Inhaled particles and respiratory disease.

This brief discussion of inhaled particles, their manner of deposition and clearance, and their association with many human disease has been designed to remind us of the importance of particulate agents as sensitizers, via their allergen content, as causative agents of lung inflammation via their immunotoxic properties, as inducers of inflammatory alveolitis based on their content of antigens and adjuvant-like material, and as infectious agents. All these properties can play a part in a wide variety of allergic parenchymal, infectious, and industrial lung diseases and in building-related illnesses.

Crawfish and lobster allergens: identification and structural similarities with other crustacea.

Antigenic and allergenic components in crawfish and lobster extracts were studied using crossed immunoelectrophoretic techniques. Crossed immunoelectrophoresis with rabbit antisera revealed 23 antigens in crawfish and 17 antigens in lobster extracts. Both extracts exhibited structural similarities in antigens mutually and with other crustacea in cross-line immunoelectrophoresis. Crossed radioimmunoelectrophoresis (CRIE) demonstrated 6 crawfish and 4 lobster allergens when individual or pooled sera from radioallergosorbent test (RAST)-positive crustacea-sensitive subjects were used. Since radiostaining was also observed with sera from RAST-negative nonsensitive subjects, specificity of IgE binding was tested using CRIE-inhibition. Preincubation of RAST-positive sera with crawfish or lobster extract decreased radiostaining in CRIE, while no changes occurred when using control sera. These results confirmed the presence of IgE-mediated mechanisms in seafood allergy and demonstrated a number of shared antigenic determinants among crustacea allergens.

Tobacco smoke "sensitivity"--is there an immunologic basis?

This study was undertaken to determine if there is an immunologic basis for reported tobacco-smoke hypersensitivity in man. Ninety-three individuals who were recruited on the basis of their smoking history and/or claimed sensitivity to tobacco smoke were skin prick tested with tobacco smoke and leaf extracts and their sera analyzed for reaginic and precipitating antibodies to these antigens. Results demonstrated that a significant number of the individuals who were tested had positive skin test and RAST responses to tobacco leaf antigens, whereas only a small number responded to smoke antigens. RAST or skin test responses of study subjects to leaf or smoke antigens did not correlate with symptoms of tobacco-smoke "sensitivity" or smoking history but did correlate with atopic status. Precipitins were detected only to tobacco leaf C in 46 of the 93 individuals who were tested but did not correlate with smoking history or smoke "sensitivity." These results suggest that subjective tobacco-smoke sensitivity is not caused by hypersensitivity to tobacco leaf or smoke antigens.

Analysis of green coffee bean and castor bean allergens using RAST inhibition.

Coffee workers with occupational allergic symptoms and positive skin tests to green coffee bean and factor dust antigens have elevated serum IgE antibodies (by radioallergosorbent test--RAST) to green coffee and castor bean allergens. These antibodies were used in a RAST inhibition assay to analyse coffee and castor allergens. Bean allergens were extracted by homogenization in PBS, centrifugation and concentration of supernates by ultrafiltration. Green coffee bean allergens, fractionated by gel filtration and Pevikon block electrophoresis, were shown to be very heterogeneous with a molecular weight range of 50 000 to 500 000 daltons. Castor allergens were more homogeneous with a molecular weight of 14 000 daltons and were partially purified by Pevikon block electrophoresis, gel filtration and isoelectrofocusing. Chemical analysis showed that protein was the major component in both allergen extracts. However, proteolytic enzymes could only partially destroy allergenic activity. Such isolation and characterization of these allergens should result in better methods of diagnosis and treatment of coffee workers with occupational allergic disease.

Castor bean allergens: evidence for distinct heat-labile and stable entities.

Castor beans contain one of the most potent allergens known to man. Previous studies suggested that these allergens are heat-stable; but our current data suggest that both heat-stable and labile allergens are present in castor bean extracts. The heat-labile allergen is of large molecular weight and is immunochemically distinct from the smaller molecular weight heat-stable allergen. Both allergens have different isoelectric points. These antigens may be clinically relevant since coffee workers sensitized to castor have IgE antibodies to both allergens.

Detection of castor allergens in castor wax.

The presence of castor bean allergens in castor wax products was determined by in vivo and in vitro analysis of castor wax extracts. Allergens were detected in one extract of castor wax by the PCA reaction in mice, the RAST inhibition reaction, and skin prick test in castor bean sensitive individuals. However, these allergens in the wax were of much lower potency than those in the bean, and were not detectable in a deodorant product utilizing castor wax.

Extraction and analysis of coffee bean allergens.

Workers in the coffee industry can develop occupational allergic disease upon exposure to dust associated with coffee manufacturing. Since controversy exists as to the source or chemical nature of these allergens, the mouse model of reaginic antibody production was used to assess the potential sources of allergens in samples obtained from a local coffee manufacturing plant. Mice were immunized with extracts of coffee dust and beans and the resulting reaginic antibody response determined by the passive cutaneous anaphylaxis reaction. Cross-reacting allergens were detected in samples of coffee dust, cleaner can debris and green coffee beans, but not in chaff or roasted coffee beans. None of the allergens detected in coffee samples cross-reacted with extract of castor beans, although these extracts contained the potent castor bean allergen. Green coffee bean allergens partially purified by gel filtration were heterogeneous with respect to molecular size, although quite similar in their reactivity with reaginic antiserum. These results suggest that the green coffee bean is the major source of allergen in coffee manufacturing plants. This allergen is heterogeneous with respect to size and heat lability, and is immunochemically different from the castor bean allergen.