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PubMed1989

Analysis of differing patterns of cross-reactivity of honeybee and yellow jacket venom-specific IgE: use of purified venom fractions.

Prior studies of sera from insect sting-allergic patients have analyzed the relationship of coexisting honeybee venom- and yellow jacket venom-specific IgE. Radioallergosorbent (RAST)-inhibition tests with these venoms revealed four different patterns of activity. In this present study, purified fractions prepared from these venoms were used to analyze these varying patterns. The hyaluronidases of yellow jacket venom and honeybee venom showed extensive cross-reaction. The phospholipases from these venoms showed minimal cross-reactivity; antigen 5 was restricted to yellow jacket venom. There was a high molecular weight component in yellow jacket venom with immunologic properties similar to honeybee venom acid phosphatase. Sera from individual patients showed quantitative and qualitative differences in the reactions to the major components of both venoms. The differences in the RAST-inhibition patterns in patients with elevated levels of both honeybee venom- and yellow jacket venom-specific IgE are accounted for by these differences as well as by differences in the cross-reactivity between the individual components.

Animals↗
PubMed1988

Late onset reactions following venom immunotherapy and venom skin tests.

This report describes patients who had late onset reactions following venom immunotherapy and venom skin tests. Six adult patients had symptoms of fatigue, malaise, fever, headache, and joint ache, starting four to six hours after venom immunotherapy and lasting up to four days. Two of the patients had prolonged reactions at or adjacent to the skin test sites. All of these patients had a history of venom anaphylaxis; four had severe cardiovascular symptoms. All received yellow jacket venom immunotherapy and four honeybee venom immunotherapy. In four patients, the reactions occurred following small venom doses, 0.1 to 2 micrograms. Two patients reacted after maintenance doses of 50 micrograms. There was no relationship to the serum IgE or IgG antibody titers. All but one patient had serum venom-specific IgE but the titers covered a wide range. Serum venom-specific IgG was present in four patients. There was no response in lymphocyte culture to bee venom stimulation in two patients. Two of these patients stopped venom immunotherapy; one had reached the maintenance dose. In three patients, prophylactic parenteral steroids have ameliorated the reactions. After a temporary dose reduction, the sixth patient is now asymptomatic. A seventh patient developed asthma, 12 hours following a maintenance dose of 50 micrograms of yellow jacket venom. Concomitant steroid administration has effectively prevented the reaction. Another patient, a 6-year-old boy, developed fever, edema of the face and lips, erythema of the leg, and a large, tender right inguinal node eight hours following venom skin tests.(ABSTRACT TRUNCATED AT 250 WORDS)

Humans↗
PubMed1988

Classification of myonecrosis induced by snake venoms: venoms from the prairie rattlesnake (Crotalus viridis viridis), western diamondback rattlesnake (Crotalus atrox) and the Indian cobra (Naja naja naja).

The pathogenesis of myonecrosis induced by three different snake venoms was studied by light microscopic examination of skeletal muscle tissue taken at time periods ranging from 0.25 hr to 4 weeks after an intramuscular injection of the venom into mice. It was possible to identify different types of myonecrosis based on the abnormal morphologic states of the damaged cells. The types of myonecrosis observed correlated with the types of components present in the venom injected. Venoms containing direct acting toxins such as myotoxin a or phospholipase A2 induced specific types of myonecrosis. Also, venoms containing hemorrhagic toxins produced a type of myonecrosis similar to that induced by pure hemorrhagic toxins. The pathogenesis of each type of myonecrosis could be divided into the same four phases based on the pathologic states of the affected cells and the time after injection. During the 'early phase' (0.25-3 hr) affected muscle cells were in several different pathologic states reflecting the types of components present in the venom injected. During the 'intermediate phase' (6-24 hr) the pathologic state of the damaged cells had changed and depending on the venom new states might be present. By the 'late phase' (48-96 hr) all damaged cells have reached a common pathologic state of necrosis. The 'final phase' (1-4 weeks) is characterized by regeneration (partial or complete) of muscle cells. Although the number of different types of myonecrosis depended on the type of venom injected, i.e. Naja naja naja venom produced only two different types whereas Crotalus atrox venom produced at least four different types, cells of each tpe of myonecrosis progressed through the same four phases. In studies of the myotoxicity of snake venoms it is important to examine tissues taken during the early and intermediate phases to obtain accurate and useful information on the types of myonecrosis caused by the venom.

