Fish play important roles in human nutrition and health, but it triggers severe allergic reactions in some population. Parvalbumin (PV) represents the major allergen of fish. While IgE cross-reactivity to PV in various bony fish species has been well characterized, little information is available about allergens in cartilaginous fish. In this study, two shark PV isoforms (named as SPV-I and SPV-II) from Mustelus griseus were purified by combination of chromatography methods to single bands. Their identies were further confirmed by mass spectroscopic and N-terminal Edman sequencing analysis. IgE immunoblot analysis showed that sera from fish-allergic patients reacted to both SPV-I and SPV-II, but more sera recognize SPV-I than SPV-II. Thermo denaturation monitored by CD spectrum showed that both of the SPV allergens are highly stable. SPV-I maintained the allergenicity after heat denaturation, while the IgE-binding ability of SPV-II reduced significantly. The results of crystal structure showed that SPV-I and SPV-II were similar in their overall tertiary structure, but their amino acid sequences share lower similarities, indicating that the differences of SPV-I and SPV-II allergenicities may be due to differential antigen epitopes in these two isoforms. This is the first report on the characterization and comparison of PVs of two lineages from the same fish species.

Purification and characterization of parvalbumins, the major allergens in Mustelus griseus

256th National Meeting (2018)

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