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.

Bee Venom May Help Treat Amyotrophic Lateral Sclerosis (ALS)

As it's frequently misdiagnosed for MS, it's really no surprise this research resembles results found for Multiple Schlerosis...  

Melittin Restores Proteasome Function in an Animal Model of ALS
J Neuroinflammation, 2011 Jun 20;8(1):69

Amyotrophic lateral sclerosis (ALS) is a paralyzing disorder characterized by the progressive degeneration and death of motor neurons and occurs both as a sporadic and familial disease.

Mutant SOD1 (mtSOD1) in motor neurons induces vulnerability to the disease through protein misfolding, mitochondrial dysfunction, oxidative damage, cytoskeletal abnormalities, defective axonal transport- and growth factor signaling, excitotoxicity, and neuro-inflammation.

Melittin is a 26 amino acid protein and is one of the components of bee venom which is used in traditional Chinese medicine to inhibit of cancer cell proliferation and is known to have anti-inflammatory and anti-arthritic effects.

The purpose of the present study was to determine if melittin could suppress motor neuron loss and protein misfolding in the hSOD1G93A mouse, which is commonly used as a model for inherited ALS. Meltittin was injected at the ZuSanLi (ST36) acupuncture point in the hSOD1G93A animal model.

Melittin-treated animals showed a decrease in the number of microglia and in the expression level of phospho-p38 in the spinal cord and brainstem. Interestingly, melittin treatment in symptomatic ALS animals improved motor function and reduced the level of neuron death in the spinal cord when compared to the control group.

Furthermore, we found increased of alpha-synuclein modifications, such as phosphorylation or nitration, in both the brainstem and spinal cord in hSOD1G93A mice. However, melittin treatment reduced alpha-synuclein misfolding and restored the proteasomal activity in the brainstem and spinal cord of symptomatic hSOD1G93A transgenic mice.

Our research suggests a potential functional link between melittin and the inhibition of neuroinflammation in an ALS animal model.