Animals↗
PubMed2004

Identification by immunoblot of venom glycoproteins displaying immunoglobulin E-binding N-glycans as cross-reactive allergens in honeybee and yellow jacket venom.

BACKGROUND: IgE antibodies against carbohydrate epitopes have been identified recently as a major cause of in vitro double positivity to honeybee (HB) and vespid venom in patients with stinging-insect allergy. As these antibodies possibly have low clinical relevance they may be misleading in the diagnosis of venom allergy. OBJECTIVE: To confirm the role of carbohydrate epitopes in double positivity and to locate the responsible glycoallergens in HB and yellow jacket (YJ) venom by western blot. METHODS: Immunoblot inhibition using HB venom, YJ venom and two glycoprotein sources displaying 1-3-fucosylated N-glycans (i.e. oilseed rape (OSR) pollen, and the synthetic neo-glycoprotein fucosylated/xylosylated N-glycans from bromelain coupled to bovine serum albumin (MUXF-BSA)) as inhibitors were performed with sera from 15 double-positive patients with stinging-insect allergy. Additionally, reactivity with blotted hymenoptera venoms of a carbohydrate-specific rabbit antiserum against OSR pollen was investigated. RESULTS: Major venom glycoallergens binding with carbohydrate-specific human IgE and rabbit IgG were detected in HB venom at 42 (hyaluronidase (HYA)), 46, 65 and 95 kDa, and in YJ venom at 38 and 43 kDa (HYA). Antibody binding to these allergens was completely lost after periodate treatment. Glycans of HB phospholipase were bound by patients' IgE only after protein denaturation. In 10 of the 15 patients the reactivity was with the second venom because of carbohydrates alone. The high-molecular-weight glycoallergens identified in HB venom probably correspond to similar proteins described earlier, including allergens B and C. The 38-kDa YJ allergen might represent a homologue of V mac 3. CONCLUSIONS: The data confirm the proposed role of carbohydrate-specific IgE in double positivity to HB and YJ venom and shed new light on some previously described minor hymenoptera allergens of uncertain clinical significance. The consideration of carbohydrate-specific IgE may allow to discriminate between patients with potentially relevant and patients with non-relevant double sensitization.

Adolescent↗
PubMed2004

Membrane independent activation of fibroblast proMMP-2 by snake venom: novel roles for venom proteinases.

ProMMP-2 activation by Bothrops asper venom was investigated in mouse gastrocnemius muscle, mammalian cell culture and a cell-free system. Zymography revealed an increment of latent and activated forms of MMP-2 in muscle homogenates 1-3 days after venom injection. To clarify if venom can induce expression and activation of MMP-2, independently of the inflammatory response, venom was added to cultured human fibroblasts, endothelial and skeletal muscle cells, which expressed proMMP-2 constitutively. Venom activated proMMP-2 without promoting its expression. Venom also activated and degraded proMMP-2 in supernatants collected from fibroblast cultures, indicating that cells are not required for this activation. Pretreatment with EDTA increased MMP-2 activation and reduced degradation. Venom serine proteinases activated proMMP-2, whereas BaP1, a P-I metalloproteinase, predominantly degraded the latent and active forms of MMP-2. Moreover, pretreatment of conditioned medium with serine proteinase inhibitors greatly reduced the venom-induced activation, suggesting that venom proteinases activate MMP-2 via a serine proteinase secreted by fibroblasts. Venom also directly activated and degraded purified proMMP-2, albeit requiring a high concentration. Thus, B. asper venom proteinases activate and degrade proMMP-2 without inducing its synthesis. Serine proteinases play a dominant role in the activation, whereas metalloproteinases predominantly degrade MMP-2. Activation of proMMP-2 by snake venom proteinases, independently of the MT1-MMP/TIMP-2 pathway, extracellular matrix degradation or apoptosis, represents a novel mechanism in human fibroblasts.

Animals↗
PubMed2005

Cross-neutralization of the neurotoxicity of Crotalus durissus terrificus and Bothrops jararacussu venoms by antisera against crotoxin and phospholipase A2 from Crotalus durissus cascavella venom.

