Compatibility of imported fire ant whole body extract with cat, ragweed, Dermatophagoides pteronyssinus, and timothy grass allergens.

BACKGROUND: Recommendations regarding the administration of imported fire ant whole body extract (IFA WBE) combined with aeroallergens or environmental allergens in a single immunotherapy injection are lacking. OBJECTIVE: To evaluate the degradative effect of IFA WBE on cat, ragweed, Dermatophagoides pteronyssinus, and timothy grass allergens. METHODS: Imported fire ant whole body extract was combined with extracts of cat, ragweed, D pteronyssinus, and timothy grass. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed on each sample after storage for 0, 1, 3, and 6 months at 4 degrees C. In addition, cat and ragweed combinations were evaluated by radial immunodiffusion (RID); D pteronyssinus by enzyme-linked immunosorbent assay (ELISA) inhibition; and timothy grass by ELISA inhibition and Western blot. RESULTS: Imported fire ant whole body extract combined with timothy grass demonstrated degradation of timothy grass allergens by SDS-PAGE, ELISA inhibition, and Western blot results. Cat and ragweed allergens were stable after mixing with IFA WBE, based on SDS-PAGE and RID analyses. Stability of D pteronyssinus allergens with IFA WBE was evident from SDS-PAGE and ELISA inhibition data. CONCLUSIONS: Imported fire ant whole body extract combined with timothy grass resulted in significant and rapid timothy protein degradation. Imported fire ant whole body extract mixed with cat, ragweed, or D pteronyssinus revealed aeroallergen stability, yielding the possibility of combining these extracts in a single immunotherapy injection. Compatibilities of IFA WBE with other common aeroallergens remain undetermined and thus are not recommended for single-injection immunotherapy formulations.

Anaphylaxis from the influenza virus vaccine.

BACKGROUND: Allergic reactions to the influenza vaccine are uncommon and usually associated with sensitivity to egg or gelatin. The aim of this study was to report the case of anaphylaxis to the influenza vaccine. METHODS: Allergy percutaneous skin testing, serum specific IgE testing and IgE immunoblotting were performed to the influenza vaccine, egg, and gelatin. RESULTS: Percutaneous skin testing to the influenza vaccine and gelatin were positive and egg (white, whole, and yolk) was negative. Immunocap serum-specific IgE testing to egg (white, whole, and yolk) and gelatin were negative (<0.35 kU/l). IgE immunoblots were performed with 2 cord blood serums and the patient's serum at a 1:20 dilution against 10 microg of the Fluzone influenza vaccine. The patient's IgE immunoblot showed a protein band at 100 kDa which is similar to the molecular weight of gelatin protein, a 68-kDa protein which is similar to the molecular weight of hemagglutinin protein from the influenza vaccine, and a 45-kDa protein band that is similar to the molecular weight of ovalbumin protein from chicken embryo/egg. CONCLUSION: Based on clinical symptoms, skin testing, Immunocap testing and immunoblot evaluation, we feel that our patient is allergic to the infectious agent in the influenza vaccine as well as gelatin and ovalbumin in egg.

Seal and whale meat: two newly recognized food allergies.

BACKGROUND: Alaska's marine mammals compose a large portion of the diet of indigenous coastal Alaskan people. Bowhead whales (Balaena mysticetus) and bearded seals (Erignathus barbatus), inhabitants of the Bering and Beaufort seas along Alaska's western and northern coasts, are 2 of the most important subsistence species, serving as major food sources to the native population. OBJECTIVE: To describe an Inupiaq boy with symptoms consistent with an IgE-mediated food allergy after ingestion of bowhead whale and bearded seal meat. METHODS: Extracts of cooked bowhead whale and bearded seal were prepared, lyophilized, and evaluated for protein content. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was performed for each extract, followed by transfer to nitrocellulose and IgE immunoblots. Skin prick testing was conducted using reconstituted extracts of 1:10 wt/vol dilution. RESULTS: Immunoblots revealed serum specific IgE binding with the extracts of bowhead whale and bearded seal meat. Protein bands of approximately 25, 40, 50, and 90 kDa were found in the seal meat. Protein bands of 55 and 90 kDa were found in the whale meat. Skin prick test results were positive to whale and seal extracts with appropriate positive and negative controls. Ten control subjects had negative reactions to both extracts. CONCLUSION: A patient with moderate anaphylaxis to bowhead whale and bearded seal meat demonstrated serum specific IgE by means of immunoblot and positive skin prick test results. This is the first known reported case of specific IgE to these species.

Generalized cutaneous reactions to the anthrax vaccine: preliminary results of anthrax vaccine-specific cell mediated immunity and cytokine profiles.

