Venoms produced by the wasp (Vespid) family of stinging insects, including hornets; the venoms contain enzymes, biogenic amines, histamine releasing factors, kinins, toxic polypeptides, etc., and are similar to bee venoms.
Any of numerous winged hymenopterous insects of social as well as solitary habits and having formidable stings.
Venoms obtained from Apis mellifera (honey bee) and related species. They contain various enzymes, polypeptide toxins, and other substances, some of which are allergenic or immunogenic or both. These venoms were formerly used in rheumatism to stimulate the pituitary-adrenal system.
Bites and stings inflicted by insects.
Immunosuppression by the administration of increasing doses of antigen. Though the exact mechanism is not clear, the therapy results in an increase in serum levels of allergen-specific IMMUNOGLOBULIN G, suppression of specific IgE, and an increase in suppressor T-cell activity.
Venoms from snakes of the subfamily Crotalinae or pit vipers, found mostly in the Americas. They include the rattlesnake, cottonmouth, fer-de-lance, bushmaster, and American copperhead. Their venoms contain nontoxic proteins, cardio-, hemo-, cyto-, and neurotoxins, and many enzymes, especially phospholipases A. Many of the toxins have been characterized.
A phospholipase that hydrolyzes the acyl group attached to the 1-position of PHOSPHOGLYCERIDES.
Poisonous animal secretions forming fluid mixtures of many different enzymes, toxins, and other substances. These substances are produced in specialized glands and secreted through specialized delivery systems (nematocysts, spines, fangs, etc.) for disabling prey or predator.
An acute hypersensitivity reaction due to exposure to a previously encountered ANTIGEN. The reaction may include rapidly progressing URTICARIA, respiratory distress, vascular collapse, systemic SHOCK, and death.
Ubiquitously-expressed tetraspanin proteins that are found in late ENDOSOMES and LYSOSOMES and have been implicated in intracellular transport of proteins.
Venoms from snakes of the genus Naja (family Elapidae). They contain many specific proteins that have cytotoxic, hemolytic, neurotoxic, and other properties. Like other elapid venoms, they are rich in enzymes. They include cobramines and cobralysins.
Venoms from SNAKES of the viperid family. They tend to be less toxic than elapid or hydrophid venoms and act mainly on the vascular system, interfering with coagulation and capillary membrane integrity and are highly cytotoxic. They contain large amounts of several enzymes, other factors, and some toxins.
An immunoglobulin associated with MAST CELLS. Overexpression has been associated with allergic hypersensitivity (HYPERSENSITIVITY, IMMEDIATE).
Granular leukocytes characterized by a relatively pale-staining, lobate nucleus and cytoplasm containing coarse dark-staining granules of variable size and stainable by basic dyes.
Venoms from snakes of the family Elapidae, including cobras, kraits, mambas, coral, tiger, and Australian snakes. The venoms contain polypeptide toxins of various kinds, cytolytic, hemolytic, and neurotoxic factors, but fewer enzymes than viper or crotalid venoms. Many of the toxins have been characterized.
Venoms of arthropods of the order Araneida of the ARACHNIDA. The venoms usually contain several protein fractions, including ENZYMES, hemolytic, neurolytic, and other TOXINS, BIOLOGICAL.
Altered reactivity to an antigen, which can result in pathologic reactions upon subsequent exposure to that particular antigen.
Venoms from animals of the phylum Arthropoda. Those most investigated are from scorpions and spiders of the class Arachnidae and from ant, bee, and wasp families of the Insecta order Hymenoptera. The venoms contain protein toxins, enzymes, and other bioactive substances and may be lethal to man.
Venoms from animals of the order Scorpionida of the class Arachnida. They contain neuro- and hemotoxins, enzymes, and various other factors that may release acetylcholine and catecholamines from nerve endings. Of the several protein toxins that have been characterized, most are immunogenic.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Antigen-type substances that produce immediate hypersensitivity (HYPERSENSITIVITY, IMMEDIATE).
The conjugation product of LEUKOTRIENE A4 and glutathione. It is the major arachidonic acid metabolite in macrophages and human mast cells as well as in antigen-sensitized lung tissue. It stimulates mucus secretion in the lung, and produces contractions of nonvascular and some VASCULAR SMOOTH MUSCLE. (From Dictionary of Prostaglandins and Related Compounds, 1990)
Epicutaneous or intradermal application of a sensitizer for demonstration of either delayed or immediate hypersensitivity. Used in diagnosis of hypersensitivity or as a test for cellular immunity.
A genus of poisonous snakes of the VIPERIDAE family. About 50 species are known and all are found in tropical America and southern South America. Bothrops atrox is the fer-de-lance and B. jararaca is the jararaca. (Goin, Goin, and Zug, Introduction to Herpetology, 3d ed, p336)
The protein complement of an organism coded for by its genome.
A mass spectrometry technique used for analysis of nonvolatile compounds such as proteins and macromolecules. The technique involves preparing electrically charged droplets from analyte molecules dissolved in solvent. The electrically charged droplets enter a vacuum chamber where the solvent is evaporated. Evaporation of solvent reduces the droplet size, thereby increasing the coulombic repulsion within the droplet. As the charged droplets get smaller, the excess charge within them causes them to disintegrate and release analyte molecules. The volatilized analyte molecules are then analyzed by mass spectrometry.

