Introduction
Natural Rubber Latex
Allergen | Hevea brasiliensis protein | Clinical relevance |
---|---|---|
Hev b 1 | Rubber elongation factor | Major allergen in SB |
Hev b 2 | β-1,3-Glucanase | Uncertain
†
|
Hev b 3 | Small rubber particle proteins | Major allergen in SB |
Hev b 4 | Lecithinase homolog | Minor allergen
†
|
Hev b 5 | Acidic structural protein | Major allergen in HCW and important in SB |
Hev b 6.01/6.02 | Prohevein/hevein | Major allergen in HCW |
Hev b 7 | Patatin-like protein (esterase) from latex-B- and C-serum | Minor allergen |
Hev b 8 | Profilin (actin-binding protein) | Minor allergen |
Hev b 9 | Enolase | Minor allergen |
Hev b 10 | Manganese superoxide dismutase (MnSOD) | Minor allergen |
Hev b 11 | Class I chitinase | Minor allergen |
Hev b 12 | Non-specific lipid transfer protein type 1 (nsLTP1) | Minor allergen |
Hev b 13 | Esterase | Uncertain
†
|
Hev b 14 | Hevamine | Minor allergen
†
|
Hev b 15 | Serine protease inhibitor | Minor allergen |
Cereals
Coffee Bean
Soybean
Furred Mammals and Derived Products
Animal source | Major allergens | Protein family | Main source | Exposed workers (reference) |
---|---|---|---|---|
Cow (Bos domesticus) | Bos d 2 | Lipocalin | Dander | Dairy farmers |
nBos d 4* | α-Lactalbumin | Milk | Candy and pastry workers | |
nBos d 6* | Albumin | Serum | Lab workers | |
nBos d 8* | Casein | Milk | Leather tanning [59] Dermatological powder use | |
Mouse (Mus musculus) | Mus m 1** | Lipocalin | Urine | Laboratory animal workers [61] |
Rat (Rattus norvegicus) | Rat n 1 | Lipocalin | Urine | Laboratory animal workers [18••] |
Guinea pig (Cavia porcellus) | Cav p 1 | Lipocalin | Dander, saliva | Laboratory animal workers [18••] |
Cav p 2 | Lipocalin | Saliva, dander |
Seafood
Biological Enzymes
Name | Source/production organism | Biological function | Industrial application | Exposed workers | References |
---|---|---|---|---|---|
Subtilisin (e.g., Alcalase®, Maxatase®, Savinase®) | Bacillus subtilis or Bacillus licheniformis | Serine protease | Detergent production, food processing | Workers in enzyme production and detergent-manufacturing | |
α-Amylase (Asp o 21) |
Aspergillus oryzae
| Catalyzes the hydrolysis of starch into sugars | Food production, baking additive | Baker (mainly) | [72] |
β-Xylosidase (Asp n 14) |
Aspergillus niger
| Hydrolysis of (1- > 4)-beta-d-xylans, to remove successive d-xylose residues from the non-reducing termini | Food production, baking additive | Baker (mainly) | [73] |
Glucoamylase or amyloglucosidase |
Aspergillus niger
| Starch-breaking enzyme; hydrolyzes terminal 1,4-linked alpha-d-glucose residues successively from non-reducing ends of amylose chains to release free glucose | Food production, baking additive | Baker (mainly) | [74] |
Phytase* |
Aspergillus niger
| Phosphatases, breaking down the non-digestible phytic acid | Animal feed supplement | Workers in phytase production | [75] |
Papain (n Car p 1) | Papaya fruit (Carica papaya) | Thiol protease | Pharmaceutical, cosmetic, and immunochemical industry | Workers in production and application of papain | [76] |
Pepsin | Swine extract (Sus)** | Acidic gastric protease; main digestive enzymes | Pepsin powder commonly used in the preparation of F(ab′)2 fragments from antibodies | Laboratory worker, cheese worker | |
Bromelain (nAna c 2) | Pineapple (Ananas comosus) | Cysteine-endoprotease | Food processing, detergent, and pharmaceutical industry | Workers in food processing industry, laboratory worker |
Molds
Conclusions
-
Assessment of sIgE reactivity to allergen components has been poorly investigated in the specific field of occupational allergies, with the notable exception of NRL and cereal flour.
-
Spiking allergen extracts with recombinant allergens may increase the sensitivity of sIgE assessment against natural extracts (e.g., Hev b 5-amplified latex extract (k82)).
-
Assessment of sIgE against occupational allergen components may help to discriminate between different routes of exposure (inhalation vs mucosal exposure), e.g., spina bifida vs health care workers, bakers’ OA from food-induced and exercise-induce allergy
-
The determination of sIgE against currently available occupational allergen components failed to increase the diagnostic sensitivity as compared to sIgE antibodies against natural extracts (e.g., NRL induced OA with negative k82), but further identification of allergens could help to establish IgE-mediated sensitization to some allergens encountered at the workplace.
-
The determination of sIgE against currently available occupational allergen components from NRL allows for improving the specificity and the positive predictive value for OA.
-
For workplace-related allergens like seafood, coffee, soybean, and molds, some characterized allergens are available, but their relevance for occupational sensitization routes should be verified in the future.