Allergens in Hymenoptera venom: XVII. Allergenic components of Solenopsis invicta (imported fire ant) venom

doi:10.1016/0091-6749(87)90035-2

Journal of Allergy and Clinical Immunology

Volume 80, Issue 3, Part 1, September 1987, Pages 300-306

https://doi.org/10.1016/0091-6749(87)90035-2 Get rights and content

Abstract

Pure venom from Solenopsis invicta was collected by having the insects sting into a capillary tube. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that three major protein bands were present in the venom. A prototype commercial extract was compared and found to contain the three major venom proteins and additional components as well as high potency and specificity by RAST. Immunoblot studies were performed with sera from allergic individuals with blots prepared from denatured SDS-PAGE gels and from two types of nondenaturing gels. The nondenaturing systems demonstrated the presence of two major allergens and three other allergens, each reacting with a third of the sera. Three of the allergens detected in SDS-PAGE blots were of identical mobility to the three major proteins in the pure venom sample. IgE binding to the SDS-PAGE blots was significantly less than that to nondenaturing blots, suggesting that much of the allergenic activity is conformation dependent.

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Imported fire ant hypersensitivity: antigenic analysis of whole body extracts and venom [Abstract]
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Cited by (35)

Unconscious Woman in Shock and Covered with Ants Pulled from an Abandoned Automobile
2019, American Journal of Medicine
Citation Excerpt :
Although venom alkaloids can cause adverse effects, they are less important as antigens because they do not induce IgE-mediated allergic responses (type 1 hypersensitivity reactions).5 A protein component in fire ant venom that makes up 0.1% of the venom induces type 1 hypersensitivity in persons allergic to fire ant stings.5–7 Reports of fatal stings caused by imported fire ants have been reported in unusual settings such as nursing homes and private houses.8–11
A middle-aged woman was taken from an abandoned automobile unconscious and covered with ants in Tucson, Arizona. When hospitalized in July 2018, she had an extensive papular-pustular skin eruption on her abdomen and thigh and disseminated intravascular coagulation. She was stung innumerable times by native golden fire ants (Solenopsis aurea) while sleeping in the vehicle. The large amount of venom injected by stings into this individual may have triggered dissemnated intravascualar coagulation because the venom contains powerful hemolytic factors.
The patient history is presented and ants were captured and identified.
Clinical findings of fire ant stings are presented and the importance of recognizing the distinctive skin lesions that occur is emphasized. Stings of the red imported fire ant, Solenopsis invicta, and the black imported fire ant, Solenopsis richteri, cause skin lesions recognized by physicians and victims alike in the southern and southeastern United States. Native fire ant stings are documented much less often. However, there is significant cross-reactivity among the venoms of Solenopsis species.
It is important for clinicians to recognize the characteristic skin lesions of fire ant envenomation as fire ant populations are expanding and they sting millions of people each year.
Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy
2019, Insect Biochemistry and Molecular Biology
Citation Excerpt :
Phospholipase A1 and -A2 are toxic and highly allergenic proteins early identified as major components in wasp (Fig. 1A) and honeybee venoms (HBV) (Fig. 1B); respectively (Hoffman, 1978; Hoffman and Shipman, 1976). Phospholipase A1 was also described as a predominant venom allergen in Solenopsis invicta (fire ant) (Hoffman, 1987; Hoffman et al., 1988) (Fig. 1A). Insect venom PLA1 (wasps) and PLA2 (bees) have a high diagnostic value and are commonly used as marker allergens during molecular diagnosis of HVA (Jakob et al., 2017a; Monsalve et al., 2012; Müller et al., 2012).
Insect venom phospholipases have been identified in nearly all clinically relevant social Hymenoptera, including bees, wasps and ants. Among other biological roles, during the envenoming process these enzymes cause the disruption of cellular membranes and induce hypersensitive reactions, including life threatening anaphylaxis. While phospholipase A2 (PLA2) is a predominant component of bee venoms, phospholipase A1 (PLA1) is highly abundant in wasps and ants. The pronounced prevalence of IgE-mediated reactivity to these allergens in sensitized patients emphasizes their important role as major elicitors of Hymenoptera venom allergy (HVA). PLA1 and -A2 represent valuable marker allergens for differentiation of genuine sensitizations to bee and/or wasp venoms from cross-reactivity. Moreover, in massive attacks, insect venom phospholipases often cause several pathologies that can lead to fatalities. This review summarizes the available data related to structure, model of enzymatic activity and pathophysiological roles during envenoming process of insect venom phospholipases A1 and -A2.
Identification, expression, and immuno-reactivity of Sol i 2 & Sol i 4 venom proteins of queen red imported fire ants, Solenopsis invicta Buren (Hymenoptera: Formicidae)
2012, Toxicon
Citation Excerpt :
In 1987, Hoffman confirmed the allergenic component of the venom as proteinaceous and that the allergenic activity is conformation dependant. Hoffman (1987) further suggests that the protein is allergenic due to its tertiary structure as opposed to its primary structure. In 1988, Hoffman et al. originally named and described four worker allergens (Sol i 1, Sol i 2, Sol i 3, and Sol i 4), which only composes 0.01% of the RIFA venom composition.