Novel gating mechanism of polyamine block in the strong inward rectifier K channel Kir2.1. (1/307)

Inward rectifying K channels are essential for maintaining resting membrane potential and regulating excitability in many cell types. Previous studies have attributed the rectification properties of strong inward rectifiers such as Kir2.1 to voltage-dependent binding of intracellular polyamines or Mg to the pore (direct open channel block), thereby preventing outward passage of K ions. We have studied interactions between polyamines and the polyamine toxins philanthotoxin and argiotoxin on inward rectification in Kir2.1. We present evidence that high affinity polyamine block is not consistent with direct open channel block, but instead involves polyamines binding to another region of the channel (intrinsic gate) to form a blocking complex that occludes the pore. This interaction defines a novel mechanism of ion channel closure.  (+info)

Nucleoside diphosphate kinase activity in soluble transducin preparations biochemical properties and possible role of transducin-beta as phosphorylated enzyme intermediate. (2/307)

Known nucleoside diphosphate kinases (NDPKs) are oligomers of 17-23-kDa subunits and catalyze the reaction N1TP + N2DP --> N1DP + N2TP via formation of a histidine-phosphorylated enzyme intermediate. NDPKs are involved in the activation of heterotrimeric GTP-binding proteins (G-proteins) by catalyzing the formation of GTP from GDP, but the properties of G-protein-associated NDPKs are still incompletely known. The aim of our present study was to characterize NDPK in soluble preparations of the retinal G-protein transducin. The NDPK is operationally referred to as transducin-NDPK. Like known NDPKs, transducin-NDPK utilizes NTPs and phosphorothioate analogs of NTPs as substrates. GDP was a more effective phosphoryl group acceptor at transducin-NDPK than ADP and CDP, and guanosine 5'-[gamma-thio]triphosphate (GTP[S]) was a more effective thiophosphoryl group donor than adenosine 5'-[gamma-thio]triphosphate (ATP[S]). In contrast with their action on known NDPKs, mastoparan and mastoparan 7 had no stimulatory effect on transducin-NDPK. Guanosine 5'-[beta, gamma-imido]triphosphate (p[NH]ppG) potentiated [3H]GTP[S] formation from [3H]GDP and ATP[S] but not [3H]GTP[S] formation from [3H]GDP and GTP[S]. Depending on the thiophosphoryl group acceptor and donor, [3H]NTP[S] formation was differentially regulated by Mg2+, Mn2+, Co2+, Ca2+ and Zn2+. [gamma-32P]ATP and [gamma-32P]GTP [32P]phosphorylated, and [35S]ATP[S] [35S]thiophosphorylated, a 36-kDa protein comigrating with transducin-beta. p[NH]ppG potentiated [35S]thiophosphorylation of the 36-kDa protein. 32P-labeling of the 36-kDa protein showed characteristics of histidine phosphorylation. There was no evidence for (thio)phosphorylation of 17-23-kDa proteins. Our data show the following: (a) soluble transducin preparations contain a GDP-prefering and guanine nucleotide-regulated NDPK; (b) transducin-beta may serve as a (thio)phosphorylated NDPK intermediate; (c) transducin-NDPK is distinct from known NDPKs and may consist of multiple kinases or a single kinase with multiple regulatory domains.  (+info)

Inverse agonist activity of pirenzepine at M2 muscarinic acetylcholine receptors. (3/307)

1. The intrinsic properties of muscarinic ligands were studied through their binding properties and their abilities to modulate the GTPase activity of G proteins coupled to muscarinic M2 receptors in pig atrial sarcolemma. 2. Competition binding experiments were performed with [3H]-oxotremorine-M to assess the affinity of receptors coupled to G proteins (R*), with [3H]-N-methylscopolamine ([3H]-NMS) to estimate the affinities of coupled and uncoupled receptors (R*+R) and with [3H]-NMS in the presence of GppNHp to assess the affinity of uncoupled receptors (R). 3. The ranking of Ki values for the agonist carbachol was R*<R*+R>R (174, 155, 115 nM), suggesting inverse agonism. 4. The Vmax of the basal high affinity GTPase activity of pig atrial sarcolemma was increased by mastoparan and decreased by GPAnt-2 indicating the relevance of this activity to G proteins coupled to receptors (R*). The K(M) value (0.26-0.33 microM) was not modified by mastoparan or GPAnt-2. 5. Carbachol increased the Vmax of GTP hydrolysis (EC50 8.1+/-0.3 microM), whereas atropine and AF-DX 116, up to 1 mM, did not modify it. Pirenzepine decreased the Vmax of GTP hydrolysis (EC50 77.5+/-10.3 microM). This effect was enhanced when KCI was substituted for NaCl (EC50 11.0+/-0.8 microM) and was antagonized by atropine and AF-DX 116 (IC50 0.91+/-0.71 and 197+/-85 nM). 6. Pirenzepine is proposed as an inverse agonist and atropine and AF-DX 116 as neutral antagonists at the muscarinic M2 receptor.  (+info)

Modulation of antibacterial peptide activity by products of Porphyromonas gingivalis and Prevotella spp. (4/307)

This study investigated the ability of anaerobic periodontal bacteria to inactivate and resist killing by antimicrobial peptides through production of extracellular proteases. Antibacterial activities of peptides were assessed in a double-layer agarose diffusion assay, and MICs and MBCs were determined in broth microdilution assays. Culture supernates of Porphyromonas gingivalis and Prevotella spp. inactivated mastoparan, magainin II and cecropin B whilst Gram-positive oral supragingival bacteria had no effect. Inactivation was prevented by protease inhibitors and was unaffected by 45% human serum. Purified proteases from the periodontopathogen Porph. gingivalis inactivated peptides [cecropin B, brevinin, CAMEL (cecropin A 1-7 + melittin 2-9), mastoparan] as would be predicted from the amino acid sequences of the peptides and the known bond specificities of these Arg-x and Lys-x enzymes. MALDI-TOF MS revealed that inactivation of cecropin B by Porph. gingivalis protease was due to specific cleavage of the molecule. Inactivation of cecropin B by proteases took 10-15 min. Paradoxically, MICs of cecropin B against Porph. gingivalis and Prevotella intermedia were low, while Prevotella nigrescens was resistant, suggesting that production of proteases alone is insufficient to protect Porph. gingivalis and Prev. intermedia from the action of antimicrobial peptides. Thus, antimicrobial peptides could be developed as therapeutic agents targeted against specific periodontal pathogens.  (+info)

The mechanism of inhibition of the Ca2+-ATPase by mastoparan. Mastoparan abolishes cooperative ca2+ binding. (5/307)