We have previously demonstrated that rabbit antisera raised against crotoxin from Crotalus durissus cascavella venom (cdc-crotoxin) and its PLA2 (cdc-PLA2) neutralized the neurotoxicity of this venom and its crotoxin. In this study, we examined the ability of these antisera to neutralize the neurotoxicity of Crotalus durissus terrificus and Bothrops jararacussu venoms and their major toxins, cdt-crotoxin and bothropstoxin-I (BthTX-I), respectively, in mouse isolated phrenic nerve-diaphragm preparations. Immunoblotting showed that antiserum to cdc-crotoxin recognized cdt-crotoxin and BthTX-I, while antiserum to cdc-PLA2 recognized cdt-PLA2 and BthTX-I. ELISA corroborated this cross-reactivity. Antiserum to cdc-crotoxin prevented the neuromuscular blockade caused by C. d. terrificus venom and its crotoxin at a venom/crotoxin:antiserum ratio of 1:3. Antiserum to cdc-PLA2 also neutralized the neuromuscular blockade caused by C. d. terrificus venom or its crotoxin at venom or toxin:antiserum ratios of 1:3 and 1:1, respectively. The neuromuscular blockade caused by B. jararacussu venom and BthTX-I was also neutralized by the antisera to cdc-crotoxin and cdc-PLA2 at a venom/toxin:antiserum ratio of 1:10 for both. Commercial equine antivenom raised against C. d. terrificus venom was effective in preventing the neuromuscular blockade typical of B. jararacussu venom (venom:antivenom ratio of 1:2), whereas for BthTX-I the ratio was 1:10. These results show that antiserum produced against PLA2, the major toxin in C. durissus cascavella venom, efficiently neutralized the neurotoxicity of C. d. terrificus and B. jararacussu venoms and their PLA2 toxins.

Analysis of Variance↗
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↗
PubMed1983

Immunological stability of an elapid venom, Tropidechis carinatus, and its relevance to the clinical detection of snake venom.

Using immunological techniques, cases of human snake-bite can be proven and individual snake species identified. A series of experiments is described, to test the antigenic stability and physical properties of an Elapid venom, venom properties which will have implications in field use, transport, or the laboratory procedures relating to the immunological characterization of Australian snake venoms. Using venom from the Elapid, Tropidechis carinatus, we have demonstrated significant immunological stability at a temperature of 37 degrees for 48 h at least, and for 24 h at least when incubated continuously with skin, muscle, and fat homogenates; the venom is stable at 56 degrees for 2 h at least. No loss of venom occurs over the pH range 7-10; at pH ranges less than 4 and at ranges greater than 10 only 30% of venom is detected after 30 min incubation. Sonication (10 min at 100 watts) does not destroy immunological properties of the venom; 10 freeze-thaw cycles result in some 9% loss of immunologically detectable activity. Venom is adsorbed significantly on to dacron swabs, only 13% of the applied does being detected after 48 h incubation at 28 degrees. Sixty-seven percent of applied venom can be recovered from the skin of human volunteers 6 h after a simulated bite. The venom of this Elapid is antigenically robust. With the currently available sensitive assays, venom from human skin should still be detected in material kept without special preparation under field conditions for up to 2 days at least.

Animals↗
PubMed2004

Stimulation of the alpha-adrenoceptor triggers the venom production cycle in the venom gland of Bothrops jararaca.

The noradrenergic innervation of Bothrops jararaca venom gland is thought to be important in the production and secretion of venom. We investigated the characteristics of the alpha-adrenoceptor in the venom gland and its role in venom production. This receptor had relatively low sensitivity to noradrenaline (pD(2)=4.77+/-0.09, N=7) and to phenylephrine (pD(2)=3.77+/-0.06, N=11). The receptor became desensitized just after venom extraction (pD(2) to phenylephrine fell to 3.27+/-0.02, N=6) and the sensitivity remained low for at least 15 days, returning to normal 30 days after venom extraction, by which time the snake was ready for a new cycle of venom production. Incubation of secretory cells with noradrenaline (10(-4) mol l(-1) for 5 min) reduced alpha-adrenoceptor sensitivity to the level seen after venom extraction. Blockade of catecholamine production with reserpine abolished the enlargement of the rough endoplasmic reticulum and the activation of the Golgi apparatus that are normally seen after venom extraction, and the venom production was restored by a single subcutaneous (s.c.) injection of phenylephrine (100 mg kg(-1)) immediately after venom extraction. Our data suggest that stimulation of the alpha-adrenoceptor during or shortly after biting is essential for the onset of the venom production cycle.