We report on two low-molecular weight proteins that are stored in the venom of queen red imported fire ants (Solenopsis invicta). Translated amino acid sequences identified one protein to have 74.8% identity with the Sol i 2w worker allergen, and the other protein was found to have 96/97% identity with Sol i 4.01w/4.02w worker allergens. Both Sol i 2 and Sol i 4 queen and worker proteins were expressed using pEXP1-DEST vector in SHuffle™ T7 Express lysY Escherichia coli. Proteins were expressed at significant concentrations, as opposed to the μg/ml amounts by our previous expression methods, enabling further study of these proteins. Sol i 2q protein bound weakly to human IgE, sera pooled from allergic patients, whereas Sol i 2w, Sol i 4.01w, and Sol i 4q proteins bound strongly. Despite Sol i 2w and Sol i 2q proteins having 74.8% identity, the queen protein is less immuno-reactive than the worker allergen. This finding is consistent with allergic individuals being less sensitive to queen than worker venom.
The Prokaryotic Expression and Bioactivity of the Recombinant Red Fire Ant Venom Allergen Sol i 4
2009, Agricultural Sciences in China
The sting of red imported fire ant (RIFA) could cause serious allergic response in fraction of people. These allergic reactions are mainly caused by its venom, especially venom allergen Sol i 1-4. To produce large amount of RIFA venom allergen Sol i 4 for diagnosis of RIFA allergy and allergen-specific immunotherapy, the gene encoding this protein was amplified and cloned into the prokaryotic expression vector pET43.1a. The recombinant plasmid was used to transform competent cells and the recombinant proteins were expressed in E. coli. SDS-PAGE and Western blotting analysis indicated that high-level expression of Sol i 4 protein was successfully achieved. Allergenic activity analysis of the recombinant allergen Sol i 4 was then performed on rabbit. The result showed that the recombinant protein obtained had significant allergenic activity. It indicated that the recombinant allergen Sol i 4 of RIFA venom was successfully expressed in E. coli, which provided foundation for further developing therapeutic and diagnosis reagents of RIFA allergy.
Hypersensitivity to fire ant venom
1996, Annals of Allergy, Asthma and Immunology
Reading this article will reinforce the reader's knowledge of the taxonomy, origin, and distribution of fire ants and will increase his ability to diagnose and manage reactions caused by the two imported species, Solenopsis invicta and richteri. This review will also enhance the reader's knowledge of the available diagnostic methods and therapeutic measures, including the role of fire ant venom versus whole body extract in the management of fire ant allergy.
Information for this review was obtained primarily from abstracts and articles written by investigators recognized for their expertise in fire ant venom research.
References were selected based on their clinical applicability and relevance to the epidemiology and pathophysiology of imported fire ant hypersensitivity.
The imported fire ant represents a significant health hazard for persons living in fire ant endemic areas in the southern United States. Sting reactions range from local pustules and large, late-phase responses to life-threatening anaphylaxis. Fire ant allergen-specific immunotherapy can reduce the risk of subsequent systemic reactions. Four important Sol i venom allergens have been isolated and characterized. Clinical studies have been designed to compare the safety and efficacy of fire ant venom with whole body extract for diagnosis and treatment of fire ant allergy.
Production of a recombinant imported fire ant venom allergen, Sol i 2, in native and immunoreactive form
1996, Journal of Allergy and Clinical Immunology
Background: The complementary DNA encoding for the important imported fire ant venom allergen, Sol i 2, has previously been cloned. The binding of human IgE antibodies to Sol i 2 has been demonstrated to be conformation-dependent. Methods: A complete cDNA clone encoding the Sol i 2 protein sequence and its natural signal sequence has been produced by polymerase chain reaction. The clone was ligated into a pBluebac III transfer vector (Invitrogen Corp., San Diego, Calif.), and the recombinant baculovirus was isolated by plaque purification. The recombinant baculovirus was grown in Sf9 and High-Five cells (Invitrogen Corp.) in serum-free media. The recombinant Sol i 2 was isolated and characterized. Results: Recombinant (r) Sol i 2 was produced in microgram/per milliliter amounts in Sf9 cells and at 30 μg/ml in High-Five cells. It was isolated by ultrafiltration and reverse-phase chromatography. The rSol i 2 demonstrated similar binding to natural-Sol i 2 in both a conformation-dependent ELISA assay and in RAST with sera from patients allergic to Sol i 2. The N-terminal sequence of the rSol i 2 was identical to that of the natural molecule. No significant increase in binding activity was found after treatment of rSol i 2 with protein disulfide isomerase. The binding of rSol i 2 to a conformation-dependent monoclonal antibody was lost by heating in sodium dodecylsulfate and reduction. Conclusions: A recombinant Sol i 2 protein was produced at high yield in a baculovirus expression system by using serum-free medium with a sequence identical to that of the natural molecule. Conformation-dependent immunologic assays indicate that the recombinant protein is produced with the native conformation. (J ALLERGY CLIN IMMUNOL 1996;98:82-8.)

