Effect of Application of Probiotic Pollen Suspension on Immune Response and Gut Microbiota of Honey Bees (Apis mellifera).

Although the use of probiotic bacteria in invertebrates is still rare, scientists have begun to look into their usage in honey bees. The probiotic preparation, based on the autochthonous strain Lactobacillus brevis B50 Biocenol™ (CCM 8618), which was isolated from the digestive tracts of healthy bees, was applied to the bee colonies in the form of a pollen suspension. Its influence on the immune response was determined by monitoring the expression of genes encoding immunologically important molecules in the honey bee intestines.

Major royal jelly proteins as markers of authenticity and quality of honey.

Until now, the properties of honey have been defined based exclusively on the content of plant components in the nectar of given plant. We showed that apalbumin1, the major royal jelly (RJ) protein, is an authentic and regular component of honey. Apalbumin1 and other RJ proteins and peptides are responsible for the immunostimulatory properties and antibiotic activity of honey.

Structure and antimicrobial activity relationship of royalisin, an antimicrobial peptide from royal jelly of Apis mellifera.

Royalisin is a 5.5-kDa antibacterial peptide isolated from the royal jelly of the honeybee (Apis mellifera). The antimicrobial activity of royalisin against fungi, Gram-positive and Gram-negative bacteria has been revealed.

New criterion for evaluation of honey: quantification of royal jelly protein apalbumin 1 in honey by ELISA.

The 55 kDa major protein of royal jelly, named apalbumin 1, is an authentic protein of honey and pollen pellet, and for its quantification an enzyme-linked immunosorbent assay (ELISA) was developed using specific polyclonal anti-apalbumin 1 antibody. The limit of detection for apalbumin 1 was 2 ng mL(-1). The floral honeys contained apalbumin 1 as follows: acacia, 0.

Towards functional proteomics of minority component of honeybee royal jelly: the effect of post-translational modifications on the antimicrobial activity of apalbumin2.

This study illustrates multifunctionality of proteins of honeybee royal jelly (RJ) and how their neofunctionalization result from various PTMs of maternal proteins. Major proteins of RJ, designated as apalbumins belong to a protein family consisting of nine members with M(r) of 49-87 kDa and they are accompanied by high number of minority homologs derived from maternal apalbumins. In spite of many data on diversity of apalbumins, the molecular study of their individual minority homologous is still missing.

Isolation and characterization of chitin from bumblebee (Bombus terrestris).

Insect chitin possessing shell-like structure was prepared from the bumblebee corpses by a consequent treatment with 1M HCl and 1M NaOH. The bumblebee chitin was compared with crustacean (shrimp) chitin by using elemental analysis, Fourier-transform infrared (FT-IR) and solid-state (13)C cross-polarization magic angle spinning nuclear magnetic resonance (CP/MAS)-NMR spectroscopy and confocal microscopy. Both chitins (bumblebee and shrimp) exhibited identical spectra, while the bumblebee chitin had a 5% lower degree of acetylation and was characterized by a fine membrane texture.

Stimulation of TNF-alpha release by fungal cell wall polysaccharides.

Carboxymethylated derivatives were prepared from the (1-->3)-beta-D-glucan isolated from the cell wall of baker's yeast Saccharomyces cerevisiae and from the chitin-glucan complex of the mycelium of the industrial filamentous fungus Aspergillus niger. The polysaccharides were applied to peritoneal mouse macrophages and after a 2-h incubation the release of TNF-alpha by the stimulated macrophages was measured using an enzyme-linked immunosorbent assay. As the third polysaccharide stimulant, a water-soluble derivative of chitin was assayed and the observed cytokine release was compared with the control experiment.

The immunostimulatory effect of the recombinant apalbumin 1-major honeybee royal jelly protein-on TNFalpha release.

Apalbumin1 (Apa1) is the major royal jelly (RJ) and honey glycoprotein having various biological properties. We have previously demonstrated that Apa1 is a regular component of honey and honeybee pollen and stimulates macrophages to release tumor necrosis factor alpha (TNFalpha). The recombinant Apa1 (rApa1) and its four recombinant protein fragments derived on the basis of partial tryptic products of Apa1 were prepared by heterologous expression in Escherichia coli BL21-CodonPlus(DE3)-RIL.

Immunochemical approach to detection of adulteration in honey: physiologically active royal jelly protein stimulating TNF-alpha release is a regular component of honey.

The presence of royal jelly (RJ) proteins in honey collected from nectars of different plants, origin, and regions and in honeybee's pollen was detected by Western-blot analysis using polyclonal antibodies raised against water-soluble RJ-proteins. The most abundant RJ-protein in honeybee products corresponded to a 55 kDa protein. The N-terminal amino acid sequence of 55 kDa protein was N-I-L-R-G-E.

Apisimin, a new serine-valine-rich peptide from honeybee (Apis mellifera L.) royal jelly: purification and molecular characterization.

A peptide named apisimin was found in honeybee (Apis mellifera L.) royal jelly (RJ). N-terminal sequencing showed that this peptide corresponded to the sequence of a cDNA clone isolated from an expression cDNA library prepared from heads of nurse honeybees.