Allergens in bee venom: III. Identification of allergen B of bee venom as an acid phosphatase☆
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Diversity of peptidic and proteinaceous toxins from social Hymenoptera venoms
2018, ToxiconCitation Excerpt :These compounds were identified mainly by using classical proteomic approaches (Hoffman et al., 1976). Furthermore, for decades most of the studies for elucidation HBV composition was aimed at the characterization of the abundant and clinically relevant allergenic proteins (Hoffman et al., 1977; Hoffman, 1977). Consequently, limited information related to none allergenic proteins was available at the time.
A combined proteomic and transcriptomic analysis of slime secreted by the southern bottletail squid, Sepiadarium austrinum (Cephalopoda)
2016, Journal of ProteomicsCitation Excerpt :Although six of our putative toxins completely satisfied all traditional toxin criteria (short (< 150AA), cysteine rich, secreted) several much larger (> 300AA) proteins were included due to strong homology with known large toxins. These larger toxins were homologous to enzymes found from bee venom (acid phosphatase and peptidase S10) [55], snake and bee venom (PLB) [51], and crown-of-thorns starfish (DNAse II) [54]. Three proteins were included in our list purely on the basis of their sequence properties but without any homology to known toxins.
Molecular characterization of a venom acid phosphatase from the Asiatic honeybee Apis cerana
2016, Journal of Asia-Pacific EntomologyCitation Excerpt :Acid phosphatase, an enzyme component of bee venom, is an enzyme that hydrolyzes phosphomonoesters at acidic pHs (Hoffman, 1977; Marz et al., 1983; Barboni et al., 1987; Peiren et al., 2005, 2008; de Abreu et al., 2010). Previous studies have demonstrated that the acid phosphatase from European honeybee Apis mellifera (Hymenoptera: Apidae) venom is an allergen (Api m 3) that releases histamine and induces wheal and flare reactions in sensitized humans (Hoffman, 1977; Barboni et al., 1987; Grunwald et al., 2006). Molecular and enzymatic properties of A. mellifera venom acid phosphatase have been reported, including gene structure, expression, and functional features (Soldatova et al., 2000; Grunwald et al., 2006).
Molecular characterization of a venom acid phosphatase Acph-1-like protein from the Asiatic honeybee Apis cerana
2014, Journal of Asia-Pacific EntomologyCitation Excerpt :Bee venom is considered a rich source of pharmacologically active components, and venom components have been intensively studied as potential compounds on which to base novel pharmaceuticals (Heinen and da Veiga, 2011; Son et al., 2007). Acid phosphatase is also a bee venom component (Barboni et al, 1987; de Abreu et al., 2010; Hoffman, 1977; Marz et al., 1983; Peiren et al., 2005, 2008) and belongs to a group of enzymes that hydrolyze phosphomonoesters at acidic pH. European honeybee Apis mellifera venom acid phosphatase (Acph-1) is an allergen that is able to release histamine and induce wheal and flare reactions in sensitized humans (Barboni et al, 1987; Grunwald et al., 2006; Hoffman, 1977). The gene structure and functional features of A. mellifera venom acid phosphatase have been reported (Grunwald et al., 2006; Soldatova et al., 2000), and a three-dimensional model of A. mellifera venom acid phosphatase has provided a basis for investigating structure–function relationships (Georgieva et al., 2009).
Detection of Honeybee Venom in Envenomed Tissues by Direct MALDI MSI
2009, Journal of the American Society for Mass Spectrometry
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Mr. Charles Mraz and Mr. Calvin Davis rendered invaluable assistance in obtaining the insect venoms and venom sacs.