Animals↗
PubMed1985

Allergens in Hymenoptera venom XIII: Isolation and purification of protein components from three species of vespid venoms.

Pure venoms were collected from individual insects of the species Dolichovespula maculata, white-faced hornet, Vespula squamosa, southern yellow jacket, and Polistes exclamans, paper wasp (one species). The venoms were first fractionated by high-resolution gel filtration on a 1.6 m column of Sephadex G-75 superfine, and the components were then purified by high-performance, ion-exchange chromatography on a Mono-S cation exchange column followed by a further gel filtration step. The isolated components were evaluated for purity by sodium dodecyl sulfate polyacrylamide gel electrophoresis by use of two different types of silver stains, by assays for enzyme activities, and by immunodiffusion with the use of rabbit antisera. The protein components were isolated in highly purified states by these techniques. Only three significant proteins were found in V. squamous venom: phospholipase (PL) A and B, hyaluronidase (HYAL), and antigen 5 (Ag 5). D. maculata venom contained HYAL, Ag 5, two isozymes of PL A and B, a high-molecular-weight protein, and several trace proteins. No significant amounts of proteases were found in D. maculata venom. P. exclamans venom contained HYAL, PL A and B, Ag 5, a high-molecular-weight protein, and several minor proteins. In all three venoms the PL A and B activities were found to be in the same molecule and did not separate. Trace components with apparent PL A activity were observed in the venoms. The venoms were screened for a variety of esterases, proteases, peptidases, glucosidases, and phosphatases, and none were detected in more than trace amounts. Vespid venoms do not appear to contain significant amounts of acid phosphatases as bee venoms do.

Allergens↗
PubMed2001

Patients still reacting to a sting challenge while receiving conventional Hymenoptera venom immunotherapy are protected by increased venom doses.

BACKGROUND: Up to 20% of patients allergic to Hymenoptera venom are not protected by conventional venom immunotherapy (VIT) with 100 microg of any single venom. OBJECTIVE: We sought to evaluate the efficacy of an increased venom dose in patients allergic to Hymenoptera venom still reacting systemically to a sting challenge despite immunotherapy with 100 microg of venom every 4 weeks. METHODS: In this retrospective study patients were included who still had reacted systemically to a sting challenge with a living bee or wasp despite VIT with a maintenance dose of 100 microg every 4 weeks. The maintenance dose was increased to 150 or 200 microg every 4 weeks, and a second sting challenge was performed. If a patient reacted again, the dose was further increased. Baseline mast-cell tryptase levels were assessed by using a fluoroenzyme immunoassay in stored patient sera. RESULTS: While receiving a maintenance dose of 100 microg of venom every 4 weeks for 7 to 38 months, 18 patients reacted systemically to a bee sting and 22 reacted to a wasp sting. After an increase of the maintenance dose to 150 microg, 2 of 4 patients allergic to bee venom (BV) and 6 of 6 patients allergic to yellow jacket venom (YJV) no longer reacted systemically to the sting challenge. The respective rates of full protection were 13 of 14 and 15 of 16 in patients with an increase of the maintenance dose to 200 microg from the start. Of those 4 individuals not protected by the first dose increase, one patient allergic to BV (prior dose of 150 microg) and one patient allergic to YJV (prior dose of 200 microg) did not react systemically to a further sting challenge while receiving 200 microg of BV or 250 microg of YJV, respectively. One patient allergic to BV who had a systemic reaction to the sting challenge while receiving 150 microg was not protected after a dose increase to 200 microg; she later received a dose of 400 microg of BV, and no further sting challenge was performed. The patient allergic to BV who still reacted systemically after a first dose increase to 200 microg was a female patient with urticaria pigmentosa. She had repeated systemic adverse reactions to further BV immunotherapy, necessitating discontinuation of the treatment; however, she tolerated well VIT with 200 microg of YJV. In all other patients, no unusual adverse reactions to the increased venom doses were observed. Baseline serum tryptase levels were elevated above 13.5 microg/L (95th percentile in normal subjects) in 9 (28.1%) of 32 patients. CONCLUSIONS: The majority of patients allergic to Hymenoptera venom who still reacted systemically to a sting challenge despite VIT with a dose of 100 microg every 4 weeks can be fully protected by an increased maintenance dose. This dose increase is well tolerated by most patients. The rather high proportion of patients with elevated baseline serum tryptase levels necessitates further investigation of a possible association between mastocytosis and treatment failure of conventionally dosed VIT.

