Sugar can glow like a soap bubble - CMCB technology platform supports microscopy courses for children in newly inaugurated digital classroom
Prof. Michael Schlierf is new B CUBE director
Anton Batalov, PicoQuant
Dr. Kerstin Blank, MPI Potsdam-Golm
Schlierf Group - Open Topic Postdoc Anja Buttstedt
I would like to express my utmost disapproval of the new scholarship for female doctoral and postdoctoral students at the TU Dresden.
Working for a scholarship of 1365 € and 1750 €, respectively, is not what I would call equal opportunity. Besides earning less money than normal employees (TV-L E13, 65 and 100%, respectively), this also means that you have to pay health insurance from the scholarship and you neither pay into unemployment insurance nor pension insurance.
(Opinions are my own and not the views of my employer.)
Elucidation of the functions of honey bees' larval food proteins
Contact details: Room 220 +49 (0)351 46343055 firstname.lastname@example.org @bienenanja
Major royal jelly proteins (MRJPs) have been first identified in royal jelly (RJ), a secretion of the hypopharyngeal and mandibular glands of young worker bees that is used to rear female larvae to majestic queens. Due to the high abundance of essential amino acids in these proteins it has been assumed that they have mainly nutritional functions during larval development. With the release of the honeybee genome it became clear that MRJPs are not only comprised of the four MRJPs actually present in RJ but moreover of nine proteins whose encoding genes (mrjp1 – 9) are located in a tandem array on chromosome 11 flanked by the genes yellow-e3 and yellow-h (Helbing et al., 2017).
Screening currently available genomes, we found that mrjps are common in Hymenopteran species but mostly restricted to one copy also located between the two yellow genes (Buttstedt et al., 2014). In addition to the honeybee, cases of copy number radiations arose in some Hymenopteran species including the leaf cutter ant Atta cephalotes and the parasitic wasp Nasonia vitripennis. However, mrjps have up to now never been found outside of the Hymenoptera and thus they seem to be limited to the order but are not a prerequisite for survival as some species, e.g., the fire ant Solenopsis invicta, can perfectly live without.
With my current research two important questions are approached:
1.) What are the functions of these major royal jelly proteins?
2.) Why does the honeybee need so many of them?
In a first study we determined the expression of the nine mrjps in various body parts (head, thorax, abdomen) in all honeybee castes and both sexes (Buttstedt et al., 2013). We found that mrjp8 and 9 have been evenly expressed among the body parts whereas the expression of mrjp1 to 7 was focused in the worker heads. Here, expression is not only high in the food jelly producing hypopharyngeal glands, but also in the worker brains, with MRJP1 being the most abundant and the 5th most abundant protein, respectively (Dobritzsch et al., 2019). Expression of mrjps in worker heads is partly controlled by the molting hormone ecdysone (Winkler et al., 2018). Interestingly, expression has not only been up-regulated in brood rearing nurses with active food glands but also in foraging bees compared to the caged controls. Thus, the functions of MRJPs are clearly not limited to the food glands.
For a monomeric form of MRJP1 a participation in queen determination by oral administration to developing larvae was claimed but could not be verified (Buttstedt et al., 2016). Nevertheless, we could show that the role of MRJP1 in RJ is in no way unspectacular. The protein simply ensures the survival of the bee colony - though in a way entirely different than initially thought (Buttstedt et al., 2018). MRJP1 assembles together with the protein apisimin only at pH 4, the native pH of RJ, into long fibrillary structures thereby increasing RJ viscosity. This becomes extremely important for developing queen larvae as those are raised in specialized queen cells which are attached to the lower edge of a honey comb. Queen larvae are essentially hanging from the ceiling of their cells and avoid with the help of the protein fibrils to fall out of them. And indeed, also in RJ fibrillar structures are only found at native pH 4 but not at an exogenously induced pH of 7 (Kurth et al., 2018). In general, MRJPs are way more stable at acidic than at neutral pH (Muresan et al., 2018; Muresan & Buttstedt, 2019). Another important function of RJ is clearly to protect the developing larvae from brood diseases as both RJ and the complex of MRJP1 and apisimin have been shown to exhibit antibacterial properties (Vezeteu et al., 2017).
