XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

Lectures
PROTEOMICS OF MULTIFUNCTIONAL ROYAL JELLY PROTEINS
Katarína Bíliková and Jozef Šimúth
Department of Molecular Apidology, Institute of Molecular Biology,
SAS, Bratislava
Presented study demonstrated how neofunctionalization results from various posttranslational
modifications of maternal proteins of honeybee royal jelly (RJ). We have purified
a minority protein of RJ, named apalbumin2a. Characterization of apalbumin2a by LC-MALDI
TOF/TOF MS revealed it as a homologue of major basic royal jelly protein apalbumin2,
carrying two fully occupied N-glycosylation sites, one with high-mannose structure,
HexNAc2Hex9, and other carrying complex type antennary structures, HexNAc4Hex3 and
HexNAc5Hex4, while the maternal protein, apalbumin2, contained only high-mannose
N-linked glycans. We have found that apalbumin2a inhibit growth of Paenibacillus
larvae, the primary honeybee pathogen of American foulbrood disease, similarly to RJ
peptide royalisin. In spite of a single gene in honeybee genome for apalbumin2, presence
of various forms of the protein, having different N-terminal sequences could be
a result of specific proteolytic degradation of mature protein, alternative splicing or
heterogonous transcription start sites by „leakage“ of the RNA transcription machinery.
Obtained data call attention for functional plasticity of RJ proteins with potential impact
on fundamental research, namely studies of novel mechanisms of action of antibacterial
proteins, as well as on the field of drug development and therapeutic application of RJ
proteins as antibiotics.
Acknowledgments: This work was supported by Max-Planck Society for Partner Group
of Slovak Academy of Sciences and by 6RP EU-BeeShop No.: 022568.
48 XXII. Biochemistry Congress, Martin