Bee Venom Antimicrobial Peptide Has Anti-Inflammatory Properties

Honey bee products deserve further funds to uncover these important discoveries which continue to elevate the merits of Apitherapy. For example, the statistically low cancer rate found in beekeepers worldwide, not to mention the reports of Bee Venom Therapy in treating numerous conditions ranging from Alzheimer's Disease to Parkinson's Disease and Rheumatoid Arthritis...

Consequences of Alteration in the Leucine Zipper Sequence of Melittin in its Neutralization of Lipopolysaccharide-Induced Pro-Inflammatory Response in Macrophage Cells and Interaction with Lipopolysaccharide

J Biological Chemistry, 2011 Nov 29

Bee venom antimicrobial peptide, melittin, besides showing versatile activity against microorganisms neutralizes lipopolysaccharide (LPS)-induced pro-inflammatory responses in macrophage cells.

However, how the amino acid sequence of melittin contributes in its anti-inflammatory properties is mostly unknown. To determine the importance of the leucine zipper sequence of melittin in its neutralization of LPS-induced inflammatory responses in macrophages and interaction with LPS, anti-inflammatory properties of melittin and its three analogues and their interactions with LPS were studied in detail.

Two of these analogues namely, melittin Mut-1 (MM-1) and melittin Mut-2 (MM-2) possess leucine to alanine substitutions in the single and double heptadic leucine residue(s) of melittin respectively while the third analogue is a scrambled peptide (Mel-SCR) which contains the amino acid composition of melittin with minor rearrangement in its leucine zipper sequence.

Though MM-1 partly inhibited the production of pro-inflammatory cytokines in RAW 264.7 and rat primary macrophage cells in the presence of LPS, MM-2 and Mel-SCR were negligibly active. A progressive decrease in interaction of melittin with LPS, aggregation in LPS and dissociation of LPS aggregates with alteration in the leucine zipper sequence of melittin was observed.

Further, with alteration in the leucine zipper sequence of melittin, these analogues failed to exhibit cellular responses that are associated with neutralization of LPS-induced inflammatory responses in macrophage cells by melittin.

The data indicated a probable important role of the leucine zipper sequence of melittin in neutralizing LPS-induced pro-inflammatory responses in macrophage cells as well as in its interaction with LPS…

Though further studies are required in understanding the role of this motif in these molecules, the data probably indicate that one can design anti-LPS or LPS-binding molecule based on this structural element.

Potent Antibacterial Components of Honey Reviewed

Honeybees continue to perplex medical researchers with something as pure and natural as honey... 

Antibacterial Components of Honey

IUBMB Life, 2011 Nov 17

The antibacterial activity of honey has been known since the 19th century. Recently, the potent activity of honey against antibiotic-resistant bacteria has further increased the interest for application of honey, but incomplete knowledge of the antibacterial activity is a major obstacle for clinical applicability.

The high sugar concentration, hydrogen peroxide, and the low pH are well-known antibacterial factors in honey and more recently, methylglyoxal and the antimicrobial peptide bee defensin-1 were identified as important antibacterial compounds in honey.

The antibacterial activity of honey is highly complex due to the involvement of multiple compounds and due to the large variation in the concentrations of these compounds among honeys. The current review will elaborate on the antibacterial compounds in honey.

We discuss the activity of the individual compounds, their contribution to the complex antibacterial activity of honey, a novel approach to identify additional honey antibacterial compounds, and the implications of the novel developments for standardization of honey for medical applications...

Bee Venom Provides ‘Collective Immunity’ for Hive

a significant finding... Could this explain the consistency of all the bee products to possess antimicrobial properties?... 

Beyond theAntipredatory Defence: Honey Bee Venom Function as a Component of SocialImmunity

Toxicon,2011 Sep 10

The honeybee colonies, with the relevant number of immature brood and adults, andstable, high levels of humidity and temperatures of their nests, result insuitable environments for the development of microorganisms includingpathogens.

Inresponse, honey bees evolved several adaptations to face the increased risks ofepidemic diseases. As the antimicrobial venom peptides of Apis mellifera arepresent both on the cuticle of adult bees and on the nest wax it has beenrecently suggested that these substances act as a social antiseptic device.

Since theuse of venom by honey bees in the context of social immunity needs to be moredeeply investigated, we extended the study of this potential role of the venomto different species of the genus Apis (A. mellifera, Apisdorsata, Apis ceranaand Apis andreniformis) using MALDI-TOF mass spectrometry techniques.

Inparticular we investigated whether (similarly to A. mellifera) the venom isspread over the body cuticle and on the comb wax of these three Asian species.Our results confirm the idea that the venom functions are well beyond theclassical stereotype of defence against predators, and suggest that thedifferent nesting biology of these species may be related to the use of thevenom in a social immunity context.

Thepresence of antimicrobial peptides on the comb wax of the cavity-dwellingspecies and on the cuticle of workers of all the studied species represents agood example of "collective immunity" and a component of the"social immunity" respectively.