Proteome analysis of Apis mellifera royal jelly.
Royal jelly plays a pivotal role in the development of honey bee larvae. However, while various health promoting properties of royal jelly have been reported, most of the active substances within royal jelly that lead to these properties are still unknown. Since up to 50% (dry mass) of royal jelly is protein, royal jelly proteome analysis is a promising starting point for attempts to identify the proteins that provide health-promoting effects. However, the comprehensive analysis of royal jelly proteins is hampered by the enormous abundance of some proteins in the major royal jelly protein family, which constitutes 80-90% of the royal jelly proteome. The high heterogeneity of these proteins is an additional challenge for proteomic analysis, since it necessitates the use of analytical techniques that provide high resolution and a wide dynamic range. The application of individual methods such as 2D-PAGE or multidimensional chromatography can only yield certain subpopulations of a proteome due to the specific bias of each method. We applied different methods for the prefractionation and separation of royal jelly proteins in order to circumvent the shortcomings of the individual techniques and achieve a high coverage of the royal jelly proteome. In this way, we were able to identify 20 different proteins in total, as well as to show a very high degree of cleavage of different proteins of the major royal jelly protein family. Furthermore, we investigated the protein phosphorylation of royal jelly proteins, and identified and located two phosphorylation sites within venom protein 2.
Schönleben
Simone
S
Biocenter, Pharmaceutical Biology, Proteomics Group, Julius-von-Sachs-Institute for Biosciences, University of Wuerzburg, Julius-von-Sachs-Platz 2, 97082, Wuerzburg, Germany.
Sickmann
Albert
A
Mueller
Martin J
MJ
Reinders
Joerg
J
D000818:Animals; D001516:Bees / Q000737:chemistry*; D002853:Chromatography, Liquid; D002918:Chymotrypsin / Q000032:analysis; D023082:Defensins / Q000032:analysis; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005227:Fatty Acids / Q000737:chemistry*; D006023:Glycoproteins / Q000032:analysis; D019476:Insect Proteins / Q000032:analysis* / Q000737:chemistry; D007525:Isoelectric Focusing; D010446:Peptide Fragments / Q000032:analysis / Q000737:chemistry; D020543:Proteome / Q000032:analysis*; D016601:RNA-Binding Proteins; D053719:Tandem Mass Spectrometry / Q000379:methods; D014357:Trypsin / Q000032:analysis; D000099219:Royal Jelly
D002918:Chymotrypsin; D023082:Defensins; D005227:Fatty Acids; D006023:Glycoproteins; D019476:Insect Proteins; D010446:Peptide Fragments; D020543:Proteome; D016601:RNA-Binding Proteins; D014357:Trypsin; D000099219:Royal Jelly; C109593:MRJP3 protein, Apis mellifera