Legitimising Belief: Identity Politics,Utility, Strategies of Concealment,and Rationalisation in Australian Aboriginal Religion

The ‘women's business’ on Hindmarsh Island has had spectacular success although vital evidence had been kept secret ‘in a sealed envelope’. This paper, drawing primarily on the author's own encounter with the native title claims procedure, discusses various formative processes involved in the contemporary construction of Aboriginal indigeneity in which religious belief is heavily valorised. Subjected to a process of rationalisation for a long time, religious traditions are now being used as a strategic resource in native title claims. In the endeavour to make best possible use of the jurisprudential opportunity offered, the maintenance of secrecy and cloaking of information emerges as an important strategy. Secrecy clearly is an integral part of traditional Aboriginal culture. However, cloaking in fact may not only privilege esoteric contents, but merge with attempts of deliberate deception. Yet, in itself this too might be considered an Aboriginal cultural tradition.     

Concealment of epitope by reduction and alkylation in prion protein

Conversion of the cellular prion protein (PrP(C)) into its pathological isoform (PrP(Sc)), the key molecular event in the pathogenesis of prion diseases, is accompanied by a conformational transition of alpha-helix into beta-sheet structures involving alpha-helix 1 (alpha1) domain from residues 144 to 154 of the protein. Reduction and alkylation of PrP(C) have been found to inhibit the conversion of PrP(C) into PrP(Sc) in vitro. Here we report that while antibody affinity of epitopes in the N- and C-terminal domains remained unchanged, reduction and alkylation of the PrP molecule induced complete concealment of an epitope in alpha1 for anti-PrP antibody 6H4 that is able to cure prion infection in the cell model. Mass spectrometric analysis of recombinant PrP showed that the alkylation reaction takes place at reduced cysteines but no modification was observed in this cryptic epitope. Our study suggests that reduction and alkylation result in local or global rearrangement of PrP tertiary structure that is maintained in both liquid and solid phases. The implications in the conversion of PrP(C) into PrP(Sc) and the therapeutics of prion diseases are discussed.