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^☆: Sera from many of the allergic patients were provided by Dr. Donald MacQueen and Dr. Ab Eisen. Dr. Brian Batcher of Tulane University made a generous gift of rabbit antiserum against the prototype commercial extract. Mr. Miles Guralnick of Vespa Laboratories generously provided his protocol for nondenaturing PAGE.

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Journal of Allergy and Clinical Immunology

Abstract

References (16)

Fire ant venoms: comparative analyses of alkaloidal components

Toxicon

Fire ant venoms: chemotaxonomic correlations with alkaloidal compositions

Toxicon

Protein components of fire ant venom (Solenopsis invicta)

Toxicon

Fire ant venom hypersensitivity. I. Comparison of fire ant venom and whole body extract in the diagnosis of fire ant allergy

J Allergy Clin Immunol

In vivo and in vitro comparison of fire ant venom and fire ant whole body extract

J Allergy Clin Immunol

Imported fire ant hypersensitivity: antigenic analysis of whole body extracts and venom [Abstract]

J Allergy Clin Immunol

Two-dimensional polyacrylamide gel electrophoresis of Hymenoptera venom and venom sac extracts

Toxicon

A method for the efficient blotting of strongly basic proteins from sodium dodecyl sulfate-polyacrylamide gels to nitrocellulose

Anal Biochem

Cited by (35)

Unconscious Woman in Shock and Covered with Ants Pulled from an Abandoned Automobile

Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy

Identification, expression, and immuno-reactivity of Sol i 2 & Sol i 4 venom proteins of queen red imported fire ants, Solenopsis invicta Buren (Hymenoptera: Formicidae)

The Prokaryotic Expression and Bioactivity of the Recombinant Red Fire Ant Venom Allergen Sol i 4

Hypersensitivity to fire ant venom

Production of a recombinant imported fire ant venom allergen, Sol i 2, in native and immunoreactive form

Original articleAllergens in Hymenoptera venom: XVII. Allergenic components of Solenopsis invicta (imported fire ant) venom☆

Abstract

Toxicon

Toxicon

Toxicon

J Allergy Clin Immunol

J Allergy Clin Immunol

J Allergy Clin Immunol

Toxicon

Anal Biochem

Original article
Allergens in Hymenoptera venom: XVII. Allergenic components of Solenopsis invicta (imported fire ant) venom☆