Occupational Allergy and Asthma Among Fish Processing Workers in South Africa

Jeebhay, Mohamed F.; Robins, Thomas G.; Jl, Malo; Lin, Xia; Seixas, Noah; Lehrer, Samuel B.; Bateman, E.D.; Baatjies, Roslynn; Miller, Mike; George, D; Russford, E; Smuts, Marius; Lopata, Andreas L.

doi:10.1097/00001648-200509000-00220

Cited by 8 publications

(9 citation statements)

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“…processing, harvesting, etc. ), and these workers are being continuously exposed to seafood allergens 4–6…”

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confidence: 99%

“…Tropomyosin (TM) is a water‐soluble and heat‐stable protein with a molecular weight (MW) ranging between 34 and 39 kDa 14. It has a highly conserved amino acid sequence among different invertebrate organisms and is present in muscle as well as non‐muscle cells 15, 16. Furthermore, differential splicing of the pre‐messenger ribonucleic acid (pre‐mRNA) produce isoforms of TM 17…”

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confidence: 99%

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Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry

Rahman

Kamath

Lopata

et al. 2010

Rapid Commun. Mass Spectrom.

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Crustaceans are the third most prevalent cause of food-induced anaphylaxis after peanuts and tree nuts. The severity of the allergenic proteins depends mainly on the amino acid sequence that induces production of IgE antibodies. In black tiger prawn (Penaeus monodon), the crude protein extract was profiled and its allergenic potency was examined against patient's sera. Proteins having strong immunoreactivity with patient's IgE were characterized using peptide mass fingerprinting (PMF). Tropomyosin (TM) (33 kDa), myosin light chain (20 kDa), and arginine kinase (40 kDa) were identified as allergenic proteins. Tropomyosin, the most abundant and potent allergen, was purified using ion-exchange chromatography for de novo sequencing experiments. Using bottom up tandem mass spectrometry, the full amino acid sequence was achieved by a combination of matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) tandem mass spectrometry (QqToF). Myosin light chain and arginine kinase were also characterized, and their related peptides were de novo sequenced using the same approach. The immunological reactivity of the crude prawn extracts and purified TM samples were analyzed using a large number of patients' sera. A signature peptide was assigned for the TM protein for future quantification work of black tiger prawn TM levels in different matrices (i.e. water, air, food) in the seafood industry.

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“…processing, harvesting, etc. ), and these workers are being continuously exposed to seafood allergens 4–6…”

mentioning

confidence: 99%

mentioning

confidence: 99%

Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry

Rahman

Kamath

Lopata

et al. 2010

Rapid Commun. Mass Spectrom.

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“…Workers involved in crab, prawn, shrimp, and fish processing are commonly exposed to airborne allergens that increase the risk of developing occupational asthma [1]. In general, occupational exposure to seafood causes a variety of health problems; one problem reported is a significant prevalence of occupational asthma [2][3][4].…”

Section: Introductionmentioning

confidence: 99%

Simultaneous determination of two major snow crab aeroallergens in processing plants by use of isotopic dilution tandem mass spectrometry

2012

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Snow crab is a major fishery in the North Atlantic region. During crab processing the proteins are aerosolized and some are responsible for development of occupational asthma. Tropomyosin and arginine kinase have recently been reported as major snow crab allergens. A liquid chromatographic tandem mass spectrometric method has been developed for simultaneous analysis of these two proteins in air samples collected from processing plants. These proteins were initially isolated then characterized by use of mass spectrometry to determine their primary structure and signature peptides. The signature peptides were chemically synthesized in light and heavy forms and used as standards for developing the multiple-reaction monitoring transitions to monitor allergen levels. A validation study was performed; precision and accuracy were 1.8-8% and 91-104%, respectively. Replicate air samples were collected on air filters from two crab-processing plants in Newfoundland and Labrador (NL) and four located in Quebec. In NL, measured levels of both tropomyosin and arginine kinase were between 1 and 20 ng m(-3). In Quebec plants, however, levels were found to be much higher at 2-2400 ng m(-3). Significant differences were also observed among the plants and individual processing workstations. For the first time arginine kinase has been detected in its aerosolized form in processing plants. In general, levels of the allergens were highest in the butchering and cooking areas; plant design can, however, have a significant effect on levels of the allergens.

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“…Identification of shrimp allergen-specific IgE antibodies has been demonstrated by prick skin test and the radio-allergosorbent test (RAST) [16][17]. Exposure to allergens in the fishing and seafood processing industry also results to production of allergen-specific IgEs [19]. Significantly high cross-reactivity between shrimp and crab allergens has been shown in a competitive IgE inhibition assay [18].…”

Section: Arthropod Allergiesmentioning

confidence: 99%

Recombinant Proteins and Peptides as Diagnostic and Therapeutic Reagents for Arthropod Allergies

Ramos¹,

Valmonte²,

Guia

2007

PPL

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Domestic arthropods are chief sources of potent allergens that trigger sensitization and stimulate IgE-mediated allergies. Diagnosis and immunotherapy of arthropod allergies rely on the use of natural allergen extracts which are associated with low specificity and efficacy, the risk of anaphylactic reactions, and the extended period of treatment. Most of the problems associated with natural allergen extracts for allergy diagnosis and immunotherapy can be circumvented with the use of recombinant allergens and peptides. Recombinant allergens are recently developed for microarray-based multi-allergen tests which provide component-resolved diagnosis (CRD) of the patient's sensitization profile. Moreover, recombinant protein technology and peptide chemistry have been used to construct isoallergens, allergen mutants, allergoids, T and B cell peptides, hypoallergens, and mimotopes with reduced allergenicity but enhanced immunogenicity for allergen-specific immunotherapy (SIT) and vaccination. The basics of recombinant arthropod allergen technology are in place providing a lucid future for the advancement of diagnosis and immunotherapy of arthropod allergies.

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Occupational Allergy and Asthma Among Fish Processing Workers in South Africa

Cited by 8 publications

References 0 publications

Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry

Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry

Simultaneous determination of two major snow crab aeroallergens in processing plants by use of isotopic dilution tandem mass spectrometry

Recombinant Proteins and Peptides as Diagnostic and Therapeutic Reagents for Arthropod Allergies

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