Bee and Wasp Sting Reactions in Current Beekeepers

Annila, Ilkka; Karjalainen, E Sakari; Annila, P.; Kuusisto, P

doi:10.1016/s1081-1206(10)63342-x

Cited by 52 publications

(60 citation statements)

References 26 publications

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“…As per the literature, bee venom extracted from the stings of Apis mellifera has been widely used medicinally in Europe for the treatment of rheumatic diseases. During ancient period, healers have practiced apitherapy with respect to honeybee products that are used for various curative purposes [2][3][4][5][6]. As per the literature, researchers focused or explored the potential of bee venom extracted from stings for treating a wide variety of conditions from acute tendonitis to chronic back pain to rheumatoid arthritis [1].…”

Section: Discussionmentioning

confidence: 99%

“…arthritis, multiple sclerosis, diseases of the central and peripheral nervous system, heart and blood system, skin diseases and other diseases [1][2][3]. In general, honeybee venom is generally produced by two glands which is associated with sting apparatus of worker and queen bees.…”

Section: Introductionmentioning

confidence: 99%

“…As per the literature, most active component that is present in major amount of bee venom i.e, mellitin which showed antimicrobial activity [6][7]. Among many species of insects belongs to the Phylum Arthropoda, only few of them have the ability to defend themselves with a sting or venom injection during stinging [3,8]. Most of these insects that can sting which represents the members of the order Hymenoptera (includes ants, wasps and bees).…”

Section: Introductionmentioning

confidence: 99%

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Anti-inflammatory Activity of Sting Protein from Apis mellifera

Shah¹,

Gupta²,

Karne³

et al. 2017

IJLSSR

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ABSTRACT-The objective of our study is to determine its anti-inflammatory potential of protein extracted from the stings of honey bee (Apis mellifera). In this study, protein extracted from the stings of Apis mellifera using Tris HCl/ice cold acetone and determined through Nano drop method and then determined its Da protein using SDS-PAGE. In addition, indirect ELISA was performed using rubella vaccine as coating antigen and determined its antibody titre using variable concentration of sting protein (15.62-250 µg) and also determined its activity on human whole blood for determining total cellular content and proliferation against rubella vaccine antigen. The results showed that protein from stings of Apis mellifera showed drastic declined in antibody titre at higher doses but there is slightly enhancement in antibody titre, total cellular content and proliferations at lower concentration as compared to control and rubella vaccine (standard).Overall, this study suggest that stings protein of Apis mellifera showed anti-inflammatory potential against rubella vaccine antigen.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Anti-inflammatory Activity of Sting Protein from Apis mellifera

Shah¹,

Gupta²,

Karne³

et al. 2017

IJLSSR

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“…Members of the Hymenoptera order are of particular importance because they are nearly ubiquitous in nature (Pasaoglu et al, 2006;Valenta, 2002;WHO, 2001;Neugut et al, 2001;Annila et al, 1996), and their stings may cause life-threatening allergic reactions (Steen at al., 2005). Stings from bees, wasps, and ants produce a variety of clinical and histological manifestations.…”

Section: Introductionmentioning

confidence: 99%

Design of a Modern Liposome and Bee Venom Formulation for the Traditional VIT-Venom Immunotherapy

Silva

Moura²,

Ramos

et al. 2008

Journal of Liposome Research

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Traditional venom immunotherapy uses injections of whole bee venom in buffer or adsorbed in Al (OH) 3 in an expensive, time-consuming way. New strategies to improve the safety and efficacy of this treatment with a reduction of injections would, therefore, be of general interest. It would improve patient compliance and provide socio-economic benefits. Liposomes have a long tradition in drug delivery because they increase the therapeutic index and avoid drug degradation and secondary effects. However, bee venom melittin (Mel) and phospholipase (PLA 2 ) destroy the phospholipid membranes. Our central idea was to inhibit the PLA 2 and Mel activities through histidine alkylation and or tryptophan oxidation (with pbb, para-bromo-phenacyl bromide, and/or NBS-N-bromosuccinimide, respectively) to make their encapsulations possible within stabilized liposomes. We strongly believe that this formulation will be nontoxic but immunogenic. In this paper, we present the whole bee venom conformation characterization during and after chemical modification and after interaction with liposome by ultraviolet, circular dichroism, and fluorescence spectroscopies. The PLA 2 and Mel activities were measured indirectly by changes in turbidity at 400 nm , rhodamine leak-out, and hemolysis. The native whole bee venom (BV) presented 78.06% of a-helical content. The alkylation (A-BV) and succynilation (S-BV) of BV increased 0.44 and 0.20% of its a-helical content. The double-modified venom (S-A-BV) had a 0.74% increase of a-helical content. The BV chemical modification induced another change on protein conformations observed by Trp that became buried with respect to the native whole BV. It was demonstrated that the liposomal membranes must contain pbb (SPC:Cho:pbb, 26:7:1) as a component to protect them from aggregation and/or fusion. The membranes containing pbb maintained the same turbidity (100%) after incubation with modified venom, in contrast with pbb-free membranes that showed a 15% size decrease. This size decrease Journal of Liposome Research Downloaded from informahealthcare.com by University of Melbourne on 11/17/14 For personal use only.354 Silva et al. was interpreted as membrane degradation and was corroborated by a 50% rhodamine leak-out. Another fact that confirmed our interpretation was the observed 100% inhibition of the hemolytic activity after venom modification with pbb and NBS (S-A-BV). When S-A-BV interacted with liposomes, other protein conformational changes were observed and characterized by the increase of 1.93% on S-A-BV a-helical content andthe presence of tryptophan residues in a more hydrophobic environment. In other words, the S-A-BV interacted with liposomal membranes, but this interaction was not effective to cause aggregation, leak-out, or fusion. A stable formulation composed by S-A-BV encapsulated within liposomes composed by SPC:Cho:pbb, at a ratio of 26:7:1, was devised. Large unilamellar vesicles of 202.5 nm with a negative surface charge (-24.29 mV) encapsulated 95% of S-A-BV. This formulation ca...

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“…Much is known about the risk factors for HVA. Among these factors, the extent of exposure plays a major role, so that some categories of workers (eg beekeepers and gardeners) are at higher risk of sensitisation and clinical manifestations 3. Little is known about the quantitative relevance and relative weight as a risk factor of the different occupations and it is not known if there is a difference in the distribution of the work occupation between individuals with HVA and the general population.…”

mentioning

confidence: 99%