18.) D Dobritzsch, D Aumer, M Fuszard, S Erler, A Buttstedt (2019): The rise and fall of major royal jelly proteins during a honeybee (Apis mellifera) workers' life. Ecology and Evolution 9(15):8771-8782 (DOI:10.1002/ece3.5429)
17.) CI Muresan, A Buttstedt (2019): pH-dependent stability of honey bee (Apis mellifera) major royal jelly proteins. Scientific Reports 9:9014 (DOI: 10.1038/s41598-019-45460-0)
16.) T Kurth, S Kretschmar, A Buttstedt (2019): Royal jelly in focus. Insectes Sociaux 66(1):81-89 (DOI: 10.1007/s00040-018-0662-3)
15.) P Winkler, F Sieg, A Buttstedt (2018): Transcriptional control of honey bee (Apis mellifera) major royal jelly proteins by 20-hydroxyecdysone. Insects 9(3):122 (DOI: 10.3390/insects9030122)
14.) CI Muresan, A Schierhorn, A Buttstedt (2018): The fate of major royal jelly proteins during proteolytic digestion in the human gastrointestinal tract. Journal of Agricultural and Food Chemistry 66(16):4164-4170 (DOI: 10.1021/acs.jafc.8b00961)
13.) A Buttstedt, CI Muresan, H Lilie, G Hause, CH Ihling, S-H Schulze, M Pietzsch, RFA Moritz (2018): How honeybees defy gravity to raise queens. Current Biology 28(7):1095-1100 (DOI: 10.1016/j.cub.2018.02.022)
12.) S Helbing, HMG Lattorff, RFA Moritz, A Buttstedt (2017): Comparative analyses of the major royal jelly protein gene cluster in three Apis species with long amplicon sequencing. DNA Research 24(3):279-287 (DOI: 10.1093/dnares/dsw064)
11.) TV Vezeteu, O Bobis, RFA Moritz, A Buttstedt (2017): Food to some, poison to others - honeybee royal jelly and its growth inhibiting effect on European Foulbrood bacteria. MicrobiologyOpen 6(1):e00397 (DOI: 10.1002/mbo3.397)
10.) A Buttstedt, CH Ihling, M Pietzsch, RFA Moritz (2016): Royalactin is not a royal making of a queen. Nature 537(7621):E10-E12 (DOI: 10.1038/nature19349)
Featured in Mitteldeutsche Zeitung
9.) T Pamminger, A Buttstedt, V Norman, A Schierhorn, C Botias, J Jones, K Basley, WHO Hughes (2016): The effects of juvenile hormone in Lasius niger reproduction. Journal of Insect Physiology 95:1-7 (DOI: 10.1016/j.jinsphys.2016.09.004)
8.) CM Aurori, A Buttstedt, DS Dezmirean, LA Marghitas, RFA Moritz, S Erler (2014): What is the main driver of ageing in long-lived winter honeybees: antioxidant enzymes, innate immunity, or vitellogenin? Journals of Gerontology, Series A 69(6):633-639 (DOI: 10.1093/gerona/glt134)
7.) A Buttstedt, RFA Moritz, S Erler (2014): Origin and function of the major royal jelly proteins of the honeybee (Apis mellifera) as members of the yellow gene family. Biological Reviews 89(2):255-269 (DOI: 10.1111/brv.12052)
6.) CI Pavel, LA Marghitas, DS Dezmirean, LI Tomos, V Bonta, A Sapcaliu, A Buttstedt (2014): Comparison between local and commercial royal jelly - use of antioxidant activity and 10-hydroxy-decenoic acid as quality parameter. Journal of Apicultural Research 53(1): 116-123 (DOI: 10.3896/IBRA.184.108.40.206)
5.) A Buttstedt, RFA Moritz, S Erler (2013): More than royal food - Major royal jelly protein genes in sexuals and workers of the honeybee Apis mellifera. Frontiers in Zoology 10: 72 (DOI: 10.1186/1742-9994-10-72)
