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In vitro stability and immunoreactivity of the native and recombinant plant food 2S albumins Ber e 1 and SFA-8 (2003)

Murtagh, G. J. ; Archer, D. B. ; Dumoulin, M. ; [et al.]

Oxford, UK : Blackwell Science Ltd

Clinical & experimental allergy 33 (2003), S. 0

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ISSN: 1365-2222

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Background The ability of an intact protein to reach the circulatory system may be a prerequisite to allergenicity and many allergens, particularly those from plant foods, have been found to be consistently more resistant to digestion by pepsin than other proteins.Objective This study assessed the pepsinolytic stability of native 2S albumins from Brazil nut and sunflower seed and their recombinant versions produced in Pichia pastoris. The physicochemical stability of native and recombinant Brazil nut 2S albumins and recombinant sunflower seed 2S albumin was also assessed. The immunoreactivity of native Brazil nut 2S albumin and recombinant 2S albumins was compared using serum from patients allergic to Brazil nuts and animals immunized with native 2S albumins.Methods Digestibility was measured in simulated gastric fluid followed by SDS-PAGE. Circular dichroism spectra were used to analyse unfolding, as proteins were denatured by temperature, pH and guanidinium chloride. Immunoreactivity was assessed by immunoblot, RAST and ELISA.Results Brazil nut 2S albumin was significantly more resistant to proteolytic digestion than other Brazil nut proteins. It was also resistant to thermally and chemically induced denaturation. Equally high resistance to proteolytic digestion was observed with sunflower seed 2S albumin. The recombinant albumins mirrored their native counterparts in stability and immunoreactivity.Conclusion The important food allergen Brazil nut 2S albumin is as stable to digestion as is sunflower seed 2S albumin, whose allergenicity has yet to be determined. The 2S albumins and their recombinant counterparts could not be easily denatured by physicochemical treatments. The results suggest that 2S albumin is the only Brazil nut protein to reach the gut immune system intact. The production of properly folded recombinant proteins will facilitate mechanistic studies as well as diagnostic testing and antigen-based therapies.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1046/j.1365-2222.2003.01736.x

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Reproductive systems Sex and the single lichen (2000)

Murtagh, G. J. ; Dyer, P. S. ; Crittenden, P. D.

[s.l.] : Macmillan Magazines Ltd.

Nature 404 (2000), S. 564-564

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ISSN: 1476-4687

Source: Nature Archives 1869 - 2009

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Notes: [Auszug] Most lichenized fungi produce abundant sexual structures, and in many species sexual spores seem to provide the only means of dispersal. For example, 90% of lichens found in Great Britain and Ireland produce ascomata (fruit bodies) containing sexually derived ascospores, whereas only 29% ...