Adult↗
PubMed2001

Antibody binding to venom carbohydrates is a frequent cause for double positivity to honeybee and yellow jacket venom in patients with stinging-insect allergy.

BACKGROUND: Up to 50% of patients with stinging-insect allergy have double-positive RAST results to honeybee and yellow jacket (YJ) venom. True double sensitization and crossreactivity through venom hyaluronidases are considered main reasons for this multiple reactivity. OBJECTIVE: We investigated the role of antibodies against cross-reactive carbohydrate determinants in venom double positivity. METHODS: CAP inhibition experiments were performed with crude oilseed rape (OSR) and timothy grass pollen extracts and a neoglycoprotein construct displaying a MUXF glycan, as present in pineapple-stem bromelain (MUXF-BSA). CAP to OSR was used as a rough measure for carbohydrate-specific IgE in individual sera. RESULTS: CAP results to OSR pollen were positive in 2 of 14 single-positive honeybee venom sera, 2 of 16 single-positive YJ venom sera, and 33 (80.5%) of 41 double-positive sera (P < .00001, chi(2) test). CAP inhibition was performed in 16 selected patients with a CAP class of 3 or higher to both venoms. In 9 of 11 patients with a highly positive CAP result to OSR (CAP score to OSR > CAP score to second venom), pollen extracts, MUXF-BSA, or both were able to completely inhibit IgE binding to one of the venoms, whereas this was not the case in 5 patients with a negative or weakly positive CAP result to OSR (CAP score to OSR < CAP score to second venom). CONCLUSIONS: The data suggest that carbohydrate-specific IgE is a major cause for the double positivity to honeybee and YJ venom seen in patients with Hymenoptera allergy. Because these antibodies may have low clinical relevance, they may severely impede the correct diagnosis of Hymenoptera venom allergy.

Animals↗
PubMed1985

Enzyme-linked immunosorbent assay (ELISA) of changes in specific IgG antibodies to five venoms during venom immunotherapy.

An enzyme-linked immunosorbent assay (ELISA) was developed that could measure titres of human IgG antibodies to five different venoms (honeybee, yellow jacket, yellow hornet, white-faced hornet, and wasp), and to honeybee phospholipase A. Changes in specific IgG anti-venom titres were measured in twenty patients that had systemic anaphylactic reactions to insect stings, and ten non-allergic controls. After being stung and prior to treatment all patients had anti-venom IgG titres greater than controls. Treatment with small doses of venom over 1-2 months resulted in prompt rises in anti-venom IgG titres that may represent secondary anemnestic responses primed by prior stings. All patients undergoing venom immunotherapy showed at least 2-fold increases in IgG antibody to the venoms they were treated with by the time maintenance doses of 100 mcg were achieved, with one exception. Significant cross-reactive increases in anti-vespid IgG antibodies to venoms not used for treatment occurred in nine of eighteen treated patients. Overall, ELISA of IgG antibodies to five venoms allowed clear evaluation of the considerable variation of IgG responses among different patients. We conclude that serial determination of venom-specific IgG titres by ELISA offers an important adjunct to evaluating the results of venom immunotherapy.

Anaphylaxis↗
PubMed2006

Enzyme immunoassays in brown snake (Pseudonaja spp.) envenoming: detecting venom, antivenom and venom-antivenom complexes.

Although a commercial snake venom detection kit (SVDK) is available to distinguish between the five major snake groups in Australia, there is no assay for quantifying venom or antivenom concentrations in envenomed patients. Serum samples were obtained from patients with brown snake (Pseudonaja spp.) envenoming before and after the administration of antivenom and patients with suspected brown snake bites but no evidence of envenoming. Enzyme immunoassays (EIAs) were developed for free venom, free antivenom and the venom-antivenom complex. Standard samples measured in duplicate had a coefficient of variation of less than 10%. The EIA for venom was able to detect brown snake venom down to concentrations of 3 ng/mL. A high baseline absorbance was measured in some patients that did not change with the addition of excess antivenom to the samples. In these patients, the baseline absorbance was subtracted from all measurements to calculate the true venom concentration. The EIA for brown snake antivenom had a limit of detection of 20 microg/mL, but 50 microg/mL was used as a cut-off based on assays in patients who had not received antivenom. The EIA for venom-antivenom complexes was unable to detect these at the low venom concentrations that occurred in patients. Quantification of venom and antivenom will help to determine the dose of antivenom required to bind venom and to establish appropriate end points for antivenom treatment.