The amphiphilic peptide mastoparan, isolated from wasp venom, is a potent inhibitor of the sarcoplasmic reticulum Ca2+-ATPase. At pH 7. 2, ATPase activity is inhibited with an inhibitory constant (Ki) of 1 +/- 0.13 microM. Mastoparan shifts the E2-E1 equilibrium toward E1 and may affect the regulatory ATP binding site. The peptide also decreases the affinity of the ATPase for Ca2+ and abolishes the cooperativity of Ca2+ binding. In the presence of mastoparan, the two Ca2+ ions bind independently of one another. Our results appear to support the model that describes the relationship between the two Ca2+ binding sites as "side-by-side," because this model allows the possibility of independent Ca2+ entry to the two sites. Mastoparan shifts the steady-state equilibrium between E1'Ca2 and E1'Ca2.P toward E1'Ca2.P, by possibly affecting the conformational change that follows ATP binding. The peptide also causes a reduction in the levels of phosphoenzyme formed from [32P]Pi. Some analogues of mastoparan were also tested and were found to cause inhibition of the Ca2+-ATPase in the range of 2-4 microM. The inhibitory action of mastoparan and its analogues appears dependent on their ability to form alpha-helices in membranes.  (+info)

Peptides derived from the human transferrin receptor stimulate endosomal acidification via a Gi-type protein. (6/307)

Peptides derived from the human transferrin receptor stimulate endosomal acidification via a Gi-type protein. BACKGROUND: Acidification of the endosomal compartment is a prerequisite for intracellular processing of endocytosed complexes. Endosomal acidification is accomplished by an H+-ATPase, in parallel with a Cl- conductance. Previous studies from our laboratory have demonstrated that endosomal acidification is modulated by a pertussis toxin-sensitive mechanism, suggesting that endosomal acidification could be regulated through a self-contained signal transduction pathway. This study was designed to test this hypothesis using the transferrin receptor as a model. METHODS: Synthetic peptides corresponding to a region of the cytosolic domain of the transferrin receptor and containing a KPKR sequence were used to stimulate endosomal acidification in a G-protein-dependent manner. RESULTS: Peptides activated the Gi, as evidenced by stimulation of the rate of GTPgammaS binding. A transferrin receptor peptide that lacked the KPKR sequence did not stimulate endosomal acidification and failed to promote GTPgammaS binding to Gi proteins. CONCLUSIONS: These results demonstrate that regulation of endosomal acidification can be achieved, in part, through a Gi-mediated signal transduction pathway. These findings suggest that regulation of endosomal acidification through such a pathway may facilitate intracellular processing of the transferrin receptor.  (+info)

Protein kinase C and a calcium-independent phospholipase are required for IgG-mediated phagocytosis by Mono-Mac-6 cells. (7/307)

Mono-Mac-6 (MM6) human monocytes ingest IgG-opsonized particles better than other human cell lines. We compared the phagocytic signaling pathway in MM6 with human monocytes. MM6 expressed FcgammaRI at levels similar to monocytes, whereas FcRgammaII expression was approximately double. MM6 ingested IgG-opsonized erythrocytes (EIgG) in a calcium-independent manner. Incubation of MM6 with bromoenol lactone, an inhibitor of the phagocytic phospholipase (pPL), coordinately decreased phagocytosis and pPL activity. This inhibition was overcome by exogenous arachidonic acid, suggesting that phagocytosis requires pPL activation and arachidonic acid release. MM6 phagocytosis was inhibited with staurosporine and activated with diacylglycerol, supporting a role for protein kinase C (PKC) in this process. The pPL activators mastoparan and melittin restored phagocytosis to PKC-inhibited cells, suggesting that pPL lies downstream from PKC. These results suggest that the MM6 signal transduction pathway for IgG-mediated phagocytosis is similar to that of monocytes (PKC-->pPL-->arachidonic acid-->phagocytosis). The results are discussed in the context of the finding that MM6 exhibit low phagocytosis relative to monocytes and thus may represent an attractive cell line for molecular manipulation in "recovery of function" studies.  (+info)

Endothelin-1 activates p38 mitogen-activated protein kinase and cytosolic phospholipase A2 in cat iris sphincter smooth muscle cells. (8/307)

We have shown previously that cytosolic phospholipase A(2) (cPLA(2)) is responsible for endothelin-1-induced release of arachidonic acid for prostaglandin synthesis in cat iris sphincter smooth muscle (CISM) cells [Husain and Abdel-Latif (1998) Biochim. Biophys. Acta 1392, 127-144]. Here we show that p38 mitogen-activated protein (MAP) kinase, but not p42/p44 MAP kinases, plays an important role in the phosphorylation and activation of cPLA(2) in endothelin-1-stimulated CISM cells. This conclusion is supported by the following findings. Both p38 MAP kinase and p42/p44 MAP kinases were present in the CISM cells and both were activated by endothelin-1. SB203580, a potent specific inhibitor of p38 MAP kinase, but not the p42/p44 MAP kinases specific inhibitor, PD98059, markedly suppressed endothelin-1-enhanced cPLA(2) phosphorylation, cPLA(2) activity and arachidonic acid release. The addition of endothelin-1 resulted in the phosphorylation and activation of cPLA(2). Endothelin-1 stimulated p38 MAP kinase activity in a time- and concentration-dependent manner, and these effects were mediated through the endothelin-A receptor subtype. The protein kinase C (PKC) inhibitor, RO 31-8220, had no inhibitory effect on endothelin-1-induced p38 MAP kinase activation, suggesting that endothelin-1 activation of p38 MAP kinase is independent of PKC. Pertussis toxin inhibited both endothelin-1 and mastoparan stimulation of p38 MAP kinase activity and arachidonic acid release. The inhibitory effects of pertussis toxin are not mediated through cAMP formation. Mastoparan-stimulated [(3)H]arachidonic acid release and cPLA(2) activation was inhibited by SB203580, but not by RO 31-8220. These data suggest that endothelin-1 binds to the endothelin-A receptor to activate the Gi-protein which, through a series of kinases, leads to the activation of p38 MAP kinase and subsequently to phosphorylation and activation of cPLA(2). Activation of cPLA(2) leads to the liberation of arachidonic acid from membrane phospholipids. The ability of the activated endothelin-A receptor, which is coupled to both Gq- and Gi-proteins, to recruit and activate this complex signal transduction pathway remains to be elucidated. Further studies on the mechanism of these relationships could provide important information about the functions of p38 MAP kinase in smooth muscle.  (+info)

