Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom

Lima, Paulo Renato Marques de; Brochetto-Braga, Márcia Regina; Chaud-Netto, José

doi:10.1590/s0104-79302000000100004

Cited by 19 publications

(13 citation statements)

References 13 publications

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“…It is also well known that some enzymes fulfill detoxification functions, because they take part in the metabolism of pesticides (Shi et al, 2009). Another group is represented by a proteolytic system that catalyzes the hydrolytic degradation of peptide bonds and takes part in many biological processes (Costa & Cruz-Landim, 2005;Frączek et al, 2013;Lima et al, 2000;Strachecka et al, 2008Strachecka et al, , 2010Walter & Clélia, 1994). Many such proteins are involved in the immunological response and not in the functioning of digestive enzymes (Ji, Wang, Guo, Hartson, & Jiang, 2004;Jiang et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

The influence of sublethal doses of imidacloprid on protein content and proteolytic activity in honey bees (Apis mellifera L.)

Wilde

Frączek

Siuda

et al. 2016

Journal of Apicultural Research

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The effect of sublethal doses of imidacloprid on protein content and activity of proteases on honey bees was analyzed. The study was conducted in three experimental groups: colonies from groups BE-5 and BE-200 were contaminated with 5 and 200 ppb of imidacloprid, respectively, via their food supply (syrup and pollen), while group BE was used as control (untreated). Bee samples were collected 3 and 10 weeks after feeding started. Protein concentration in bee tissue extracts was analyzed with reference: (a) to the dose of imidacloprid; and (b) duration of exposure to the chemical. The average quantity of protein content was significantly higher at the 3-week interval than in the 10-week interval and the bees from control colonies (BE) had significantly higher protein contents than contaminated bees (BE-5 and BE-200), even 3 weeks after feeding with imidacloprid started. Similarly, the activity of proteolytic enzymes (proteases) was found to be dependent on the dose of imidacloprid used, compared to bees from control colonies showing significantly higher activity.Influencia de las dosis subletales de Imidacloprid en el contenido de proteína y la actividad proteolítica en las abejas melíferas (Apis mellifera L.)Se ha analizado el efecto de las dosis subletales de imidacloprid en el contenido de proteínas y la actividad de las proteasas en las abejas melíferas. El estudio se realizó en tres grupos experimentales: las colonias de los grupos de BE-5 y BE-200 se contaminaron con 5 y 200 ppb de imidacloprid, respectivamente, a través del alimento suministrado (jarabe y polen), mientras que el grupo SER se utilizó como control (sin tratar). Se recogieron muestras de abejas en las semanas 3 y 10 después del comienzo de la alimentació n. La concentració n de proteína en extractos de tejido de abejas se analizó en relació n con: a) la dosis de imidacloprid; y b) la duració n de la exposició n a la sustancia química. La cantidad promedio del contenido de proteína fue significativamente mayor en el intervalo de 3 semanas que en el intervalo de 10 semanas y las abejas de las colonias control (BE) tuvieron un contenido de proteína significativamente más alto que las abejas contaminadas (BE-5 y BE-200), incluso 3 semanas después de que comenzara la alimentació n con imidacloprid. Del mismo modo se encontró que la actividad de las enzimas proteolíticas (proteasas) depende de la dosis de imidacloprid usada, en comparació n con las abejas de colonias de control que muestran una actividad significativamente más alta.

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Section: Discussionmentioning

confidence: 99%

The influence of sublethal doses of imidacloprid on protein content and proteolytic activity in honey bees (Apis mellifera L.)

Wilde

Frączek

Siuda

et al. 2016

Journal of Apicultural Research

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“…The presence of different molecules in the venom, including phospholipase A2, hyaluronidase, melittin, apamine [37][38][39][40] , and, most recently, a serine protease-like protein studied by Lima et al 41 , may contribute to skin necrosis at the sting site. Such necrosis has frequently occurred and has been reported by most studies in Brazil [33][34][35][36][37][38][39][40][41][42][43][44][45] . The presence of rhabdomyolysis characterized by fiber eosinophilia, vacuolization, and absence of nuclei can be seen in Figure 1B.…”

Section: Anatomopathological Examinationmentioning

confidence: 99%

Africanized honeybee stings: how to treat them

Almeida

Olivo

Mendes

et al. 2011

Rev. Soc. Bras. Med. Trop.

