References/Publications for RAST of Api m 2

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1016291 Clin Allergy. 1976 Nov;6(6):587-95.

Allergenic potency of bee antigens measured by RAST inhibition.

Arbesman CE, Reisman RE, Wypych JI.

The potency of various bee antigens including bee venom, several whole bee body
extracts and fractions of bee venom was studied using the RAST inhibition method.
As compared to whole bee body extract, bee venom was a much more potent inhibitor
of both bee venom and whole body RAST, suggesting that venom has a greater
capacity to bind specific bee IgE antibodies. Whole body extracts also varied
substantially in their inhibiting activity. Phospholipase A and hyaluronidase
were the most potent of the bee venom fractions suggesting their potential use as
an assay for standardization of insect extracts.

PMID: 1016291 [Indexed for MEDLINE]
J Allergy Clin Immunol. 1976 Jan;57(1):29-40.

Allergy to insect stings. II. Phospholipase A: the major allergen in honeybee

Sobotka AK, Franklin RM, Adkinson NF Jr, Valentine M, Baer H, Lichtenstein LM.

In order to determine the proteins of major allergenic importance in honeybee
venom (Apis mellifera) it was chromatographed on G-50 Sephadex. The four major
protein peaks eluted were identified as hyaluronidase, phospholipase, melittin,
and apamin. Testing these preparations on the leukocytes of 6 honeybee-sensitive
patients, with the in vitro method of histamine release, revealed that all
individuals were most sensitive to phospholipase A. IgE antibodies against
phospholipase A (RAST) were found in the sera of honeybee-sensitive patients and
IgG antibodies to this venom component were found in the sera from beekeepers and
venom-treated patients. Melittin appeared to be allergenic in several patients,
but the results were variable and were possibly due to contamination with
phospholipase. All patients were insensitive to the hyaluronidase and apamin
preparations. We conclude that phospholipase A is the major allergen of honeybee
venom and, since this protein is readily available, it should be useful for
diagnostic and therapeutic studies as well as for the standardization of
materials used in the management of honeybee-sensitive patients.

PMID: 54382 [Indexed for MEDLINE]
Int Arch Allergy Appl Immunol. 1987;83(2):113-20.

Immune response to bee venom. II. Quantitation of the absolute amounts of IgE and
IgG antibodies by saturation analysis.

Kemeny DM, Lessof MH.

We have measured in allergic and non-allergic beekeepers IgE and IgG antibodies
to the bee venom allergens, phospholipase A2 (PLA2) and hyaluronidase (HYAL), by
the radioallergosorbent test (RAST) and a 125I-radiolabelled antigen-binding
assay. The absolute amount of IgG antibody in a reference serum was determined by
saturation analysis using 125I-radiolabelled PLA2 and HYAL. Using monoclonal
anti-IgE coated microtitre plates, the absolute amount of IgE antibody to the
same antigen was also determined by saturation analysis. Regardless of the IgE
response to the different allergens, IgG antibody concentrations to PLA2 were
invariably higher than those to HYAL. In addition, the ratio of IgG to IgE
antibody was higher for PLA2 (220:1) than for HYAL (10:1). Higher levels of IgG
antibody to both allergens (especially HYAL) were found in those who had had
prolonged exposure to bee stings. These data suggest that the level of IgG
antibody produced is related to the dose administered, while the amount of IgE
antibody may be regulated by other factors.

PMID: 3583409 [Indexed for MEDLINE]
Int Arch Allergy Appl Immunol. 1989;89(1):60-6.

Analysis of differing patterns of cross-reactivity of honeybee and yellow jacket
venom-specific IgE: use of purified venom fractions.

Wypych JI(1), Abeyounis CJ, Reisman RE.