Wasp venoms are complex mixtures of bioactive molecules produced by wasps (Hymenoptera: Vespidae) to defend themselves and paralyze prey. The main components include:

1. Phospholipases A2 (PLA2): Enzymes that can cause pain, inflammation, and damage to cell membranes.
2. Hyaluronidase: An enzyme that helps spread the venom by breaking down connective tissues.
3. Proteases: Enzymes that break down proteins and contribute to tissue damage and inflammation.
4. Antigen 5: A major allergen that can cause severe allergic reactions (anaphylaxis) in sensitive individuals.
5. Mastoparan: A peptide that induces histamine release, leading to localized inflammation and pain.
6. Neurotoxins: Some wasp venoms contain neurotoxins that can cause paralysis or neurological symptoms.

The composition of wasp venoms may vary among species, and individual sensitivity to the components can result in different reactions ranging from localized pain, swelling, and redness to systemic allergic responses.

I'm sorry for any confusion, but "wasps" is not a term that has a specific medical definition. Wasps are a type of insect in the order Hymenoptera, and some people can have allergic reactions to their stings. However, there is no medical condition or disease specifically associated with wasps. If you have any specific medical concerns or questions, I would be happy to try to help if I can!

Bee venom is a poisonous substance that a honeybee (Apis mellifera) injects into the skin of a person or animal when it stings. It's produced in the venom gland and stored in the venom sac of the bee. Bee venom is a complex mixture of proteins, peptides, and other compounds. The main active components of bee venom include melittin, apamin, and phospholipase A2.

Melittin is a toxic peptide that causes pain, redness, and swelling at the site of the sting. It also has hemolytic (red blood cell-destroying) properties. Apamin is a neurotoxin that can affect the nervous system and cause neurological symptoms in severe cases. Phospholipase A2 is an enzyme that can damage cell membranes and contribute to the inflammatory response.

Bee venom has been used in traditional medicine for centuries, particularly in China and other parts of Asia. It's believed to have anti-inflammatory, analgesic (pain-relieving), and immunomodulatory effects. Some studies suggest that bee venom may have therapeutic potential for a variety of medical conditions, including rheumatoid arthritis, multiple sclerosis, and chronic pain. However, more research is needed to confirm these findings and to determine the safety and efficacy of bee venom therapy.

It's important to note that bee stings can cause severe allergic reactions (anaphylaxis) in some people, which can be life-threatening. If you experience symptoms such as difficulty breathing, rapid heartbeat, or hives after being stung by a bee, seek medical attention immediately.

Insect bites and stings refer to the penetration of the skin by insects, such as mosquitoes, fleas, ticks, or bees, often resulting in localized symptoms including redness, swelling, itching, and pain. The reaction can vary depending on the individual's sensitivity and the type of insect. In some cases, systemic reactions like anaphylaxis may occur, which requires immediate medical attention. Treatment typically involves relieving symptoms with topical creams, antihistamines, or in severe cases, epinephrine. Prevention measures include using insect repellent and protective clothing.

Desensitization, Immunologic is a medical procedure that aims to decrease the immune system's response to an allergen. This is achieved through the controlled exposure of the patient to gradually increasing amounts of the allergen, ultimately leading to a reduction in the severity of allergic reactions upon subsequent exposures. The process typically involves administering carefully measured and incrementally larger doses of the allergen, either orally, sublingually (under the tongue), or by injection, under medical supervision. Over time, this repeated exposure can help the immune system become less sensitive to the allergen, thereby alleviating allergic symptoms.

The specific desensitization protocol and administration method may vary depending on the type of allergen and individual patient factors. Immunologic desensitization is most commonly used for environmental allergens like pollen, dust mites, or pet dander, as well as insect venoms such as bee or wasp stings. It is important to note that this procedure should only be performed under the close supervision of a qualified healthcare professional, as there are potential risks involved, including anaphylaxis (a severe and life-threatening allergic reaction).

Crotalid venoms are the toxic secretions produced by the members of the Crotalinae subfamily, also known as pit vipers. This group includes rattlesnakes, cottonmouths (or water moccasins), and copperheads, which are native to the Americas, as well as Old World vipers found in Asia and Europe, such as gaboon vipers and saw-scaled vipers.

Crotalid venoms are complex mixtures of various bioactive molecules, including enzymes, proteins, peptides, and other low molecular weight components. They typically contain a variety of pharmacologically active components, such as hemotoxic and neurotoxic agents, which can cause extensive local tissue damage, coagulopathy, cardiovascular dysfunction, and neuromuscular disorders in the victim.

The composition of crotalid venoms can vary significantly between different species and even among individual specimens within the same species. This variability is influenced by factors such as geographic location, age, sex, diet, and environmental conditions. As a result, the clinical manifestations of crotalid envenomation can be highly variable, ranging from mild local reactions to severe systemic effects that may require intensive medical treatment and supportive care.

Crotalid venoms have been the subject of extensive research in recent years due to their potential therapeutic applications. For example, certain components of crotalid venoms have shown promise as drugs for treating various medical conditions, such as cardiovascular diseases, pain, and inflammation. However, further studies are needed to fully understand the mechanisms of action of these venom components and to develop safe and effective therapies based on them.

Phospholipase A1 (PLA1) is an enzyme that catalyzes the hydrolysis of the ester bond at the sn-1 position of glycerophospholipids, resulting in the production of free fatty acids and lysophospholipids. This enzyme plays a crucial role in various biological processes, including cell signaling, membrane remodeling, and inflammation. PLA1 is widely distributed in nature and can be found in different organisms, such as bacteria, plants, and animals. In humans, PLA1 is involved in several physiological and pathological conditions, including lipid metabolism, atherosclerosis, neurodegenerative diseases, and cancer.

