Identification, cloning, and sequence of a major allergen (Hev b 5) from natural rubber latex (Hevea brasiliensis).

Proteins in commercial latex products, derived from the rubber tree Hevea brasiliensis, cause anaphylaxis in susceptible individuals, especially health care workers and children with spina bifida. To identify latex allergens, we utilized IgE from the serum of a latex-allergic health care worker to screen a cDNA library from Hevea latex. The identified cDNA clone, cDNA Hev b 5, encodes an open reading frame of 163 peptide residues.

Immunodetection of latex antigens.

Background: Protein antigens in latex products can cause type I reactions. In the past antigens have been measured by protein assays, high-performance liquid chromatography, RAST inhibition, and skin tests. We examined the use of a mouse monoclonal antibody (CRI-C) to latex in the detection of latex antigens.

Characterization of the interaction of the glp repressor of Escherichia coli K-12 with single and tandem glp operator variants.

The glp operons of Escherichia coli are negatively controlled by the glp repressor. Comparison of the repressor-binding affinities for consensus and altered consensus operators in vivo showed that all base substitutions at positions 3, 4, 5, and 8 from the center of the palindromic operator caused a striking decrease in repressor binding. Substitutions at other positions had a severe to no effect on repressor binding, depending on the base substitution.

Affinity purification of latex antigens.

Latex extracts are complex mixtures of antigenic peptides. We attempted to raise monoclonal antibodies to latex and to use these antibodies to purify latex antigens. A monoclonal antibody, CRI-C, was raised by standard techniques.