Crocodiles could save us from deadly infections latrobe NatureComms
. As there are no other reported TEM images of β-defensin:lipid oligomers to date, it is currently unknown if the CpoBD13:PA sheet-like morphology observed is representative for β-defensins. However, it is likely that these structures are exaggerated versions of smaller physiological membrane disruption complexes that are generated only within localised regions of the fungal membrane upon accumulation of CpoBD13 to those regions enriched with PA.
Overall, our findings reveal that the structure and lipid-binding capability of β-defensins have been conserved from the divergence of humans and reptiles to the present day. Intriguingly, the structure of our CpoBD13:PA complex revealed the existence of large and continuous helical oligomers. Whilst phospholipid binding has been previously shown for other-defensin:phospholipid oligomeric membrane attack complexes remained unresolved to date.
, or with an additional C-terminal haemagglutinin tag was codon-optimised for expression in the methylotrophic yeast, synthesised by Bioneer Pacific , subcloned into the pPIC9 vector for recombinant protein expression in. CpoBD13 point mutations were generated using the QuikChange II Site-Directed Mutagenesis Kit as per the manufacturer’s instructions. CpoBD13 compound mutants were synthesised by GenScript Biotech directly into the pPIC9 vector.
. For propidium iodide uptake assays in serum-free medium, U937 cells were washed once in serum-free RPMI-1640, pelleted again and resuspended in serum-free media. 4×10cells were seeded and incubated with a range of CpoBD13 concentrations for 30 min at 37°C. PI was added to a final concentration of 1 µg/mL before analysis by flow cytometry using a BD FACSCanto II with FACSDiva 8.0.1 .
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