Comparison of vespid venoms collected by electrostimulation and by venom sac extraction

Muêller, U.; Reisman, Robert E.; Wypych, John I.; Elliott, W.B.; Steger, R.; Walsh, Stephen R.; Arbesman, Carl E.

doi:10.1016/0091-6749(81)90148-2

Cited by 32 publications

(30 citation statements)

References 18 publications

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“…Further more, the protection is reported to be dose dependent [35,36]. The results of our study indicate that the allergenic po tency of the venoms studied was low, and this can explain why the reaction after immunotherapy with vespid venoms is less intense than with bee venom [13,17]; in addition, the presence of nonvenom protein may induce the appearance of adverse reactions to irrelevant proteins [9,11,15].…”

Section: Discussionmentioning

confidence: 62%

“…The inadequacy of these reagents used for diagnosis [2,4,5] and the treatment failures [1,6,7] led to the determination of the allergenic content of this material and to immunology stud ies [3,8]. The obtention of pure venom and separation and purification of the proteins with allergenic capacity confirm early reports about the inadequacy of the whole-body mate rial extracts [1,7,9], Although expensive, pure bee venom is available for diagnostic and therapeutic purposes [3], How ever, vespid venoms available for clinical use are made by venom sac dissection [10][11][12][13]. It has been reported that the allergenic content of this material is lower than that ob This work was supported in part by Grant No.…”

Section: Introductionmentioning

confidence: 72%

“…Purified bee venom proteins and bee venom are available for diagnostic and therapeutic purposes [3,30], but venom from vespids is more difficult to obtain, and the material available is pro cured by venom sac dissection [10,11]. This material is of lower allergenic potency and contains nonvenom proteins [10][11][12][13]31], In our study, the enzymatic and allergenic properties of different Vespula venoms used for diagnostic and therapeut ic purposes, commercially available VG, and VG venom ob tained by sac dissection were studied and compared with VGP. The hyaluronidase activity of the three venoms stud ied was 52-60% and the phospholipase A|B activity 52-66% of VGP.…”

Section: Discussionmentioning

confidence: 99%

“…This may vary between different insects [10][11][12], Vespid venom for immunotherapeutical purposes represents a mixture of different species [3,[14][15][16][17]. In this study we compare Vespula species venom from different commercial sources used worldwide for di agnosis and immunotherapy and sac dissection Vespula ger manica (VG) venom with pure VG venom obtained by the capillary method.…”

Section: Introductionmentioning

confidence: 99%

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Comparison of Vespula germanica Venoms Obtained from Different Sources

Sánchez

Blanca

Miranda

et al. 1994

Int Arch Allergy Immunol

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This study was carried out to compare the allergenic potency of Vespula germanica (VG) venoms extracted by different methods and commercially available venoms from Vespula species currently used for in vivo and in vitro studies including immunotherapy. Pure VG venom was used as the reference material. Protein content and enzymatic and allergenic properties of all venoms studied were determined by dye stain reagent, hyaluronidase and phospholipase AB enzyme activities, and radioallergosorbent test inhibition studies, respectively. Radioallergosorbent test discs sensitized with commercial and pure VG venom were compared using specific IgE antibodies from subjects allergic to VG venom. The data obtained indicate that there were important differences in the allergenic potency between the Vespula species venoms employed for in vivo and/or in vitro assays, VG venom obtained by sac dissection, and pure VG venom. These results indicate that venoms from Vespula species used for in vitro and in vivo tests have a lower concentration of allergens and contain nonvenom proteins. These data should be taken into account when these vespid venoms are used for diagnostic purposes and also when evaluating immunotherapy studies.

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Section: Discussionmentioning

confidence: 62%

Section: Introductionmentioning

confidence: 72%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Comparison of Vespula germanica Venoms Obtained from Different Sources

Sánchez

Blanca

Miranda

et al. 1994

Int Arch Allergy Immunol

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“…A recent report by Hannan et al [18] suggests that the allergenicity may reside in a phospholipase compo nent of IFAV. Phospholipase A has been shown in other Hymenoptera to be the allergen responsible for allergic reactions to stings [2] although the phospholi pase A components of various venoms are antigenically distinct [ 19]. InCIEstudies performed in our laboratory with venom preparations from a number of Hymen-optera (yellow jacket, white-faced hornet, honeybee, wasp, and yellow hornet) and IFAV, we were unable to demonstrate cross-reactivity between venoms from IFA and other Hymenoptera [unpubl.…”

Section: Discussionmentioning

confidence: 99%

Superiority of Solenopsisinvicta Venom to Whole-Body Extract in RAST for Diagnosis of Imported Fire Ant Allergy

Butcher

deShazo

Ortiz

et al. 1988

Int Arch Allergy Immunol

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RAST determinations using imported fire ant (IFA) whole-body extract (IFAWBE) and venom (IFAV) were performed with the sera of 29 sting-sensitive patients. Only 48% (14/29) of sera were positive (percent binding ≥ 6%) in RAST to IFAWBE compared with 79% (23/29) positive to IFAV, and there was significantly greater binding to IFAV than to IFAWBE (p≤0.0002). Thus, RAST with IFAV identified 31% more sting-sensitive individuals than RAST with IFAWBE, a finding similar to that noted in studies using IFAV and IFAWBE for skin testing. We conclude that IFAV is the more appropriate allergen for use in in vitro tests to detect IFA-specific IgE antibody in allergic patients.

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Context‐dependent venom deployment and protein composition in two assassin bugs

Fischer

Wielsch

Heckel

et al. 2020

Ecology and Evolution

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The Heteroptera are a diverse suborder of phytophagous, hematophagous, and zoophagous insects. The shift to zoophagy can be traced back to the transformation of salivary glands into venom glands, but the venom is used not only to kill and digest invertebrate prey but also as a defense strategy, mainly against vertebrates. In this study, we used an integrated transcriptomics and proteomics approach to compare the composition of venoms from the anterior main gland (AMG) and posterior main gland (PMG) of the reduviid bugs Platymeris biguttatus L. and Psytalla horrida Stål. In both species, the AMG and PMG secreted distinct protein mixtures with few interspecific differences. PMG venom consisted mostly of S1 proteases, redulysins, Ptu1‐like peptides, and uncharacterized proteins, whereas AMG venom contained hemolysins and cystatins. There was a remarkable difference in biological activity between the AMG and PMG venoms, with only PMG venom conferring digestive, neurotoxic, hemolytic, antibacterial, and cytotoxic effects. Proteomic analysis of venom samples revealed the context‐dependent use of AMG and PMG venom. Although both species secreted PMG venom alone to overwhelm their prey and facilitate digestion, the deployment of defensive venom was species‐dependent. P. biguttatus almost exclusively used PMG venom for defense, whereas P. horrida secreted PMG venom in response to mild harassment but AMG venom in response to more intense harassment. This intriguing context‐dependent use of defensive venom indicates that future research should focus on species‐dependent differences in venom composition and defense strategies among predatory Heteroptera.

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Comparison of vespid venoms collected by electrostimulation and by venom sac extraction

Cited by 32 publications

References 18 publications

Comparison of <i>Vespula germanica</i> Venoms Obtained from Different Sources

Comparison of <i>Vespula germanica</i> Venoms Obtained from Different Sources

Superiority of <i>Solenopsis</i><i>invicta</i> Venom to Whole-Body Extract in RAST for Diagnosis of Imported Fire Ant Allergy

Context‐dependent venom deployment and protein composition in two assassin bugs

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