Venom of bee

Histamine is found in most of the tissues, present in various biological fluids. In most tissues, histamine exists in bound form in granules, in mast cells or basophils. These mast cells are especially rich at sites of potential tissue injury i.e. skin, lungs, liver, GIT etc. and is unevenly distributed. It is also present in many venoms (of bees wasps), bacteria and plant tissues. 

Formic acid (also called methanoic acid) is the simplest carboxylic acid. Its chemical formula is HCOOH or HCO2H. It is an important intermediate in chemical synthesis and occurs naturally, most notably in the venom of bee and ant stings. In fact, its name comes from the Latin word for aat, formica, referring to its early isolation by the distillation of ant bodies. Esters, salts, and the anion derived from formic acid are referred to as formates. 

As a general trend, the venoms of parasitic wasps possess a much more complex array of high molecular weight proteins than the venoms of bees and predatory wasps. The structures of a number of comparatively small proteins have been reported from honey bee venom, such as melittin (31), apamin (32), and hyaluronidase (33). The venom of predatory wasps has been reported to contain small components such as kinins (17). 

Despite the fact that a definite decrease in IgE antibody levels and IgE-mediated skin sensitivity normally requires several years of SIT, most patients are protected against bee stings already at an early stage of bee venom-SIT. The reason for this is that effector cells of allergic inflammation, such as mast cells, basophils and eosinophils. 

Philadelphia, Saunders, 1992, pp 13-37. Jutel M, Muller UM, Pricker M, Rihs S, Pichler W, Dahinden C Influence of bee venom immunotherapy on degranulation and leukotriene generation in human blood basophils. Clin Exp Allergy 1996 26 112-118. 

Muller U, Akdis CA, Fricker M, Akdis M, Blesken T, Bettens F, Blaser K Successful immunotherapy with T-cell epitope peptides of bee venom phosphohpase A2 induces specific T-cell anergy in patients allergic to bee venom. J Allergy Chn Immunol 1998 101 747-754. 

Sting. The venoms of both bees and wasps contain fonnic acid as well, among other toxic chemicals. 

The other phospholipids can be derived from phosphatidates (residue = phosphatidyl). Their phosphate residues are esterified with the hydroxyl group of an amino alcohol choline, ethanolamine, or serine) or with the cyclohexane derivative myo-inositol. Phosphatidylcholine is shown here as an example of this type of compound. When two phosphatidyl residues are linked with one glycerol, the result is cardiolipin (not shown), a phospholipid that is characteristic of the inner mitochondrial membrane. Lysophospholipids arise from phospholipids by enzymatic cleavage of an acyl residue. The hemolytic effect of bee and snake venoms is due in part to this reaction. 

The venoms of many kinds of bees, wasps, and hornets (the genera Vespa, Polistes, Vespula, Ropalidia, etc.) contain biogenic amines such as histamine (136), serotonin (141), and catecholamines in addition to polyamines such as putrescine (111), spermidine (110), and spermine (112) (Table VIII). The biogenic amines in the venoms act as the main pain-producing principles 46). The contents of these amines in the venom may affect the severity of pain production, edematous reaction of the skin, or increase in skin permeability by stings of these insects. Consequently these amines act as toxins for their defense, together with acetylcholine, enzymes, and peptides 47). 

Channel-forming toxins and antibiotics. Some of the bacterial toxins known as colicins (Box 8-D) kill susceptible bacteria by creating pores that allow K+ to leak out of the cells. One part of the complement system of blood (Chapter 31) uses specific proteins to literally punch holes in foreign cell membranes. Mel-litin, a 26-residue peptide of bee venom,372 373 as well as other hemolytic toxins and antibiotic peptides of insects, amphibians, and mammals (Chapter 31) form amphip-athic helices which associate to form voltage-dependent anion-selective channels in membranes.374-377... 

The structures of nine of these compounds were determined by spectroscopic methods, while those of the 14 remaining materials were established by GC-MS only. The compounds can be classified into four types (A to D) the 1,2,4-trithiolanes (145-154), 1,2,4,5-tetrathianes (155-157), 1,2,3,5,6-pentathiepanes (158-163), which are all generally quite stable compounds, and the monoalkyl-substituted polysulfides (164-167), which tend to disproportionate into sulfur and disubstituted cyclic polysulfides. These compounds are structurally related to the cyclic polysulfide compounds reported from red alga Chondria californica in 1976 [136] and to compound 168 (3-hexyl-4,5-dithiacycloheptanone) reported from the brown algae of the Dictyopteris genus in 1971 [137]. The latter compound has more recently been found to be a potent inhibitor of bee venom-derived phospholipase A2 (PLA2) [138]. 

