Radioallergosorbent test (RAST) for the measurement of IgE antibodies has been introduced more than 15 years ago and a number of technical modifications have since improved its sensitivity and reproducibility. The test has been applied to the diagnosis of allergy and to determine changes in the levels of IgE antibodies following immunotherapy. However, specific IgG antibodies are raised during such a therapy and can interfere with the RAST. We have developed a reverse enzymoallergosorbent test (REAST) where microtiter plates are first coated with a purified polyclonal anti-IgE antibody, then with the serum to test and finally with peroxidase-labeled antigen. This assay is antigen specific as shown by the significant inhibition of binding of the labeled antigen in presence of unlabeled specific antigen (greater than 95%) and the absence of inhibition in presence of irrelevant antigens. The values found in atopic patients (85 subjects) were significantly higher than in the non-atopic donors (35 subjects) (1.14 U +/- 1.20 vs. 0.01 U +/- 0.02, P less than 0.0005) and there was a good correlation with the Pharmacia RAST (P less than 0.0005). The levels of specific IgE by both REAST and RAST correlated well with the clinical symptomatology.

Download full-text PDF

Source
http://dx.doi.org/10.1016/0022-1759(86)90276-0DOI Listing

Publication Analysis

Top Keywords

ige antibodies
12
reverse enzymoallergosorbent
8
enzymoallergosorbent test
8
test reast
8
test
5
rast
5
development reverse
4
reast detect
4
detect timothy-specific
4
ige
4

Similar Publications

Background: XKH001 is a recombinant humanized IgG1 monoclonal antibody against IL-25 for the treatment of type 2 inflammatory diseases. This study aimed to evaluate the tolerability, pharmacokinetics, and pharmacodynamics of XKH001 in humans for the first time.

Research Design And Methods: This clinical investigation adopted a randomized, double-blind, and placebo-controlled single ascending dose (SAD) and multiple ascending dose (MAD) design.

View Article and Find Full Text PDF

Antigenic determinants underlying IgE-mediated anaphylaxis to peanut.

J Allergy Clin Immunol

January 2025

Department of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Vanderbilt University, Nashville, TN; Department of Pharmacology, Vanderbilt University Medical Center, Vanderbilt University, Nashville, TN.

Background: Studies of human IgE and its targeted epitopes on allergens have been very limited. We have an established method to immortalize IgE encoding B cells from allergic individuals.

Objective: To develop an unbiased and comprehensive panel of peanut-specific human IgE mAbs to characterize key immunodominant antigenic regions and epitopes on peanut allergens to map the molecular interactions responsible for inducing anaphylaxis.

View Article and Find Full Text PDF

Use of Immunoglobulin Replacement Therapy in Clinical Practice: A Review.

J Immunother Precis Oncol

February 2025

Department of Pediatrics, Division of Immunology, Allergy and Retrovirology, Baylor College of Medicine, Houston, TX, USA.

Immunoglobulins (Igs) are produced by B lymphocytes and play a key role in humoral immunity. Igs are classified into five isotypes (IgG, IgA, IgM, IgE, and IgD). Their primary function is to recognize and bind to foreign antigens.

View Article and Find Full Text PDF

Insights into structural and binding studies of pollen allergen Bet v 1 using computational approaches.

In Silico Pharmacol

January 2025

Bioinformatics Infrastructure Facility, Sri Venkateswara College (University of Delhi), Benito Juarez Road, Dhaula Kuan, New Delhi, 110021 India.

Unlabelled: Bet v 1, the European White Birch tree pollen allergen is responsible for a number of allergic responses in humans such as rhinitis, asthma and oral allergy syndrome. The allergen belongs to pathogenesis-related (PR) class 10 protein superfamily and exists in several naturally occurring isoforms. Limited structural information on Bet v 1 isoallergens and variants prompted us to carry out their in silico structural characterization.

View Article and Find Full Text PDF

Structural determinants of peanut induced anaphylaxis.

J Allergy Clin Immunol

January 2025

Department of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Vanderbilt University, Nashville, TN; Department of Pharmacology, Vanderbilt University Medical Center, Vanderbilt University, Nashville, TN. Electronic address:

Background: Human monoclonal IgE antibodies recognizing peanut allergens have recently become available, but we lack a detailed understanding of how these IgEs target allergens.

Objective: To determine the molecular details of the antibody-allergen interaction for a panel of clinically important human IgE monoclonal antibodies and to develop strategies to disrupt disease causing antibody-allergen interactions.

Methods: We identified candidates from a panel of epitope binned human IgE monoclonals that recognize two important and homologous peanut allergens, Ara h 2 and Ara h 6.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!