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Introduction:In 1956, Africanized honeybees (AHB) migrated from Brazil to other regions of the Western Hemisphere, including South, Central, and North America, except for Canada. Despite being productive, they are highly aggressive and cause fatal accidents. This study aimed to evaluate patients at the Clinical Hospital of Botucatu Medical School (HC-FMB) and to propose treatment guidelines. Methods: From 2005 to 2006, the clinical and laboratorial aspects of 11 patients (7 male and 4 female) and the anatomopathological aspects of one patient who had died in 2003 were analyzed. Results: The age of the surviving patients varied from 5 to 87 years, with a mean of 42.5 years. The majority of accidents occurred in the afternoon, and the number of stings ranged from 20 to 500. The principal signs and symptoms were pain and local inflammatory signs, nausea, tachycardia, and vomiting. Biochemical findings presented increased levels of creatine phosphokinase, lactate dehydrogenase, and aspartate/alanine aminotransferase. An 11-year-old male patient died upon entering the attic of a two-storey building where he was attacked by a swarm, receiving more than 1,000 stings. He was sent to HC-FMB where he was treated, but he died 24h later. Observed at the autopsy were erythematous-purpuric skin lesions besides necrosis at the sting locations, rhabdomyolysis, focal myocardial necrosis, tubular hydropic degeneration and focal tubular acute necrosis of the kidneys, myoglobinuria, and centrolobular necrosis in the liver. Conclusions: Accidents caused by multiple AHB stings always constitute a medical emergency. As there is no specific antivenom, we have developed guidelines, including first aid, drugs, and the proper removal of stingers.

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“…Proteases play a prominent role in a wide array of physiological processes such as food digestion, blood clotting, embryogenesis, tissue reorganization, defense mechanisms and immune responses (Schoofs and Salzet 2002). Proteolytic enzymes are known to be present in the bee alimentary duct, hemolymph, moult liquid, venom and on the body surface (Terra and Ferreira 1994, Bode et al 1999, Lima et al 2000, Malone et al 2004, Evans et al 2006, Strachecka et al 2011. Up to date, the body-surface proteolytic system of mites has not been analysed.…”

Section: Introductionmentioning

confidence: 99%

Proteolysis on the body surface of pyrethroid-sensitive and resistant Varroa destructor

Strachecka

Borsuk

Olszewski

et al. 2013

Acta Parasitologica

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The aim of this work was to determine the activity of proteases and protease inhibitors sampled from the body surface of taufluvalinate-sensitive and resistant V. destructor. Proteins were isolated from the tau-fluvalinate-sensitive and resistant mites, while mites untreated with tau-fluvalinate constituted the control. Subsequently, the following methodology was applied: protein concentration assay by the Lowry method -as modified by Schacterle and Pollack; assay of proteolytic activity in relation to various substrates (gelatine, haemoglobin, ovoalbumin, albumin, cytochrome C, casein) by the modified Anson method; identification of proteolytic activity in relation to diagnostic inhibitors of proteolytic enzymes (pepstatin A, PMSF, iodoacetamide, o-phenantrolin), using the Lee and Lin method; identification of acidic, neutral and basic protease activities by means of the modified Anson method; electrophoretic analysis of proteins in a polyacrylamide gel for protease detection with the Laemmli method and for protease inhibitor detection with the Felicioli method. The highest value of protein concentration was found in the tau-fluvalinate-sensitive V. destructor, while the highest activity levels of acidic, neutral and alkaline proteases were observed in the tau-fluvalinate-resistant mites. Aspartic, serine, thiolic and metallic proteases were found in the drug-resistant and drug-sensitive Varroa mites. The control samples were found to contain aspartic and serine proteases. In an acidic and alkaline environment, the results revealed a complete loss of inhibitor activities in the in vitro analyses and electrophoresis. Serine protease inhibitor activities (at pH 7.0) were high, especially in the group of tau-fluvalinate-resistant mites.

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Proteolytic activity of africanized honeybee (Apis mellifera: hymenoptera, apidae) venom

Cited by 19 publications

References 13 publications

The influence of sublethal doses of imidacloprid on protein content and proteolytic activity in honey bees (Apis mellifera L.)

The influence of sublethal doses of imidacloprid on protein content and proteolytic activity in honey bees (Apis mellifera L.)

Africanized honeybee stings: how to treat them

Proteolysis on the body surface of pyrethroid-sensitive and resistant Varroa destructor

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