Honey-bee

Although the honey bee s sting is unpleasant, this tiny creature is crucial to the world s agricultural economy. Honey bees produce more than jjilOO million worth of honey each year, and, more importantly, the pollination of numerous plants by honey bees is responsible for the production of i20 billion worth of crops in the United States alone. 

In the body, this reaction is reversed by the enzyme sucrase. This occurs in digestion, which makes glucose and fructose available for absorption into the blood. Honey bees also carry an enzyme that can hydrolyze sucrose. Honey consists mostly of a 1 1 mol mixture of glucose and fructose with a small amount of unreacted sucrose. 

As pesticides are applied, large numbers of honey bees and wild bees are poisoned resulting in not only a diminished honey crop, but perhaps more important, reduced crop pollination that is vital to agricultural production (51). The estimated yearly cost of reduced pollination and reduced honey production is about 230 million (Pimentel, D., in manuscript). 

Thompson, H.M. and Mans, C. (2007). The relevance of sublethal effects in honey bee testing for pesticide risk assessment. Pest Management Science 63, 1058-1061. 

In one synthesis of the queen substance of honey bees (9) (cf p ) the double bond is derived from an... 

Muller U, Helbling A, Bischof M Predictive value of venom-specific IgE, IgG and IgG subclass antibodies in patients on immunotherapy with honey bee venom. Allergy 1989 44 412-418. 

Fig. 2. Species of Hymenoptera responsible for systemic allergic reactions (a) honey bee A. mellif-era), (b) bumble bee (Bombus spp.j, (c) wasp, in the USA yellow jacket (Vespula spp.j, (d) European paper wasp (P. gallicus), (e) European hornet (V. crabro), and (f) Australian jack jumper ant (M. pilo-sula) [by courtesy of Dr. S.G. Brown, Perth, Australia]. 

Venom collection is done by electrostimulation in honey bees [8] and by venom sac extraction in vespids [9]. While electrostimulation results in pure venom, venom sac extracts may be contaminated by some body proteins. The amoimt of venom injected by a sting varies from 50 to 140 pg dry weight for the honey bee, but was estimated to be much lower in vespids 1.7-3.1 pg for Vespula, 2.4-5 pg for Dolichovespula, and 4.2-17 pg for Polistes [10]. 

Bumble bee venom contains also a phospholipase A2 with partial identity to bee venom phospholipase Aj and a protease, but no melittin. Instead there are several small peptides called bombolitins [9]. There is limited cross-reactivity between honey bee and bumblebee venoms [2]. 

A number of allergens from both honey bee and vespid venoms have been cloned and expressed by either Escherichia coli or baculovirus-infected insect cells (table 1) phospholipase Aj [20], hyaluronidase [21], acid phosphatase [13] and Api m6 [14] from honey bee venom, as well as antigen 5 [22], phospholipase A and hyaluronidase [23] from vespid venom, and dipeptidylpeptidases from both bee and Vespula venoms [15, 16]. Their reactivity with human-specific IgE antibodies to the respective allergens has been documented [11-16, 22, 23] and their specificity is superior... 

The natural history of Hymenoptera venom anaphylaxis, that is the risk to develop anaphylaxis again when re-stung, has been analyzed in several prospective studies (table 3) [35-37], and in placebo or whole-body extract treated controls of prospective studies on venom immunotherapy [38-40]. It is higher in patients with a history of severe as compared to mild systemic anaphylactic reactions, and in honey bee than in vespid venom-allergic patients - most likely because of the smaller and less constant amoimt of venom applied by vespids [10,41]. A short interval between two stings increases the risk of anaphylaxis [25], but severe anaphylaxis may occur again even after intervals of 10-20 years or more. 

Sting provocation tests are often considered to be the gold standard, although they are less reliable in vespids than in honey bees [35-37, 41, 43]. They are commonly used to assure the efficacy of venom immunotherapy, but are generally considered as unethical in untreated patients with a history of venom anaphylaxis. 

Grunwald T, Bockisch B, Spillner E, Ring J, Brede-horst R, Ollert M Molecular cloning and expression and expression in insect cells of honey bee venom allergen acid phosphatase (Api m3). J Allergy Clin Immunol 2006 117 848-854. 

Nielsen J. Haeberli G Hymenoptera venom allergy analysis of double positivity to honey bee and Vespula venom by estimation of IgE antibodies to 38 species-specific major allergens Api ml and Ves v5. Allergy 2009 64 543-548. 

Muller UR, Helbling A, Berchtold E Immunotherapy with honey bee and yellow jacket venom is different regarding efficacy and safety. J Allergy Clin Imm- 48 unol 1992 89 529-535. 

Maly FE, Marti-Wyss S, Blumer S, Cuhat-Stark I, Wiithrich B Mononuclear blood cell sulfidoleukot-riene generation in the presence of interleukin-3 and whole blood histamine release in honey bee and yellow jacket venom allergy. J Investig Allergol Clin Immunol 1997 7 217-224. 49... 

Muller UR, Jutel M, Reimers A, Zumkehr J, Huber C, Kriegel C, Steiner U, Haeberli G, Akdis M, Helbling A, Schnyder B, Blaser K, Akdis C Clinical and immunologic effects of H1 antihistamine preventive medication during honey bee venom immunotherapy. J Allergy Clin Immunol 2008 122 1001-1007. 

Andrada, A. C. and Telleria, M. C. (2005). Pollen collected by honey bees (Apis mellifera L.) from south of Calden district (Argentina) Botanical origin and protein content. Grana 44, 115-122. 

Coffey, M. F. and Breen, J. (1997). Seasonal variation in pollen and nectar sources of honey bees in Ireland. J. Apicult. Res. 36, 63-76. 

Nabors, R. A. (1997). Trapping pollen collection of the honey bee Apis mellifera L. to determine pollen flow periods. Am. Bee J. 137, 215-216. 

Pearson, W. D. and Braiden, V. (1990). Seasonal pollen collection by honey bees from grass/ shrub highlands in Canterbury, New Zealand. /. Apicult. Res. 29, 206-213. 

Both compounds show about the same degree of activity toward red ants and honey bees, but DDT is superior against red scale crawlers and greenhouse thrips. 

Premier, C., Mach, L., Glossl, J. and Marz, L. (1992) The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of al,3-fucosylation of the asparagine-bound IV-acetylglucosamine. Bio chemicalJournal 284, 377-380. 

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