Over two years, the Vaccine Adverse Event Reporting System reported that 0.042% of all anthrax vaccine (Biothrax, Bioport Corporation) doses administered were associated with cutaneous reactions, half of which were eczematous. This case series attempts to immunologically detail this eczematous reaction in four patients by measuring anthrax vaccine-specific cell mediated immunity (ASCMI), profiling TH1 and TH2 cytokine response to the anthrax vaccine in vitro, and analyzing of skin biopsy specimens. Results demonstrated that (1) ASCMI was variable and likely unrelated to this reaction; (2) a lack of TH1 cytokine response to anthrax vaccine may be associated with an increased risk of this eczematous reaction; and (3) skin biopsy findings were nonspecific but supportive of a clinical diagnosis of eczema. Future studies with more patients may yield data to further characterize the ASCMI response and cytokine profiles among patients with this type of reaction.

Effect of imported fire ant extract on the degradation of mountain cedar pollen allergen.

BACKGROUND: Dust mite, cockroach, and mold extracts have been shown to contain proteases capable of degrading the proteins in other extracts. Loss of potency of allergens has been reported in mixtures containing cockroach and fungal extracts. Fire ant venoms consist of 90% to 95% n-alkyl and n-alkenyl piperidine alkaloids, which are not allergenic. No studies are available addressing the mixture of imported fire ant (IFA) whole-body extract with other allergens or the presence of proteolytic activity in the venom extract. OBJECTIVES: To evaluate the stability of mountain cedar pollen extract mixed with IFA whole-body extract and to qualitatively analyze the extract mixture for degradation of mountain cedar protein. METHODS: One milliliter each of mountain cedar and IFA whole-body extracts at a concentration of 500 microg/mL were combined and stored at 4 degrees C for 1, 3, 6, 15, 30, 60, 90, and 180 days. Separate mixtures of 1 mL of mountain cedar and IFA with 1 mL of human serum albumin were used as controls. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was performed, and protein bands were qualitatively analyzed for degradation. RESULTS: We detected 3 distinct IFA protein bands and 1 mountain cedar protein band. With respect to these bands, no protein degradation was observed during 6 months of study in the extract mixture compared with the controls. CONCLUSIONS: Imported fire ant whole-body extract does not seem to degrade mountain cedar protein. Mixtures of allergenic extracts may be able to include IFA whole-body extract.

Cross-reactivity among edible nuts: double immunodiffusion, crossed immunoelectrophoresis, and human specific igE serologic surveys.

BACKGROUND: As many as one third of all food allergen anaphylactic events are related to tree nut ingestion. Although concurrent allergen sensitivity to tree nuts is common, cross-reactivity among nut antigens is less well defined. OBJECTIVE: To survey serologic cross-reactivities among 7 tree nuts (walnut, pecan, hazelnut, cashew, Brazil nut, pistachio, and almond) and peanut. METHODS: Human specific IgE enzyme-linked immunosorbent assay inhibition was used to identify nut allergen cross-reactivities. Single-nut rabbit antisera were used in double immunodiffusion, crossed-line immunoelectrophoresis, and crossed immunoelectrophoresis with intermediate gel studies of nut antigen cross-reactivity. RESULTS: Nut specific IgE enzyme-linked immunosorbent assay inhibition demonstrated no cross-reactivities between peanut and tree nuts. Among tree nuts, 2 groups with allergen cross-reactivity were defined: (1) walnut, pecan, and hazelnut and (2) hazelnut, cashew, Brazil nut, pistachio, and almond. Double immunodiffusion, crossed-line immunoelectrophoresis, and crossed immunoelectrophoresis with intermediate gel results supported the same groupings of cross-reactive tree nuts and identified several less prominent nut-nut antigen cross-reactivities between groups and with peanut. CONCLUSION: With few exceptions (notably limited peanut cross-reactivity with pistachio and walnut), peanut antigens did not serologically cross-react with tree nuts. Walnut, pecan, and hazelnut form a group of strongly cross-reactive tree nuts. Hazelnut, cashew, Brazil nut, pistachio, and almond form a group of moderately cross-reactive tree nuts. Cross-reactivities between these groups are less pronounced (notably limited cross-reactivity of walnut and pecan with Brazil nut). The strongest cross-reactivities among tree nuts follow botanical family associations: (1) walnut and pecan in the family Juglandaceae and (2) cashew and pistachio in the family Anacardiaceae.

Cross-reactivity between allergens in the venom of the common striped scorpion and the imported fire ant.

