Structure of native glycolipoprotein filaments in honeybee royal jelly

Simone Mattei, Arvid Ban, Armin Picenoni, Marc Leibundgut, Rudi Glockshuber () and Daniel Boehringer ()
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Simone Mattei: ETH Zurich
Arvid Ban: ETH Zurich
Armin Picenoni: ETH Zurich
Marc Leibundgut: ETH Zurich
Rudi Glockshuber: ETH Zurich
Daniel Boehringer: ETH Zurich

Nature Communications, 2020, vol. 11, issue 1, 1-7

Abstract: 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.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-20135-x

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DOI: 10.1038/s41467-020-20135-x

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