Venom is a complex mixture of toxic compounds produced by certain animals, such as snakes, spiders, scorpions, and marine creatures like cone snails and stonefish. These toxic substances are specifically designed to cause damage to the tissues or interfere with the normal physiological processes of other organisms, which can lead to harmful or even lethal effects.

Venoms typically contain a variety of components, including enzymes, peptides, proteins, and small molecules, each with specific functions that contribute to the overall toxicity of the mixture. Some of these components may cause localized damage, such as tissue necrosis or inflammation, while others can have systemic effects, impacting various organs and bodily functions.

The study of venoms, known as toxinology, has important implications for understanding the evolution of animal behavior, developing new therapeutics, and advancing medical treatments for envenomation (the process of being poisoned by venom). Additionally, venoms have been used in traditional medicine for centuries, and ongoing research continues to uncover novel compounds with potential applications in modern pharmacology.

Anaphylaxis is a severe, life-threatening systemic allergic reaction that occurs suddenly after exposure to an allergen (a substance that triggers an allergic reaction) to which the person has previously been sensitized. The symptoms of anaphylaxis include rapid onset of symptoms such as itching, hives, swelling of the throat and tongue, difficulty breathing, wheezing, cough, chest tightness, rapid heartbeat, hypotension (low blood pressure), shock, and in severe cases, loss of consciousness and death. Anaphylaxis is a medical emergency that requires immediate treatment with epinephrine (adrenaline) and other supportive measures to stabilize the patient's condition.

CD63 is a type of protein found on the surface of certain cells, including platelets and some immune cells. It is also known as granulophysin and is a member of the tetraspanin family of proteins. CD63 is often used as a marker for activated immune cells, particularly those involved in the immune response to viruses and other pathogens.

In the context of antigens, CD63 may be referred to as a target antigen, which is a molecule on the surface of a cell that can be recognized by the immune system. In this case, CD63 may be targeted by antibodies produced by the immune system in response to an infection or other stimulus.

It's important to note that while CD63 is often used as a marker for activated immune cells, it is not itself an antigen in the sense of being a foreign molecule that can elicit an immune response. Rather, it is a protein that can be targeted by the immune system in certain contexts.

Cobra venoms are a type of snake venom that is produced by cobras, which are members of the genus Naja in the family Elapidae. These venoms are complex mixtures of proteins and other molecules that have evolved to help the snake immobilize and digest its prey.

Cobra venoms typically contain a variety of toxic components, including neurotoxins, hemotoxins, and cytotoxins. Neurotoxins target the nervous system and can cause paralysis and respiratory failure. Hemotoxins damage blood vessels and tissues, leading to internal bleeding and organ damage. Cytotoxins destroy cells and can cause tissue necrosis.

The specific composition of cobra venoms can vary widely between different species of cobras, as well as between individual snakes of the same species. Some cobras have venoms that are primarily neurotoxic, while others have venoms that are more hemotoxic or cytotoxic. The potency and effects of cobra venoms can also be influenced by factors such as the age and size of the snake, as well as the temperature and pH of the environment.

Cobra bites can be extremely dangerous and even fatal to humans, depending on the species of cobra, the amount of venom injected, and the location of the bite. Immediate medical attention is required in the event of a cobra bite, including the administration of antivenom therapy to neutralize the effects of the venom.

"Viper venoms" refer to the toxic secretions produced by members of the Viperidae family of snakes, which include pit vipers (such as rattlesnakes, copperheads, and cottonmouths) and true vipers (like adders, vipers, and gaboon vipers). These venoms are complex mixtures of proteins, enzymes, and other bioactive molecules that can cause a wide range of symptoms in prey or predators, including local tissue damage, pain, swelling, bleeding, and potentially life-threatening systemic effects such as coagulopathy, cardiovascular shock, and respiratory failure.

The composition of viper venoms varies widely between different species and even among individuals within the same species. However, many viper venoms contain a variety of enzymes (such as phospholipases A2, metalloproteinases, and serine proteases) that can cause tissue damage and disrupt vital physiological processes in the victim. Additionally, some viper venoms contain neurotoxins that can affect the nervous system and cause paralysis or other neurological symptoms.

Understanding the composition and mechanisms of action of viper venoms is important for developing effective treatments for venomous snakebites, as well as for gaining insights into the evolution and ecology of these fascinating and diverse creatures.

Immunoglobulin E (IgE) is a type of antibody that plays a key role in the immune response to parasitic infections and allergies. It is produced by B cells in response to stimulation by antigens, such as pollen, pet dander, or certain foods. Once produced, IgE binds to receptors on the surface of mast cells and basophils, which are immune cells found in tissues and blood respectively. When an individual with IgE antibodies encounters the allergen again, the cross-linking of IgE molecules bound to the FcฮตRI receptor triggers the release of mediators such as histamine, leukotrienes, prostaglandins, and various cytokines from these cells. These mediators cause the symptoms of an allergic reaction, such as itching, swelling, and redness. IgE also plays a role in protecting against certain parasitic infections by activating eosinophils, which can kill the parasites.

In summary, Immunoglobulin E (IgE) is a type of antibody that plays a crucial role in the immune response to allergens and parasitic infections, it binds to receptors on the surface of mast cells and basophils, when an individual with IgE antibodies encounters the allergen again, it triggers the release of mediators from these cells causing the symptoms of an allergic reaction.

Basophils are a type of white blood cell that are part of the immune system. They are granulocytes, which means they contain granules filled with chemicals that can be released in response to an infection or inflammation. Basophils are relatively rare, making up less than 1% of all white blood cells.

When basophils become activated, they release histamine and other chemical mediators that can contribute to allergic reactions, such as itching, swelling, and redness. They also play a role in inflammation, helping to recruit other immune cells to the site of an infection or injury.

Basophils can be identified under a microscope based on their characteristic staining properties. They are typically smaller than other granulocytes, such as neutrophils and eosinophils, and have a multi-lobed nucleus with dark purple-staining granules in the cytoplasm.

While basophils play an important role in the immune response, abnormal levels of basophils can be associated with various medical conditions, such as allergies, infections, and certain types of leukemia.

