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At least 883 records · Page 49Linked to original sources
PubMed2003

Characterization of the major allergens purified from the venom of the paper wasp Polistes gallicus.

Allergic reactions to vespid stings are one of the major causes of IgE-mediated anaphylaxis. Vespa and Vespula venoms are closely related; Polistes venom is more distantly related and its allergens are less well studied. There is limited cross-reactivity between Polistes and the other vespid venoms because of differences in the epitopes on the allergen molecules. In this study, the major allergens of Polistes gallicus are isolated and characterized. P. gallicus venom contains four major allergens: phospholipase, antigen 5 (Ag5), hyaluronidase and protease that were characterized by mass spectrometry and specific binding to IgE. The complete amino acid sequence of Ag5 and the sequence of the N-terminal region of phospholipase were also determined. The alignment of Ag5 from P. gallicus (European species) and Polistes annularis (American species) shows an 85% identity that increases to 98% within the same subgenus. This could suggest the presence of specific epitopes on Ag5 molecule being the variations on the superficial loops. The features of the P. gallicus allergens could explain the partial cross-reactivity found between the American and European Polistes venoms, and suggest that the use of European Polistes venoms would improve the diagnostic specificity and the therapy of European patients and of North American patients sensitized by European Polistes.

Allergens↗
PubMed2005

Hydrolase activity in the venom of the pupal endoparasitic wasp, Pimpla hypochondriaca.

Venom from the pupal endoparasitoid, Pimpla hypochondriaca has previously been shown to contain a mixture of biologically active molecules. Currently, P. hypochondriaca venom was examined for the presence of hydrolase activity. Six hydrolases were consistently detected using the API ZYM semiquantitative colourimetric kit. The main hydrolases detected were; acid phosphatase, beta-glucosidase, esterase, beta-galactosidase, esterase lipase, and lipase. The most rapid and intense colour reaction was detected for acid phosphatase. The pH optimum and the specific activity of venom acid phosphatase was determined using p-nitrophenol phosphate as a substrate and were 4.8 and 0.47 nmol p-nitrophenol/min/microg of venom protein, respectively. The acid phosphatase activity was inhibited in a dose dependent manner by sodium fluoride (IC(50) 4.2 x 10(-4) M), and by cocktail inhibitor 2 (CI 2). P. hypochondriaca venom has previously been shown to display potent cytotoxic activity towards Lacanobia oleracea haemocytes maintained in vitro. The contribution of acid phosphatase in venom to this cytotoxic activity was investigated by titrating venom against CI 2 prior to the addition of L. oleracea haemocytes. The results suggest that, despite the relatively high levels of acid phosphatase activity in venom, venom acid phosphatase plays no role in the antihaemocytic activity of P. hypochondriaca venom in vitro.

Acid Phosphatase↗
PubMed2005

Advances and prospects on biosynthesis, structures and functions of venom proteins from parasitic wasps.

Molecular and biochemical properties of parasitoid Hymenoptera's venom proteins are currently receiving an increasing interest. In this review, we will highlight the progress that has been made over the past 10 years in fundamental research on this field. Main knowledge acquired on the structural features of parasitoid venom peptides, proteins and enzymes will be summarized and discussed and several examples showing the diversity of their biological functions will be given with respect to future prospects and applications.

Animals↗
PubMed1997

Pharmacological investigation of oedema induced by venom from the wasp Polistes fuscatus.

Subplantar injection of Polistes fuscatus venom induced dose-dependent rat hindpaw oedema. The oedema was significant in the first hour and reached maximum size in the fifth hour after injection of the venom (20-600 micrograms/paw). Low doses of the venom (20-80 micrograms/paw) produced oedema which disappeared within 48 hr after injection, while at doses of 300-600 micrograms/paw, oedema was present in excess of 48 hr. Pharmacological studies suggested that P. fuscatus venom-induced oedema probably has a mechanism which is multimediated. Pretreatment of rats with a combination of cyproheptadine (5 mg/kg)-captopril (2 mg/kg)-dexamethasone (1 mg/kg) inhibited the formation of oedema (maximal swelling) produced by the venom (300 micrograms/paw) by about 79% and improved the time to recovery. Paw swellings caused by 20 and 40 micrograms/paw venom were completely eliminated by the same doses of this drug combination. The kinins, autacoids (histamine and serotonin) and lipogenase derivatives are probably involved in the venom-induced oedema.

Animals↗
PubMed2001

Preliminary cryocrystallography analysis of an eumenine mastoparan toxin isolated from the venom of the wasp Anterhynchium flavomarginatum micado.

