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

Schmidt, Margit; McConnell, Thomas J.; Hoffman, Donald R.

doi:10.1016/s0091-6749(96)70229-4

Cited by 30 publications

(22 citation statements)

References 25 publications

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“…Under reducing condition (Figure 2, lane 4), the Sol gem 2 band co-migrated with the Sol gem 4 band, suggesting that these two proteins might have similar structures. Sol i 2 and Sol i 4 are members of a unique protein family (3,38,39). Sol i 4 is structurally related to Sol i 2, with 118 amino acids and no carbohydrate modifications (40).…”

Section: Page Analysis and Protein Identification Of Crude Venommentioning

confidence: 99%

Characterization of the allergen Sol gem 2 from the fire ant venom, Solenopsis geminata

Sukprasert¹,

Uawonggul²,

Jamjanya³

et al. 2012

J. Venom. Anim. Toxins incl. Trop. Dis

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Sol i 2 is a potent allergen in Solenopsis invicta venom, and most humans exhibit reactivity to it. The Sol gem 2 allergen found in the venom of the Thai tropical fire ant Solenopsis geminata was analysed in the present study. The protein was present in higher amounts than other proteins, as determined by SDS-PAGE, and presumably has allergenic properties similar to those of Sol i 2. Sol gem 2 molecular weight is 28 and 15 kDa, respectively, under non-reducing and reducing conditions, indicating that its native form is a dimer. LC-MS/MS analysis confirmed its similarity to Sol i 2. The mono/dimeric form of Sol gem 2 was determined to be relevant by proteomic approach and immunoblotting. An anti-Sol gem 2 antibody was produced in mice, with a titer greater than 1:800 according to the Western blotting analysis. The Sol gem 2-neutralising activity of this antibody was determined in crickets. The paralytic dose 50 (PD 50 ) of crude S. geminata venom was elevated from 0.18 mg/g of body weight to more than 0.90 mg/g of body weight after preincubation with antibody at a ratio of 1:1. These results suggest that Sol gem 2 plays an important role in mediating the effects of the piperidine derivatives in the venom.Key words: allergy, ant venom, hymenoptera, immunoreactivity. Original PaPer The Journal of Venomous Animals and Toxins including Tropical Diseases ISSN 1678-9199 | 2012 | volume 18 | issue 3 | pages 325-334 INTRODUCTIONVenomous insects such as bees, wasps, hornets, yellow jackets and fire ants belong to the order Hymenoptera. These insects have a stinging apparatus at the tail end of their abdominal segment and still comprise a serious problem in tropical climates. Every year, a large number of people are stung by these insects (1). The stings are capable of delivering between 100 ng (fire ants) and 50 μg (bees) of venom (2, 3). The venom is injected from a gland through the stinger and is used to catch prey and to defend against predators. The venom of these insects is composed of various biologically active peptide and protein components, some of which can cause toxicity or anaphylaxis in humans (4).Fire ants (Solenopsis sp.) are members of the Formicidae family. The medically important aggressive species are S. invicta, S. richteri, S. geminata and S. saevissima (5, 6). The venom components of these ants and their immunoreactivity have been extensively studied. Approximately 95% of fire ant venom consists of water-insoluble piperidine alkaloids, and approximately 0.1% of its weight (10 to 100 ng of protein in 0.04 to 0.11 μL per sting) is protein (7). The toxicity of the venom is thought to be due to solenopsins and methyl-, alkylor alkenyl-substituted piperidines (7-9). The venom has cytotoxic, insecticidal, antibiotic and antimicrobial properties as well (7,(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19). The protein components of venom, which are wellknown allergens, are believed to play important roles in accelerating the spread of solenopsins to nearby cells and tissues. Solenopsins are believed t...

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Section: Page Analysis and Protein Identification Of Crude Venommentioning

confidence: 99%

Characterization of the allergen Sol gem 2 from the fire ant venom, Solenopsis geminata

Sukprasert¹,

Uawonggul²,

Jamjanya³

et al. 2012

J. Venom. Anim. Toxins incl. Trop. Dis

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“…This prokaryotic expression system is still applied for the production of many different recombinant allergens [103, 104, 105, 106, 107, 108]. In more recent years, several allergens were produced in eukaryotic expression systems like the yeast Pichia pastoris [109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127], insect cells [128, 129, 130, 131, 132, 133, 134, 135, 136], and tobacco plants [137, 138]. These systems facilitate post-translational modifications that do not (easily) occur in E. coli , like disulfide-bridge formation, hydroxylation of prolines, glycosylation.…”

Section: Recombinant Allergens For Application In Diagnostics and Immmentioning

confidence: 99%

Carbohydrate Epitopes and Their Relevance for the Diagnosis and Treatment of Allergic Diseases

Ree¹

2002

Int Arch Allergy Immunol

173

119

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Allergenicity of plant and invertebrate N-glycans has been shown to be caused by the presence of two typical nonmammalian substitutions: an α(1,3)-fucose linked to the proximal N-acetylglucosamine and a β(1,2)-xylose linked to the core mannose. IgE antibodies against these carbohydrate structures are induced upon exposure to pollen or after insect stings, and result in extensive cross-reactivity to plant and invertebrate foods. These cross-reactive IgE antibodies have been shown to possess variable degrees of biological activity, but have never been convincingly shown to induce clinical food allergy. The most likely explanation for this lack of clinical relevance has to be sought in a combination of epitope valency and antibody affinity. In diagnostic tests, these antibodies are at the basis of many false-positive test results for food allergy. Recombinant technologies offer the possibility to produce allergens that do not carry IgE-binding glycans. Whether their absence or presence is of importance for the application of recombinant allergens in immunotherapy is still largely unknown.

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“…The venom allergens of bees, fire ants and vespids of known sequences and structures are listed in table 2 [5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27]. The vespids include hornets, yellow jackets and paper wasps.…”

Section: Biochemical Studies Of Hymenoptera Venom Allergensmentioning

confidence: 99%

“…Recombinant proteins from insect or yeast cells have the native conformation of the natural proteins as they are folded into their native structure during secretion into culture medium, e.g. bee venom hyaluronidase [39], fire ant Sol i 2 and 3 [21, 22]and vespid antigen 5s [15, 18]. …”

Section: Biochemical Studies Of Hymenoptera Venom Allergensmentioning

confidence: 99%

Structure and Biology of Stinging Insect Venom Allergens

King

Spangfort²

2000

Int Arch Allergy Immunol

208

142

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Bees, fire ants and vespids cause insect sting allergy. These insects have unique as well as common venom allergens. Vespids, including hornets, paper wasps and yellow jackets, have common allergens. Bees and vespids have one common allergen with hyaluronidase activity; they also have unique allergens with different phospholipase activities. Fire ants and vespids have one common allergen, antigen 5 of unknown biologic activity. The common venom allergens with < 70% sequence identity have barely detectable levels of antigenic cross-reactivity. Possible uses of modified allergens for immunotherapy are described.

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

Cited by 30 publications

References 25 publications

Characterization of the allergen Sol gem 2 from the fire ant venom, Solenopsis geminata

Characterization of the allergen Sol gem 2 from the fire ant venom, Solenopsis geminata

Carbohydrate Epitopes and Their Relevance for the Diagnosis and Treatment of Allergic Diseases

Structure and Biology of Stinging Insect Venom Allergens

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