Elapid venoms are the toxic secretions produced by elapid snakes, a family of venomous snakes that includes cobras, mambas, kraits, and coral snakes. These venoms are primarily composed of neurotoxins, which can cause paralysis and respiratory failure in prey or predators.

Elapid venoms work by targeting the nervous system, disrupting communication between the brain and muscles. This results in muscle weakness, paralysis, and eventually respiratory failure if left untreated. Some elapid venoms also contain hemotoxins, which can cause tissue damage, bleeding, and other systemic effects.

The severity of envenomation by an elapid snake depends on several factors, including the species of snake, the amount of venom injected, the location of the bite, and the size and health of the victim. Prompt medical treatment is essential in cases of elapid envenomation, as the effects of the venom can progress rapidly and lead to serious complications or death if left untreated.

Spider venoms are complex mixtures of bioactive compounds produced by the specialized glands of spiders. These venoms are primarily used for prey immobilization and defense. They contain a variety of molecules such as neurotoxins, proteases, peptides, and other biologically active substances. Different spider species have unique venom compositions, which can cause different reactions when they bite or come into contact with humans or other animals. Some spider venoms can cause mild symptoms like pain and swelling, while others can lead to more severe reactions such as tissue necrosis or even death in extreme cases.

Hypersensitivity is an exaggerated or inappropriate immune response to a substance that is generally harmless to most people. It's also known as an allergic reaction. This abnormal response can be caused by various types of immunological mechanisms, including antibody-mediated reactions (types I, II, and III) and cell-mediated reactions (type IV). The severity of the hypersensitivity reaction can range from mild discomfort to life-threatening conditions. Common examples of hypersensitivity reactions include allergic rhinitis, asthma, atopic dermatitis, food allergies, and anaphylaxis.

Arthropod venoms are toxic secretions produced by the venom glands of various arthropods, such as spiders, scorpions, insects, and marine invertebrates. These venoms typically contain a complex mixture of bioactive molecules, including peptides, proteins, enzymes, and small molecules, which can cause a range of symptoms and effects in humans and other animals.

The specific composition of arthropod venoms varies widely depending on the species and can be tailored to serve various functions, such as prey immobilization, defense, or predation. Some arthropod venoms contain neurotoxins that can disrupt nerve function and cause paralysis, while others may contain cytotoxins that damage tissues or hemotoxins that affect the blood and cardiovascular system.

Arthropod venoms have been studied for their potential therapeutic applications, as some of their bioactive components have shown promise in treating various medical conditions, including pain, inflammation, and neurological disorders. However, it is important to note that arthropod venoms can also cause severe allergic reactions and other adverse effects in susceptible individuals, making it essential to exercise caution when handling or coming into contact with venomous arthropods.

Scorpion venoms are complex mixtures of neurotoxins, enzymes, and other bioactive molecules that are produced by the venom glands of scorpions. These venoms are primarily used for prey immobilization and defense. The neurotoxins found in scorpion venoms can cause a variety of symptoms in humans, including pain, swelling, numbness, and in severe cases, respiratory failure and death.

Scorpion venoms are being studied for their potential medical applications, such as in the development of new pain medications and insecticides. Additionally, some components of scorpion venom have been found to have antimicrobial properties and may be useful in the development of new antibiotics.

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

An allergen is a substance that can cause an allergic reaction in some people. These substances are typically harmless to most people, but for those with allergies, the immune system mistakenly identifies them as threats and overreacts, leading to the release of histamines and other chemicals that cause symptoms such as itching, sneezing, runny nose, rashes, hives, and difficulty breathing. Common allergens include pollen, dust mites, mold spores, pet dander, insect venom, and certain foods or medications. When a person comes into contact with an allergen, they may experience symptoms that range from mild to severe, depending on the individual's sensitivity to the substance and the amount of exposure.

Leukotriene C4 (LTC4) is a type of lipid mediator called a cysteinyl leukotriene, which is derived from arachidonic acid through the 5-lipoxygenase pathway. It is primarily produced by activated mast cells and basophils, and to a lesser extent by eosinophils, during an allergic response or inflammation.

LTC4 plays a crucial role in the pathogenesis of asthma and other allergic diseases by causing bronchoconstriction, increased vascular permeability, mucus secretion, and recruitment of inflammatory cells to the site of inflammation. It exerts its effects by binding to cysteinyl leukotriene receptors (CysLT1 and CysLT2) found on various cell types, including airway smooth muscle cells, bronchial epithelial cells, and immune cells.

LTC4 is rapidly metabolized to Leukotriene D4 (LTD4) and then to Leukotriene E4 (LTE4) by enzymes such as gamma-glutamyl transpeptidase and dipeptidases, which are present in the extracellular space. These metabolites also have biological activity and contribute to the inflammatory response.

Inhibitors of 5-lipoxygenase or leukotriene receptor antagonists are used as therapeutic agents for the treatment of asthma, allergies, and other inflammatory conditions.

Skin tests are medical diagnostic procedures that involve the application of a small amount of a substance to the skin, usually through a scratch, prick, or injection, to determine if the body has an allergic reaction to it. The most common type of skin test is the patch test, which involves applying a patch containing a small amount of the suspected allergen to the skin and observing the area for signs of a reaction, such as redness, swelling, or itching, over a period of several days. Another type of skin test is the intradermal test, in which a small amount of the substance is injected just beneath the surface of the skin. Skin tests are used to help diagnose allergies, including those to pollen, mold, pets, and foods, as well as to identify sensitivities to medications, chemicals, and other substances.

"Bothrops" is a genus of venomous snakes commonly known as lancehead vipers, found primarily in Central and South America. The name "Bothrops" comes from the Greek words "bothros," meaning pit, and "ops," meaning face, referring to the deep pits on the sides of their heads that help them detect heat and locate prey. These snakes are known for their aggressive behavior and potent venom, which can cause severe pain, swelling, tissue damage, and potentially life-threatening systemic effects if left untreated.

