Venom antigen

Chavez-Olortegui C, Bohorquez K, Alvarenga LM, et al. (2001) Sandwich-ELISA detection of venom antigens in envenoming by Phoneutria nigriventer spider. Toxicon 39 909-911. 

A prospective enquiry was conducted in 1990 and 1991 in France by the Unite des Venins in order to collect epidemiological, clinical and biological data from hospitals. Vipera aspis venom antigens were quantified in urine and blood samples by a sandwich enzyme linked immunosorbant assay. 

The effect of antivenom administration on the kinetics of Vipera aspis envenomation was also examined. Radiolabelled Vipera aspis venom was injected intramuscularly to mimic the route of administration in case of accidental envenomations. The use of a radiolabelled venom allowed the quantification of plasma venom components free and bound to antivenom antibodies. Free venom proteins were detected by ELISA. The plasma concentration time profile of venom in antivenom-treated animals is shown in Figure 2. The plasma concentration curves measured by counting radioactivity or by ELISA superimposed before the administration of the antivenom. After intravenous injection of 125 mg of IPSER Europe serum, the total venom concentrations in plasma rapidly increased more than ten-fold and remained elevated during three days, whereas the plasma levels of free venom antigens measured by ELISA rapidly decreased and remained undetectable for the same period of time. Antivenom Fab 2 administration therefore results in the immunocomplexation of venom proteins in the vascular compartment and in the plasma redistribution of venom antigens from the extravascular compartment to the vascular compartment. 

Audebert, F., Grosselet, O., Sabouraud, A. and Bon, C. (1993) Quantitation of venom antigens from European vipers in human serum or urine by ELISA. J. Anal Toxicol 17, 236-240. 

Major allergens in all vespid venoms are phospholipase A, a 33.5-kDa enzyme which digests cell membranes (Ves vl for V vulgaris) and antigen 5 (Ves v5), a 23-kDa... 

A number of allergens from both honey bee and vespid venoms have been cloned and expressed by either Escherichia coli or baculovirus-infected insect cells (table 1) phospholipase Aj [20], hyaluronidase [21], acid phosphatase [13] and Api m6 [14] from honey bee venom, as well as antigen 5 [22], phospholipase A and hyaluronidase [23] from vespid venom, and dipeptidylpeptidases from both bee and Vespula venoms [15, 16]. Their reactivity with human-specific IgE antibodies to the respective allergens has been documented [11-16, 22, 23] and their specificity is superior... 

Premier, C., Mach, L., Glossl, J. and Marz, L. (1992) The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of al,3-fucosylation of the asparagine-bound IV-acetylglucosamine. Bio chemicalJournal 284, 377-380. 

There are two types of immunisation passive and active. Passive immunisation involves transfer of antibodies formed in response to an antigen in one individual to another. Such antibodies were first produced in animals but now most antibodies used for passive immunisation are of human origin, which minimises allergic reactions. This form of immunisation gives immediate protection but it does not last very long, since the antibodies are soon degraded in the body. It is used, for example, to protect against tetanus, rabies and the toxins in snake venom. 

The authors performed RAST inhibition to measure the relative potencies of the different venom extracts using the patient s serum as a source of IgE anti-venom. Although they initially suspected the new source of Polistes wasp venom, the relative potency tests showed greater variation in the honeybee venom. The IgG concentrations were consistent with this finding. This report emphasizes the care that must be taken with the preparation of each injection, especially when using a new batch of antigen. 

The classical pathway is activated primarily by the antibody antigen complexes. In 1913, Browning and Mackie showed that cobra venom could trigger serum-mediated lysis of erythrocytes in the absence of an antibody. Pillemer described properdin as a component of the antibody-independent complement pathway in 1954, and proposed the name properdin pathway. His work was not accepted until the 1960s, however, when the alternative pathway was... 

ANTIGENS These include vaccines, toxoids, allergens, venoms, etc. 

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