Field measurements of a massive Porites coral at Goolboodi (Orpheus Island), Great Barrier Reef.

An exceptionally large coral Porites sp. has been identified and measured at Goolboodi (Orpheus Island), Great Barrier Reef (GBR). This coral was measured in March 2021 during citizen science research of coral reefs in the Palm Islands group. We conducted a literature review and consulted scientists to compare the size, age and health of the Porites with others in the GBR and internationally. This is the largest diameter Porites coral measured by scientists and the sixth highest coral measured in the GBR. The health of the Porites was assessed as very good with over 70% live coral cover and minor percentages of sponge, live coral rock and macroalgae. An estimated age of 421-438 years was calculated based on linear growth models. Manbarra Traditional Owners were consulted and suggested that the Porites be named Muga dhambi (big coral) to communicate traditional knowledge, language and culture to indigenous, tourists, scientists and students.

Characterization of conformation-dependent prion protein epitopes.

Whereas prion replication involves structural rearrangement of cellular prion protein (PrP(C)), the existence of conformational epitopes remains speculative and controversial, and PrP transformation is monitored by immunoblot detection of PrP(27-30), a protease-resistant counterpart of the pathogenic scrapie form (PrP(Sc)) of PrP. We now describe the involvement of specific amino acids in conformational determinants of novel monoclonal antibodies (mAbs) raised against randomly chimeric PrP. Epitope recognition of two mAbs depended on polymorphisms controlling disease susceptibility. Detection by one, referred to as PRC5, required alanine and asparagine at discontinuous mouse PrP residues 132 and 158, which acquire proximity when residues 126-218 form a structured globular domain. The discontinuous epitope of glycosylation-dependent mAb PRC7 also mapped within this domain at residues 154 and 185. In accordance with their conformational dependence, tertiary structure perturbations compromised recognition by PRC5, PRC7, as well as previously characterized mAbs whose epitopes also reside in the globular domain, whereas conformation-independent epitopes proximal or distal to this region were refractory to such destabilizing treatments. Our studies also address the paradox of how conformational epitopes remain functional following denaturing treatments and indicate that cellular PrP and PrP(27-30) both renature to a common structure that reconstitutes the globular domain.