Mastoparans are tetradecapeptides found to be the major component of vespid venoms. These peptides present a wide spectrum of biological activities, such as mast cell degranulation, hemolytic activity and also reveals antimicrobial activity. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized. At room temperature these crystals diffracted to 2.8 A resolution. However, upon cooling to cryogenic temperature around 85 K, the original resolution limit could be improved to 2.0 A. Crystals were determined to belong to the space group P3(1) (P3(2)). This is the first mastoparan to be crystallized and it will provide further insights in the conformational significance of mastoparan toxins, with respect to their potency and activity in G protein regulation.

Animals↗
PubMed2002

Analysis of venom constituents from the parasitoid wasp Pimpla hypochondriaca and cloning of a cDNA encoding a venom protein.

Venom from Pimpla hypochondriaca, an endoparasitoid of pupae, was size-fractionated using gel filtration chromatography and analysed by SDS-PAGE in the presence and absence of reducing agent. A complex mixture of more than 20 venom constituents was identified which ranged in M(r) between approximately 5 and 100 kDa. Venom from a wide range of size fractions inhibited the motility of larval haemocytes and prevented the formation of cell aggregates when analysed in vitro, indicating that anti-haemocytic activity is mediated by multiple venom components. Sephadex A25 beads injected into the haemocoel of pupae were encapsulated within 24h. This reaction was abolished when the pupae were injected with 30 microg of venom protein, equivalent to one-fifth of a venom sac, 1h prior to implantation of the beads, confirming that venom suppresses encapsulation in pupae. Using random 5' end sequencing of a P. hypochondriaca venom gland cDNA library, we have isolated a cDNA encoding a 25.3 kDa protein containing a signal peptide and having sequence similarity to serine proteases. The N-terminal sequence of six residues from two venom proteins of 28 and 30 kDa was the same and identical to amino acids encoded by the cDNA, confirming that two mass forms of the protein are secreted into the venom sac. The N-terminal sequence of both venom proteins began nine residues towards the C terminus following the predicted signal sequence cleavage site, suggesting that the proteins are proteolytically processed before or during storage in the venom sac. The general applicability of using random 5' sequencing to identify cDNAs encoding secretory products is discussed.

Amino Acid Sequence↗
PubMed2003

A serine proteinase homolog venom protein from an endoparasitoid wasp inhibits melanization of the host hemolymph.

Activation of prophenoloxidase (proPO) in insects is a defense mechanism against intruding microorganisms and parasites. Pattern recognition molecules induce activation of an enzymatic cascade involving serine proteinases, which leads to the conversion of proPO to active phenoloxidase (PO). Phenolic compounds produced by pPO-activation are toxic to invaders. Here, we describe the isolation of a venom protein from the parasitoid, Cotesia rubecula, injected into the host, Pieris rapae, which is homologous to serine proteinase homologs (SPH). The data presented here indicate that the protein interferes with the proteolytic cascade, which under normal circumstances leads to the activation of proPO and melanin formation.

Amino Acid Sequence↗
PubMed1987

Provocation test with a living insect as a diagnostic tool in systemic reactions to bee and wasp venom: a prospective study with emphasis on the clinical aspects.

The use of the sting challenge (SC) in insect allergy has brought into doubt the widely held belief that clinical data, specific IgE and the skin test are reliable tools in diagnosis and decision making with regard to therapy. We subjected ninety patients, known to have a systemic reaction to SC, in the Intensive Care Unit. Of these patients, 28% once more showed a systemic reaction; 72% had only a local reaction. No statistically significant difference could be demonstrated between positive and negative SC patients with regard to age; sex; the presence of allergic disease(s)--other than allergy to insects--and the severity of the preceding systemic reaction; the sting site and the related time interval; or specific IgE, IgG1, IgG4, their ratios and the skin test. A negative skin test and/or specific IgE, however, does not exclude the possibility of a recurrent systemic reaction. The long-term value of the SC appeared to be good since the results of the revision SC remained unchanged. Skin test and specific IgE are useful as diagnostic tools in establishing the insect concerned. SC provides information on the likelihood of a recurrent systemic reaction.

Adolescent↗
PubMed1985

Crossed immunoelectrophoresis and crossed radioimmunoelectrophoresis analysis of "yellow jacket-common wasp" (Vespula spp.).

Crossed immunoelectrophoresis (CIE) pattern of Yellow jacket vespid venom showing 25 immunoprecipitates was used in crossed radioimmunoelectrophoresis (CRIE) analysis with sera from 35 subjects allergic to vespid venom. Phospholipase A and B, hyaluronidase, acid and alkaline phosphatases and a lytic active component were demonstrated in immunoprecipitates using zymography and direct haemolysis of sheep erythrocytes. CRIE analysis proved the allergenicity of these proteins. In addition, another antigen (Ag 17) with no detectable enzymatic or lytic activity was identified as an important allergen. This allergen is most likely identical to the previously described Antigen 5 in vespid venoms. By using CIE/CRIE the presence and complexity of multiple forms of the allergenic protein components were well demonstrated.

Allergens↗