure of native glycolipoprotein filaments in honeybee royal jelly.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 33293513.
- Also identified by DOI 10.1038/s41467-020-20135-x and PMC identifier 7722742.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Fatty Acids
- Glycoproteins
- Insect Proteins
- Lipoproteins