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Title: Study of molecular mechanisms that confer allergenicity to 2S albumin proteins in vitro : Ber e 1 as a model system
Author: Jambari, Nuzul Noorahya
ISNI:       0000 0004 6352 0046
Awarding Body: University of Nottingham
Current Institution: University of Nottingham
Date of Award: 2016
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In order to study the intrinsic allergenicity of the plant-based storage 2S albumins Ber e I, the major allergen from Brazil nut seeds (Bertholletia excelsa) and the related but weak allergenic SFA8 from sunflower seeds (Helianthus anniuis), were used as model proteins. Previous studies showed that stimulation of bmDCs with Ber e 1 and SFA8 resulted in polarised DC programming that affect DC maturation state and Thl/Th2 responses. The recombinant Ber e 1 (rBer e 1) and SFA8 (rSFA8) produced in P. pastoris expression system were shown to retain the tertiary structure, biochemical properties and immunoreactivity of their native counterparts. However, previous findings indicate that rBer e 1 is glycosylated whereas native Ber e 1 (nBer e 1) is not. Glycosylation of proteins has been shown to increase immunogenicity of antigens and characterised as allergenic Th2 adjuvant in other systems. Thus amongst other objectives, the main aim of this study was to determine whether glycosylation plays a role as an antigenic determinant for Ber e 1 and its effects on the immunogenicity of the protein. Furthermore, we questioned whether the differences in intrinsic properties of the 2S albumin model allergens affect the modulation of gene expression in dendritic cells that may result in the polarisation of Thl/Th2 response. The glycosylation patterns of rBer e 1 and nBer e 1 extracted from Brazil nut were detected and profiled by periodic acid Schiff’s (PAS)-SDS-PAGE and mass spectrometry (MS). MS analysis confirmed that mannose residues are present in rBer e 1.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available