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1.
J. venom. anim. toxins incl. trop. dis ; 25: e.20190020, 2019. ilus, tab, graf
Article in English | LILACS, VETINDEX | ID: biblio-1484762

ABSTRACT

Background:Ant venoms express surface molecules that participate in antigen presentation involving pro- and anti-inflammatory cytokines. This work aims to investigate the expression of MHC-II, CD80 and CD86 on the polymorphonuclear cells (PMNs) in rats injected with samsum ant venom (SAV).Methods:Rats were divided into three groups - control, SAV-treated (intraperitoneal route, 600 μg/kg), and SAV-treated (subcutaneous route, 600 μg/kg). After five doses, animals were euthanized and samples collected for analysis.Results:The subcutaneous SAV-trated rats presented decreased levels of glutathione with increased cholesterol and triglyceride levels. Intraperitoneal SAV-treated animals displayed significantly reduced concentrations of both IFN-γ and IL-17 in comparison with the control group. However, intraperitoneal and subcutaneous SAV-treated rats were able to upregulate the expressions of MHC-II, CD80 and CD86 on PMNs in comparison with the control respectively. The histological examination showed severe lymphocyte depletion in the splenic white pulp of the intraperitoneal SAV-injected rats.Conclusion:Stimulation of PMNs by SAV leads to upregulation of MHC-II, CD 80, and CD 86, which plays critical roles in antigen presentation and consequently proliferation of T-cells. Subcutaneous route was more efficient than intraperitoneal by elevating MHC-II, CD80 and CD86 expression, disturbing oxidative stability and increasing lipogram concentration.


Subject(s)
Animals , Major Histocompatibility Complex , Oxidation-Reduction , Spider Venoms/analysis , Spider Venoms/immunology
2.
J. venom. anim. toxins incl. trop. dis ; 24: 6, 2018. tab, graf, ilus
Article in English | LILACS | ID: biblio-894167

ABSTRACT

Advancements in proteomics, including the technological improvement in instrumentation, have turned mass spectrometry into an indispensable tool in the study of venoms and toxins. In addition, the advance of nanoscale liquid chromatography coupled to nanoelectrospray mass spectrometry allows, due to its high sensitivity, the study of venoms from species previously left aside, such as ants. Ant venoms are a complex mixture of compounds used for defense, predation or communication purposes. The venom from Neoponera ants, a genus restricted to Neotropical regions, is known to have cytolytic, hemolytic, antimicrobial and insecticidal activities. Moreover, venoms from several Neoponera species have been compared and differences in their toxicity related to nesting habitat variation were reported. Therefore, the present study aimed to perform a deep peptidomic analysis of Neoponera villosa venom and a comparison of seasonal and nesting habitat variations using high-resolution mass spectrometry. Methods: Specimens of N. villosa ants were captured in Panga Natural Reserve (Uberlândia, MG, Brazil) from arboreal and ground-dwelling nests during summer and winter time. The venom glands were dissected, pooled and disrupted by ultra-sonic waves. The venom collected from different habitats (arboreal and ground-dwelling) and different seasons (summer and winter) was injected into a nanoACQUITY ULPC hyphened to a Q-Exactive Orbitrap mass spectrometer. The raw data were analyzed using PEAKS 7. Results: The results showed a molecular diversity of more than 500 peptides among these venoms, mostly in the mass range of 800-4000 Da. Mutations and post-translational modifications were described and differences among the venoms were observed. Part of the peptides matched with ponericins, a well-known antimicrobial peptide family. In addition, smaller fragments related to ponericins were also identified, suggesting that this class of antimicrobial peptide might undergo enzymatic cleavages. Conclusion: There are substantial differences among the venom of N. villosa ants collected in different seasons and from different nest habitats. The venom composition is affected by climate changes that influence prey availability and predator presence. Clearly, nano-LC-MS boosted the knowledge about ant venom, a rich source of unexplored and promising bioactive compounds.(AU)


Subject(s)
Animals , Peptides/analysis , Seasons , Mass Spectrometry/methods , Ant Venoms/analysis , Nesting Behavior
3.
J. venom. anim. toxins incl. trop. dis ; 24: 1-11, 2018. graf, tab
Article in English | LILACS, VETINDEX | ID: biblio-1484737

ABSTRACT

Background: Advancements in proteomics, including the technological improvement in instrumentation, have turned mass spectrometry into an indispensable tool in the study of venoms and toxins. In addition, the advance of nanoscale liquid chromatography coupled to nanoelectrospray mass spectrometry allows, due to its high sensitivity, the study of venoms from species previously left aside, such as ants. Ant venoms are a complex mixture of compounds used for defense, predation or communication purposes. The venom from Neoponera ants, a genus restricted to Neotropical regions, is known to have cytolytic, hemolytic, antimicrobial and insecticidal activities. Moreover, venoms from several Neoponera species have been compared and differences in their toxicity related to nesting habitat variation were reported. Therefore, the present study aimed to perform a deep peptidomic analysis of Neoponera villosa venom and a comparison of seasonal and nesting habitat variations using high-resolution mass spectrometry. Methods: Specimens of N. villosa ants were captured in Panga Natural Reserve (Uberlândia, MG, Brazil) from arboreal and ground-dwelling nests during summer and winter time. The venom glands were dissected, pooled and disrupted by ultra-sonic waves. The venom collected from different habitats (arboreal and ground-dwelling) and different seasons (summer and winter) was injected into a nanoACQUITY ULPC hyphened to a Q-Exactive Orbitrap mass spectrometer. The raw data were analyzed using PEAKS 7. Results: The results showed a molecular diversity of more than 500 peptides among these venoms, mostly in the mass range of 8004000 Da. Mutations and post-translational modifications were described and differences among the venoms were observed. Part of the peptides matched with ponericins, a well-known antimicrobial peptide family...


Subject(s)
Animals , Mass Spectrometry/methods , Peptide Mapping , Peptides/classification , Ant Venoms , Seasons
4.
J. venom. anim. toxins incl. trop. dis ; 18(3): 325-334, 2012. ilus, graf, tab
Article in English | LILACS, VETINDEX | ID: lil-649480

ABSTRACT

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 (PD50) 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.(AU)


Subject(s)
Animals , Body Weight , Allergens , Blotting, Western , Ant Venoms , Molecular Weight
5.
Yonsei Medical Journal ; : 281-287, 1992.
Article in English | WPRIM | ID: wpr-54328

ABSTRACT

Hypersensitivity to the stings of the Hymenoptera has been described since antiquity. The hypersensitive reactions to insect stings vary from minor skin reactions to severe and sometimes fatal anaphylaxis. Concerns about sting hypersensitivity have been increasing because of many incidents of allergic reactions of patients to the fire ant in the southern area of the United States as well as the harvester ant in some areas. We experienced one unique case with severe allergic reactions by ant of the Ectomomyrmex spp. of the subfamily Ponerinae, which is not a harvester ant. For three years the patient had been suffering from generalized allergic reactions such as anaphylaxis after the ant stings four-five attacks in a year. We determined that her reactions were due to specific IgE mediated type I hypersensitivity by the detection of a high level of specific IgE to the ant venom in her serum. The high level of specific IgG4 to the ant venom was also noted in her serum, however, the role of ant venom IgG4 was not clearly determined.


Subject(s)
Adult , Female , Humans , Anaphylaxis/etiology , Ant Venoms/immunology , Enzyme-Linked Immunosorbent Assay , Immunoglobulin E/analysis , Immunoglobulin G/classification
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