Adolescent↗
PubMed2003

Use of microarrays for investigating the subtoxic effects of snake venoms: insights into venom-induced apoptosis in human umbilical vein endothelial cells.

The pathological effects of only a small percentage of the total number of protein components of snake venoms are well documented, yet this knowledge has led to a general understanding of the physiological consequences of snake venom poisoning. The aim of this study was to assess the effect of subpathological levels of Crotalus atrox (Western diamondback rattlesnake) and Bothrops jararaca (Jararaca) snake venoms on the gene expression profile of human umbilical vein endothelial cells (HUVEC) in culture. Analysis of the data demonstrated that HUVECs treated with C. atrox venom had 33 genes up-regulated with significant fold changes of 1.5 or greater compared to untreated control cells. Ten genes were down-regulated with 1.5 or greater fold changes. In cells treated with B. jararaca venom, 33 genes were observed to be up-regulated and 11 genes were down-regulated with a fold change of 1.5 or more. More than half of the up-regulated genes and approximately half of the down-regulated genes detected in cells treated with the venoms were found in both data sets underscoring both the similarities and differences between the two venoms. Ontological categorization of the up-regulated genes from endothelial cells treated with either C. atrox or B. jararaca venom gave the cell growth/maintenance and signal transducer groups as having the most members. The ontology of the down-regulated genes from both venom-treated cell samples was more varied but interestingly, the predominant ontology class was also cell growth/maintenance. Many of the up-regulated genes are involved in the Fas ligand/TNF-alpha receptor apoptotic pathway. In summary, these experiments demonstrate the power of gene expression profiling to explore the subtoxic effects of venoms on gene expression and highlight its potential for the discovery of novel insights into a variety of biological processes and signal transduction pathways. Furthermore, these studies illustrate the subtle functional differences between similar venoms that are not always evident from standard analyses.

Animals↗
PubMed1983

[Measurement of bee venom specific IgG antibody in bee venom hypersensitivity and the relation between the specific IgE antibody and total IgE].

Bee venom specific IgG antibodies for honeybee and common wasp were measured in normal control group, slightly bee injury group, heavy bee injury group and honeybee keeper's group. Relation among bee venom specific IgG antibody, bee venom specific IgE antibody and total IgE was analyzed. Normal control level of bee venom specific IgG antibody was measured under 60 U/ml. Bee venom specific IgG antibody in slightly bee injury group was higher than that in heavy bee injury group. Bee venom specific IgE antibody in slightly bee injury group was lower than that in heavy bee injury group. Bee venom specific IgE antibody in bee keeper's group was very high but bee venom specific IgG antibody was also high. From this results it seems that bee venom hypersensitivity can be prevented by high titer of bee venom specific IgG antibody even if bee venom specific IgE antibody is high titer.

Adult↗
PubMed1981

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

Venoms of three vespid species, yellow jacket, bald-faced hornet, and yellow hornet, obtained by either electrostimulation of venom sac extraction were compared with regard to their enzymatic activity, antigenicity, and allergenicity. Phospholipase a, phospholipase B, and hyaluronidase enzymatic activities were present in all six preparations. The activity of venom sac extracts lay in the range found in different batches of venoms obtained by electrostimulation for each species. Analysis of sera from vespid-sensitive patients in the radioallergosorbent test (RAST) with discs coupled with either venom sac extracts or venoms obtained by electrostimulation showed a good correlation of the results within all three species (r = 0.95). In RAST inhibition the potency of venom sac extracts and venom obtained by electrostimulation was similar for each species. Analysis of rabbit antisera to the six preparations revealed similar patterns in immunoelectrophoresis and identity reactions between the major antigens within each species. Tissue protein contamination was detected in all venom sac extracts but not in venoms obtained by electrostimulation.

Animals↗