4.) A Buttstedt, T Wostradowski, C Ihling, G Hause, A Sinz, E Schwarz (2013): Different morphology of fibrils originating from agitated and non-agitated conditions. Amyloid 20(2): 86-92 (DOI: 10.3109/13506129.2013.784962)
3.) N Barbezier, A Chartier, Y Bidet, A Buttstedt, C Voisset, H Galons, M Blondel, E Schwarz, M Simonelig (2011): PABPN1 toxicity and aggregation in oculopharyngeal muscular dystrophy involve the protein folding activity of rRNA and are reduced by 6-aminophenanthridine and guanabenz. EMBO Molecular Medicine 3(1): 35-49 (DOI: 10.1002/emmm.201000109)
2.) A Buttstedt, R Winter, M Sackewitz, G Hause, FX Schmid, E Schwarz (2010): Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation. PLoS ONE 5(11): e15436 (DOI: 10.1371/journal.pone.0015436)
1.) A Hauburger, S von Einem, GK Schwaerzer, A Buttstedt, M Zebisch, M Schräml, P Hortschansky, P Knaus, E Schwarz (2009): The pro-form of BMP-2 interferes with BMP-2 signalling by competing with BMP-2 for IA receptor binding. FEBS Journal 276(21): 6386-6398 (DOI: 10.1111/j.1742-4658.2009.07361.x)
- since 2017: Open Topic Postdoc, Technische Universität Dresden, B CUBE
- 2013-2017: Research associate, Martin-Luther-Universität Halle-Wittenberg, Molecular Ecology, DFG research grant ‘The role of the major royal jelly proteins (MRJPs) for caste differentiation in the honeybee Apis mellifera’
- 2012-2013: Postdoctoral researcher, Universitatea de Stiinte si Medicina Veterinaria Cluj-Napoca (Romania), ERDF project RoBeeTech ‘Romanian Bee Technology’
- 2007-2011: PhD student, Martin-Luther-Universität Halle-Wittenberg, Institute of Biotechnology, DFG Research Training Group GRK1026
- 2002-2007: Studies of Biology, Martin-Luther-Universität Halle-Wittenberg
- 2011: Dr. rer. nat.: Martin-Luther-Universität Halle-Wittenberg, Institute of Biotechnology, Prof. Elisabeth Schwarz, Thesis: Influence of the polypeptide environment on fibril formation of an amyloidogenic peptide.
- 2007: Diploma (Biology): Martin-Luther-Universität Halle-Wittenberg, Institute of Biotechnology, Prof. Elisabeth Schwarz, Thesis: Analysis of the binding of the pro-form of bone morphogenetic protein-2 (proBMP-2) to noggin, an antagonist of the mature growth factor (BMP-2).
Technische Universität Dresden: Zukunftskonzept
Program: Exzellenzinitiative des Bundes und der Länder
Coordinator: Technische Universität Dresden
Project duration: 11/2017 - 10/2019
DFG: The role of major royal jelly proteins for caste determination in the honey bee
Coordinator: Martin-Luther-Universität Halle-Wittenberg
Reference Number: MO373/32-1
Project duration: 11/2014 - 03/2018
Martin-Luther-Universität: Prorektorat für Forschung und wissenschaftlichen Nachwuchs
Program: Postdoc-Förderung für Wissenschaftlerinnen der Martin-Luther-Universität
Coordinator: Martin-Luther-Universität Halle-Wittenberg
Project duration: 07/2013 - 06/2014
ERDF: RoBeeTech - Romanian High Competence Scientific Center in Bee Biotechnology
Program: European Regional Development Fund
Coordinator: Universitatea de Stiinte Agricole si Medicina Veterinara Cluj-Napoca
Reference Number: POS CCE 206/20.07.2010
Project duration: 01/2012 - 05/2013
DFG: Conformational transitions in macromolecular interactions
Coordinator: Martin-Luther-Universität Halle-Wittenberg
Reference Number: GRK 1026
Project duration: 01/2008 - 03/2011