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The concentrations of proteins, allergens and rubber chemicals are essential parameters of the allergenicity of NRL gloves. To date, a standardized method has been given only for analysis of the protein concentration (DIN EN 455-3), and not for the concentrations of allergens and rubber chemicals. In the present study, we investigated 11 brands of surgical gloves currently available on the German market. Additionally 1 glove, not subjected to final leaching procedures, was added for comparison purposes. Protein concentrations were analysed by different methods in different laboratories. Allergen concentrations were assayed by prick tests in NRL-allergic volunteers and by RAST inhibition methods. Rubber chemicals were analysed by HPTLC and GC. The protein concentrations analysed by the Lowry method in the 2 laboratories gave concordant results, but the correlations between protein and allergen concentrations were low. The protein concentration analysed by HPLC correlated with the allergen concentration, and gave better information on the allergenicity of the gloves. The development of standardized methods for allergen analysis in the assessment routine is necessary, due to significant discrepancy between protein and allergen levels of some gloves. Thiurams were not found in any of the gloves, though carbamates were present in all gloves tested. Our data indicate that washing procedures have little or no effect on the concentration of rubber chemicals. [ABSTRACT FROM AUTHOR]

Background: IgE-mediated hypersensitivity to latex has been recognized as an increasing health problem with far-reaching consequences for patients, regarding both their occupational situation and safety in medical care. Therefore, a correct diagnosis of natural rubber latex (NRL) allergy is essential. The purpose of the study was to evaluate sensitivity and specificity of several established diagnostic methods for NRL allergy (in vitro assays and skin prick test) in relation to a new semiquantitative dipstick test (Allergodip[sup ®] -Latex, Allergopharma) as a screening test for NRL allergy. Methods: Data obtained with quantitative assays including Pharmacia CAP System[sup ®] (FEIA), DPC-AlaSTAT[sup ®] and Magic Lite[sup ®] were compared with the dipstick test results in latex-sensitized (n = 151) and nonsensitized persons (n = 232). In addition these in vitro findings were related to clinical symptoms after exposure to latex and skin prick test results with a panel of different latex allergen extracts. Results: When comparing sensitivity and specificity of all in vitro assays relative to skin prick test results the Pharmacia CAP System[sup ®] (FEIA) had the highest sensitivity in the range of 90%. Sensitivity of the other in vitro assays was in the range of 73.7–74.9%, specificity varied from 85.3 to 89.8%. A diagnostic standard was defined in terms of at least three corresponding test results out of all diagnostic methods (in vitro assays and skin prick test). The sensitivity and specificity of each diagnostic test were determined relative to this diagnostic standard. Hereby the Allergodip test results showed a sensitivity of 91% and a specificity of 93%. Conclusion: The dipstick test results are in line with the data of the other in vitro assays. In contrast to other in vitro assays the dipstick test requires no further laboratory equipment and is easy to perform.Copyright © 2001 S. Karger AG, Basel [ABSTRACT FROM AUTHOR]

Background: Plant profilins are important pan-allergens. They are responsible for a significant percentage of pollen-related allergies. Limited information is available about their involvement in the latex-fruit syndrome and the cross-reactivities between latex and pollen. We aimed to clone and express the Hevea brasiliensis latex profilin to investigate its allergological significance and serological cross-reactivities to profilins from plant foods and pollens. Methods: A DNA complementary to messenger RNA (cDNA) coding for the Hevea latex profilin, Hev b 8, was amplified by polymerase chain reaction from latex RNA. Recombinant (r)Hev b 8 was produced in Escherichia coli and used to screen sera from 50 latex- allergic health care workers (HCWs) with well-documented histories of food and pollen allergy and 34 latex-allergic spina bifida (SB) patients. The cross-reactivity of natural Hev b 8 and rHev b 8 with other plant profilins was determined by ELISA inhibition assays. A three-dimensional homology model of Hev b 8 was constructed based on known profilin structures. Results: The cDNA of Hev b 8 encoded a protein of 131 amino acids with a predicted molecular mass of 14 kD. Twelve of the 50 HCWs and 2 of the 34 SB patients were sensitized to Hev b 8. All Hev b 8-sensitized patients showed allergic symptoms to pollen or plant foods. Cross-reactivities between profilins of latex, pollen and plant food were illustrated by their ability to inhibit IgE binding to rHev b 8. Homology modeling of Hev b 8 yielded a structure highly similar to Bet v 2, the birch pollen profilin, with the most distinct differences located at the N-terminus. Conclusions: We conclude that primary sensitization to latex profilin in the majority of cases takes place via pollen or food profilins. Additionally, pollinosis and food-allergic patients with profilin-specific IgE can be at risk of developing latex allergy.Copyright © 2001 S. Karger AG, Basel [ABSTRACT FROM AUTHOR]

Provides information on rubber latex allergy. Types of allergy caused by clinical reactions to contact with latex gloves; Identification of allergens derived from H brasiliensis in natural rubber latex; Guidelines to prevent the occurrence of allergy.

Natural rubber latex allergy is an IgE-mediated disease that is caused by proteins that elute from commercial latex products. A complementary DNA (cDNA) coding for Hev b 9, an enolase (2-phospho- d-glycerate hydrolyase) and allergen from latex of the rubber tree Hevea brasiliensis , was amplified by PCR. The PCR primers were designed according to conserved regions of enolases from plants. The obtained cDNA amplification product consisted of 1651 bp and encoded a protein of 445 amino-acid residues with a calculated molecular mass of 47.6 kDa. Sequence comparisons revealed high similarities of the Hevea latex enolase to mold enolases that have been identified as important allergens. In addition, the crucial amino-acid residues that participate in the formation of the catalytic site and the Mg2+ binding site of enolases were also conserved. Hevea latex enolase was produced as a recombinant protein in Escherichia coli with an N-terminal hexahistidyl tag, and purified by affinity chromatography. The yield amounted to 110 mg of purified Hev b 9 per litre of bacterial culture. The recombinant allergen bound IgE from latex, as well as mold-allergic patients, in immunoblot and ELISA experiments. The natural enolase was isolated from Hevea latex by (NH4 )2 SO4 precipitation and ion exchange chromatography. The natural and the recombinant (r)Hev b 9 showed equivalent enzymatic activity. Patients’ IgE-antibodies preincubated with rHev b 9 lost their ability to bind to natural (n) Hev b 9, indicating the identity of the B-cell epitopes on both molecules. Cross-reactivity with two enolases from Cladosporium herbarum and Alternaria alternata was determined by inhibition of IgE-binding to these enolases by rHev b 9. Therefore, enolases may represent another class of highly conserved enzymes with allergenic potentials. [ABSTRACT FROM AUTHOR]