BACKGROUND: The common striped scorpion, Centruroides vittatus, and the imported fire ant (IFA) are endemic to the south-central United States. There is evidence of venom-specific IgE in patients experiencing hypersensitivity reactions to scorpion stings. The infrequency of repeated scorpion stings and the presence of immediate reactions to an initial sting suggest prior sensitization. OBJECTIVE: In the present study we evaluated the cross-reactivity of C vittatus venom with IFA whole-body extract (WBE). METHODS: Sera were obtained from patients with symptoms of immediate hypersensitivity to C vittatus stings and from scorpion sting-naive patients allergic to IFA venom. Inhibition IgE immunoblots were performed by using scorpion venom and IFA WBE. Skin testing with scorpion venom was performed on scorpion sting-naive patients allergic to IFA venom. RESULTS: Sera from patients with scorpion venom allergy demonstrated IgE binding to multiple allergens of similar sizes against both scorpion venom and IFA WBE. This binding was completely inhibited by preincubation of the sera with scorpion venom and IFA WBE. Pooled sera from patients with IFA venom allergy demonstrated similar bands on IgE immunoblotting against both IFA WBE and scorpion venom, with the latter being completely inhibited by preincubation of the sera with IFA WBE. Skin testing with scorpion venom was positive in 6 of 9 patients with IFA venom allergy. CONCLUSION: Significant cross-reactivity exists between the venom of C vittatus and IFA WBE. The high sensitization rate to IFA venom in endemic areas may therefore be a risk factor for subsequent immediate reactions to an initial scorpion sting. Patients with immediate hypersensitivity reactions to scorpion stings may potentially benefit from immunotherapy with IFA WBE.

Cross-reactivity between coconut and hazelnut proteins in a patient with coconut anaphylaxis.

BACKGROUND: The medical literature reports few cases of severe allergic reactions to coconut. We encountered a patient with anaphylaxis to coconut and oral symptoms to tree nuts. OBJECTIVE: To identify cross-reactive antibodies between coconut and other tree nuts. METHODS: We performed commercial radioallergosorbent tests to coconut and various tree nuts using the patient's serum. Skin prick testing was performed to fresh coconut and commercial extracts of coconut, almond, Brazil nut, cashew, pecan, walnut, and hazelnut. Proteins from fresh coconut, commercial coconut extract, and tree nuts were extracted. Immunoblot and inhibition assays were performed to evaluate for cross-reacting IgE antibodies between similar-sized allergens in coconut and hazelnut. RESULTS: Positive skin test results occurred to the coconut and multiple tree nut extracts. In vitro serum specific IgE was present for coconut, hazelnut, Brazil nut, and cashew. Immunoblots demonstrated IgE binding to 35- and 50-kDa protein bands in the coconut and hazelnut extracts. Inhibition assays using coconut demonstrated complete inhibition of hazelnut specific IgE, but inhibition assays using hazelnut showed only partial inhibition of coconut specific IgE. CONCLUSIONS: Our study demonstrates the presence of cross-reactive allergens between hazelnut (a tree nut) and coconut (a distantly related palm family member). Because there are many potentially cross-reactive allergens among the tree nuts, we recommend patients with coconut hypersensitivity be investigated for further tree nut allergies.

Cross-reactivity between raw mushroom and molds in a patient with oral allergy syndrome.

BACKGROUND: Oral allergy syndrome, resulting from a cross-reactivity between raw fruits and vegetables and a number of pollens, is well described. However, it has never been associated with mold spore sensitivity and mushrooms. We evaluated a patient with oral allergy symptoms to raw, but not cooked, mushrooms, who also had positive skin testing to molds. OBJECTIVE: To identify and characterize antigenic cross-reactivity between mushroom and mold spores. METHODS: The patient underwent skin prick testing to molds and mushroom. Proteins from raw and cooked mushrooms were extracted and immunoblot/inhibition assays were performed to evaluate for cross-reacting immunoglobulin E antibodies between mushroom and mold extracts to which the patient was sensitive. RESULTS: The patient had a positive skin prick test result to raw mushroom and four types of molds. The immunoblot assay revealed immunoglobulin E antibodies directed against similar molecular weight proteins in the raw mushroom and 3 of the 4 molds: Alternaria tenuis, Fusarium vasinfectum, and Hormodendrum cladosporioides. These protein bands on protein electrophoresis were absent in the cooked mushrooms. Inhibition immunoblot of the raw mushroom with the three molds indicated total inhibition of the 43- and 67-kD protein bands. CONCLUSIONS: We report the first case of cross-reactivity between mushroom and molds in a patient with oral allergy syndrome to raw mushroom and allergic rhinitis secondary to molds.