Shea and colleagues [109-111] added an exciting contribution to this field They created molecular imprints for the peptide melittin, the main component of bee venom, in polymer nanoparticles, resulting in artificial antibody mimics that can be used for the in vivo capture and neutralization of melittin. Melittin is a peptide comprising 26 amino acids which is toxic because of its cytolytic activity. Shea and colleagues strategy was to synthesize cross-linked, acrylamide-based MIP nanoparticles by a process based on precipitation polymerization using a small amount of surfactant. To maximize the specificity and the affinity for melittin, a number of hydrophilic monomers were screened for complementarity with the template. The imprinted nanoparticles were able to bind selectively the peptide with an apparent dissociation constant of Ax>app > 1 nM [109]. 

Anionic peptides are almost inactive in the presence of serum because they have the disadvantage of binding to serum proteins. Amphiphilic basic peptides, such as melittin (GIGAVLKVLTTGLPALISWIKRKRQQ-NH2), isolated from the venom of the European honey bee Apis mellifera (Dempsey, 1990) and K5, the... 

Animal products constitute 20% of homeopathic remedies and are collected from whole animals or their parts. Apis mellifica is prepared from the whole honey bee, Cantharis from the dried powder of the beetle, Cantharis vasicata, Sepia officinalis from the ink gland of the cuttle fish, Lachesis from the venom of the bush master snake and Tarantula hispanica from the poisonous Spanish spider (Cook, 1988). Lac caninum is prepared from dog s milk and Calcarea carbonica from oyster shell. 

KB Glaser, RS Jacobs. Inactivation of bee venom phospholipase A2 by manoalide. A model based on the reactivity of manoalide with amino acids and peptide sequences. Biochem Pharmacol 36 2079-2086, 1987. 

Kyaluronidase from bee venom has about die same substrate specificity as snake hyalunmidase [19]. Venom of social wasps was found to contain high levels of hyahuonidase activity, whereas venotn from ants contains low levels of activity r201. Lizard venom contains a hyalunmidase that acts almost specific an hyaluronan, i ., it has no activity toward chondroitin-b-suifale, dermatan sulfate, or heparin and only weak activity toward chondroitin suifaie [21J. 

Table 1 presents a survey of hyalunmidase activity in the venom of several animal species. Transgiycosyiation properties have been observed with hyal-uronidase from snake venom Cmtalus terrificus) [8], but not with hyalunmidase from bee venom [19]. 

One of the most well-known examples of insect toxins is melittin, a bee venom peptide with potent haemolytic activity. Melittin adopts an a-helical conformation, and has been extensively characterised using a range of techniques, including both solution- and solid-state NMR spectroscopy.176 Some helical peptides with antimicrobial activity have also been found in wasps, such as eumenine mastroparan-AF (EMP-AF-NH2) from the venom of the solitary wasp Anterhynchium flavormarginatum micado,177 and the cecropins found in the haemolymph of Hyalophora cecropia.178 Several of these peptides have cytotoxic activity and are potential anticancer agents.179... 

Simple proteins can also act as potent agents for cell destruction. The main active component of bee sting venom is a protein composed of 26 amino acids called mellitin which adopts a helical, and potentially membrane puncturing, conformation. The protein is also an inhibitor of bacteria that cause Lyme disease and suppresses infections caused by Candida albicans, Mycoplasma hominis and Chlamydia tracomatis. 

All the substances that cause these unpleasant and possibly lethal effects are chemicals, albeit manufactured by a plant, micro-organism, or animal. They may be simple irritant chemicals such as the formic acid in ant bites (formica is the Latin for ant), or complex protein molecules such as is found in bee venom. Proteins are relatively large molecules, one of the main building blocks of the body and also the main component of enzymes (biological catalysts). The venom of animals such as snakes often contains enzymes which degrade flesh. Mushrooms and toadstools are another source of poisonous chemicals, for example the Death Cap mushroom found in Britain which can be lethal if eaten. 

Even relatively simple peptides can have important biological functions. Bradykinin, for example, is a peptide hormone composed of nine amino acids. It stimulates smooth muscle contraction, dilates blood vessels, and causes pain. Bradykinin is a component of bee venom. 

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