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Characterisation of allergens in pilchard, responsible for the development of occupational allergy in the seafood processing industry in the Western Cape
Author(s)
Hikuam, Christopher Willem
Date Issued
2006
Type
Thesis
Publisher
Cape Peninsula University of Technology
Abstract
The increase in popularity of fish, coupled with technological advances in the
fishing industry and changes in the control and management of fishing resources,
has led to a significant increase of fish processing workers from 13 million in
1970 to 38 million in 2002. Whereas allergic reactions to fish proteins were
previously only documented in consumers, increasing reports of occupational fish
allergies of fish processing workers has become evident. In South Africa, the
reported prevalence of occupational asthma associated with fish processing
workers is 2 - 8%, and the prevalence of occupational protein contact dermatitis
3 - 11%. Pilchard is one of the most consumed fish species in South Africa and
the immunological analysis of this species will therefore contribute to the
provision of occupational health services in the pilchard processing industry.
Proteins extracted from fresh, frozen and canned pilchard (Sardinops sagax), as
well as fresh samples of six other processed and consumed South African fish
were characterised by denaturing protein electrophoresis and immunoblotted with
different monoclonal and polyclonal antibodies. Sera from sensitised workers
were subsequently used to characterise the membrane-bound pilchard proteins
and analysed for human Immunoglobulin G (lgG) and Immunoglobulin E (IgE)
antibodies to determine antigen recognition.
A protein of 12 kDa molecular weight was found to be present in all fish protein
extracts, however, at various concentrations. With the aid of the monoclonal and polyclonal antibodies, the 12 kDa protein was postulated to be parvalbumin, a
known allergen in some fish species. Immunoblotting experiments for the
identification of workers' IgG- and IgE-reactivities to fresh, frozen and canned
pilchard showed a 12 kDa protein as an immunolgically reactive fish protein.
This protein was also found to occur in dimeric, trimeric and tetrameric forms,
which may have significant implications in the diagnosis and management of
occupational sensitisation to pilchard.
fishing industry and changes in the control and management of fishing resources,
has led to a significant increase of fish processing workers from 13 million in
1970 to 38 million in 2002. Whereas allergic reactions to fish proteins were
previously only documented in consumers, increasing reports of occupational fish
allergies of fish processing workers has become evident. In South Africa, the
reported prevalence of occupational asthma associated with fish processing
workers is 2 - 8%, and the prevalence of occupational protein contact dermatitis
3 - 11%. Pilchard is one of the most consumed fish species in South Africa and
the immunological analysis of this species will therefore contribute to the
provision of occupational health services in the pilchard processing industry.
Proteins extracted from fresh, frozen and canned pilchard (Sardinops sagax), as
well as fresh samples of six other processed and consumed South African fish
were characterised by denaturing protein electrophoresis and immunoblotted with
different monoclonal and polyclonal antibodies. Sera from sensitised workers
were subsequently used to characterise the membrane-bound pilchard proteins
and analysed for human Immunoglobulin G (lgG) and Immunoglobulin E (IgE)
antibodies to determine antigen recognition.
A protein of 12 kDa molecular weight was found to be present in all fish protein
extracts, however, at various concentrations. With the aid of the monoclonal and polyclonal antibodies, the 12 kDa protein was postulated to be parvalbumin, a
known allergen in some fish species. Immunoblotting experiments for the
identification of workers' IgG- and IgE-reactivities to fresh, frozen and canned
pilchard showed a 12 kDa protein as an immunolgically reactive fish protein.
This protein was also found to occur in dimeric, trimeric and tetrameric forms,
which may have significant implications in the diagnosis and management of
occupational sensitisation to pilchard.
Additional information
Thesis (MTech (Tourism and Hospitality Management))--Cape Peninsula University of Technology, 2006.
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Thesis
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