Nucleotide sequence of cDNA encoding the fire ant venom protein Sol i II

Schmidt, Margit; Walker, Robert B.; Hoffman, Donald R.; McConnell, Thomas J.

doi:10.1016/0014-5793(93)80053-w

Cited by 22 publications

(11 citation statements)

References 7 publications

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“…This result obviously indicated that spots A and B are different proteins; therefore, the protein in spot A was Sol gem 3, whereas the protein in spot B was Sol gem 2. These MS results The amino acid residues at the N-terminus of Sol gem 2 were determined to be ANEELKIIRK, a sequence that has 80% identity with that of the N-terminus of Sol i 2 (24,38). This result indicated that Sol gem 2 most likely shares high homology with allergen Sol i 2.…”

Section: Page Analysis and Protein Identification Of Crude Venommentioning

confidence: 82%

“…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%

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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: 82%

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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“…3,5 The primers used are shown in Table I. The mRNA was isolated by using the Promega (Madison, Wis) polyATtract system.…”

Section: Cloning Of the Phospholipasementioning

confidence: 99%

“…The primary sequences of these allergens have been determined by both amino acid sequencing 2 and cDNA cloning. 3,4 Sol i 3 is a member of the antigen 5 family. 2,5,6 Sol i 2, 3, and 4 have all been expressed by insect cells in immunoreactive form.…”

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confidence: 99%

Sol i 1, the phospholipase allergen of imported fire ant venom

Hoffman

Sakell

Schmidt

2005

Journal of Allergy and Clinical Immunology

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“…The first step in producing recombinant allergens can utilize any of several strategies including IgE immunoscreening of expression cDNA libraries [20, 21], phage display with immunoscreening [22, 23, 24, 25, 26]or DNA-based techniques such as reverse transcriptase-polymerase chain reaction (RT-PCR) which requires the determination of a partial amino acid sequence of the natural allergen or closely related protein [27, 28, 29, 30]. RT-PCR methods are particularly advantageous if the IgE-binding activity is dependent on posttranslational modifications, or if only a limited supply of specific IgE is available, and it also allows the isolation of multiple isoforms simultaneously [29, 31, 32, 33, 34, 35].…”

Section: Introductionmentioning

confidence: 99%

Expression Systems for Production of Recombinant Allergens

Schmidt

Hoffman

2002

Int Arch Allergy Immunol

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Recombinant allergenic proteins have been produced in a variety of different expression systems. This review gives examples of and compares prokaryotic expression systems, such as Escherichia coli, and eukaryotic systems including the yeasts, Saccharomyces cerevisiae and Pichia pastoris, baculovirus-insect cell systems, mammalian cell systems and plant systems. Important factors to consider in choosing an expression system are discussed and examples of applications are given.

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Nucleotide sequence of cDNA encoding the fire ant venom protein Sol i II

Cited by 22 publications

References 7 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

Sol i 1, the phospholipase allergen of imported fire ant venom

Expression Systems for Production of Recombinant Allergens

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