The genus "Bothrops" includes over 30 species of pit vipers, many of which are considered medically important due to their ability to inflict serious envenomations in humans. Some notable examples include Bothrops asper (the terciopelo or fer-de-lance), Bothrops atrox (the common lancehead), and Bothrops jararaca (the jararaca).

If you encounter a snake of this genus, it is essential to seek medical attention immediately if bitten, as the venom can cause significant harm if not treated promptly.

The proteome is the entire set of proteins produced or present in an organism, system, organ, or cell at a certain time under specific conditions. It is a dynamic collection of protein species that changes over time, responding to various internal and external stimuli such as disease, stress, or environmental factors. The study of the proteome, known as proteomics, involves the identification and quantification of these protein components and their post-translational modifications, providing valuable insights into biological processes, functional pathways, and disease mechanisms.

Mass spectrometry with electrospray ionization (ESI-MS) is an analytical technique used to identify and quantify chemical species in a sample based on the mass-to-charge ratio of charged particles. In ESI-MS, analytes are ionized through the use of an electrospray, where a liquid sample is introduced through a metal capillary needle at high voltage, creating an aerosol of charged droplets. As the solvent evaporates, the analyte molecules become charged and can be directed into a mass spectrometer for analysis.

ESI-MS is particularly useful for the analysis of large biomolecules such as proteins, peptides, and nucleic acids, due to its ability to gently ionize these species without fragmentation. The technique provides information about the molecular weight and charge state of the analytes, which can be used to infer their identity and structure. Additionally, ESI-MS can be interfaced with separation techniques such as liquid chromatography (LC) for further purification and characterization of complex samples.

How much wasp venom can kill you?. How much wasp venom can kill you?. (See also Introduction to Bites and Stings.) The average ... Is wasp poison dangerous to humans?. A wasps stinger contains venom (a poisonous substance) thats transmitted to humans ... Do wasps remember you?. Which is more dangerous wasps or hornets?. Though both wasps and hornets are generally known to be more ... Can a common wasp kill you?. Unlike bees, wasps do not die after one sting. They can, and will, sting you quite a few times, ...
Engineered Wasp Venom Could Help Fight Antibiotic Resistance ... wasp venom.. Wasps may not be known for being our best friends ... The researchers believe by repurposing the wasp venom, a potent antimicrobial drug could be produced that is as effective as ... We think that venom-derived molecules such as the ones we engineered in this study are going to be a valuable source of new ... Venom is an untapped resource that more scientists are now looking towards for drug usage, and with so many recent advances, it ...
This panel tests for bumblebee, honeybee, paper wasp, white face hornet, yellow hornet and yellow jacket venom allergies by ... Wasp and Hornet Venom (Hymenoptera) Blood Test: ... Allergen Profile Bee Wasp and Hornet Venom Hymenoptera Blood ...
The loss of a single wasp might not seem very important, but spider wasps have venom that could be useful for treating ... A new wasp species, with Alzheimers-fighting venom, may be lost to science due to bushfires. August 7, 2020. August 10, 2020. ... "The wasps habitat has been destroyed by fire, so we dont know if any of the wasps survived" said Dr Rodriguez. "Its sad to ... The Namadgi spider wasp, now named Epipompilus namadgi, is one of three new wasp species recently described in Zootaxa. ...
His research fond that the specific wasp that has the correct venom for this task is the Polybia paulista. The toxin produced ... This article (Brazilian Wasp Venom Found To Kill Cancer Cells Without Harming Healthy Cells) is free and open source. You have ... Brazilian Wasp Venom Found To Kill Cancer Cells Without Harming Healthy Cells. ... According to recent studies conducted by Professor Mario Palma at Sao Paulo State University Brazilian wasp venom has the ...
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Wasp venom allergy treatment - Special Authority SA1367 -- Retail pharmacy* Treatment kit (Paper wasp venom) - 1 vial 550 mcg ... Treatment kit (Paper wasp venom) - 1 vial 550 mcg freeze dried venom, with diluent * Brand Fully subsidised brand. Hymenoptera ... Treatment kit (Paper wasp venom) - 6 vials 120 mcg freeze dried venom, with diluent * Brand Fully subsidised brand. Venomil ... "Wasp venom allergy treatment","data":{"category":"Medicine","linkRef":"Wasp venom allergy treatment"}},{"value":"Water","data ...
... Laura Mae. July 27, 2022, 4:58 pm. July 27, 2022. 0. 203. ... But White Hats dont believe the wasp venom is part of a eugenics program to eradicate our children. Rather, they assert the ... The shot is painful enough, but with the wasp venom added, its 100 times worse," said Captain John Forsythe at Medical ... Four of the 75 vials contained 19mg of venom per 1,000-unit vial. A typical tarantula hawk sting delivers ~100mcg of venom. In ...
Types of Wasps. Florida is home to several wasp species, including Paper Wasps, Yellow Jackets, Cicada Killers and Mud Daubers. ... The Dangers of Wasps, Hornets and Bees. Common in or close to nearly every household, wasps, hornets, and yellow jackets can ... Paper Wasps. Paper wasps are common insects in Florida and can be easily identified with their yellow bodies with brown ... It is not safe to have your children live in a wasp-infested home, but we do not advise resolving the wasp issue by yourself. ...
The venom of insects such as wasps and bees is full of compounds that can kill bacteria. Unfortunately, many of these compounds ... Wasp Venom As An Antibiotic Drug. December 9, 2018. by The Science Thinkers ... The peptide that de la Fuente-Nunez and his colleagues focused on in this study was isolated from a wasp known as Polybia ... After performing a systematic study of the antimicrobial properties of a toxin normally found in a South American wasp, ...
RESULTS: Wasp venom-allergic individuals have detectable whole wasp venom-specific T cells directly ex vivo, which show rapid ... OBJECTIVE: We sought comprehensively to characterize the T cell proteome for wasp venom to facilitate the future development of ... METHODS: Using peripheral blood mononuclear cells from wasp venom-allergic individuals and IL-4 ELISPOT analysis, we ... Although it is likely that there are many T cell antigens within wasp venom, the main responses are to proteins coincident with ...
Wasp venom uniquely contains kinin. One of the kinins found in wasp venom, "polistes kinin 3", is found to lead to similar ... including the neotropical red paper wasp, the red-headed paper wasp, and Klugs velvet ant (a wingless wasp and not a true ant ... The composition of tarantula hawk venom is unknown. Schmidt also later rated the sting of a species of warrior wasp as a 4, ... Habermann, E. (28 July 1972). "Bee and Wasp Venoms". Science. 177 (4046): 314-322. Bibcode:1972Sci...177..314H. doi:10.1126/ ...
Previous studies have shown that venoms of social wasps and bees exhibit strong anticoagulant activity. The present study ... In conclusion, fibrinogenolytic and anticoagulant properties of this wasp venom find a potential application in drug ... Anticoagulant and fibrinogenolytic properties of the venom of Polybia occidentalis social wasp. Blood Coagulation & ... Anticoagulant and fibrinogenolytic properties of the venom of Polybia occidentalis social wasp. ...
Recently, the entire genome of this ectoparasitoid wasp was sequenced, enabling the identification of 79 venom proteins. The ... The value of deciphering this venom is also discussed. ... wasps and honeybees. In honeybee venom, it is called a "venom ... In the venom from the endoparasitic wasp P. hypochondriaca, ACE-like enzyme activity was detected [66]. This venom protein was ... Not only does this wasp have an elaborate venom system, it produces venom that is always injected prior to oviposition and ...
An assessment of the reliability and validity of the kinesiological muscle test in patients allergic to wasp venom. ...
Proteo-trancriptomic analyses reveal a large expansion of metalloprotease-like proteins in atypical venom vesicles of the wasp ... we performed a transcriptome analysis of the venom gland and a proteomic analysis of the venom and purified MpVLPs. About half ... that are synthesized in the venom gland and injected into the parasitoid host along with the venom during oviposition. In order ... The role of DUF4803 proteins, also present in the venom of other braconids, remains to be clarified. ...
Brazilian Wasp Venom Kills Cancer Cells - CER. Students complete an CER on how Brazilian wasp venom can disrupt the cell ...
Wasps are members of the order Hymenoptera, suborder Apocrita. Members of this order, which includes bees, yellow jackets, ... the muscles around the wasps venom sac begin to inject the venom. Wasp venom contains up to 13 different antigens. The wasp ... Wasps can be further divided into social wasps and solitary wasps. Social wasps include the aggressive wasps found in northern ... 2] This is more related to the existing level of circulating IgE than to the number of wasp stings or the amount of venom ...
This article describes the effects of a wasp sting. ... This article describes the effects of a wasp sting. ... Wasps carry this venom. Some people are allergic to the venom and have a serious reaction if they are stung. Most people do not ... Wasp venom is toxic. It is injected into you when you are stung. ... are from an allergic reaction to the venom, not from the venom ... If you do this, do not pinch the venom sac at the end of the stinger. If this sac is broken, more venom will be released. ...
Categories: Wasp Venoms Image Types: Photo, Illustrations, Video, Color, Black&White, PublicDomain, CopyrightRestricted 54 ...
MCP: Wasp venom causes slow burn in roach brain John Arnst. MCP: A royal legacy Laurel Oldach ... MCP: Just drops of viper venom pack a deadly punch Laurel Oldach ...
The venom of a parasitic wasp turns cockroaches into slaves by specifically reducing their desire to walk. ... Now, Ram Gal and Frederic Libersat from Ben-Gurion University in Israel have discovered how the wasps venom keeps its victim ... The fact that stung cockroaches could still flip themselves back on their feet shows that the jewel wasps venom doesnt affect ... Regardless of the method, its clear that the wasps venom is a precision weapon. It doesnt just indiscriminately target the ...
Compound: protein (wasp venom peptide (mastoparan)). Species: Vespula lewisii [TaxId:7452]. Database cross-references and ...
Wasp bite induced ATN from direct venom toxicity is very rare. We report two such cases. The first case was a 14 years old boy ... highlighting the importance of early detection and treatment of renal failure from wasp venom. ... Acute Renal Failure Following Multiple Wasp Stings. November 2014 ยท Journal of the College of Physicians and Surgeons--Pakistan ... suggesting direct venom toxicity. Both the patients recovered completely after a period of few weeks, ...
Despite their size and potent venom, executioner wasps are not aggressive. They will attack as a colony if they feel threatened ... Theyre also referred to as "drumming wasps" for this reason.. #2 Executioner Wasps. Another member of the paper wasp family ... The hawk wasp is set on one thing: tarantulas.. Tackling tarantulas. A hawk wasp paralyzing its prey. Photo by National Park ... 1 Tarantula Hawk Wasps. The top spot and winner of the most painful sting on the planet goes to the tarantula hawk wasp. ...
This treatment is also considered mandatory for life-threatening bee and wasp sting (hymenoptera venom) reactions. [36] ...
Tag Archives: jewel wasp A Parasitic Wasp that Injects Its Venom Into a Cockroachs Brain in Order to Control It. July 11, 2011 ... Today I found out that the Jewel Wasp, also known as the "Emerald Cockroach Wasp", is a parasitic wasp that injects various ...
When the wasps sting the Indian meal moth larvae, they inject venom that causes paralysis. In previous research, we discovered ... The parasitoid wasp Habrobracon hebetor injects a paralytic venom into P. interpunctella larvae before laying eggs. A previous ... Technical Abstract: Entomopathogenic nematodes and parasitoid wasps are used as biological control agents for management of ... Entomopathogenic nematodes (also called beneficial nematodes) and parasitic wasps attack Indian meal moth larvae. The ...
Is having a food allergy different to having an allergy to bee and wasp venom, a prescription drug or even anaesthetics?. All ... He has found that most patients would agree that allergen drugs or insect venom can usually be avoided by the individual. In ...
Ya its very true Polybia-MP1 (MP1 extracted from the venom of Brazilian wasp Polybia paulista) have anticancer potential I have ... Brazilian Wasps venom kills cancer cells without harming normal cells, What do you think? ...

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