Snail pox can treat severe forms of malaria

Heavy forms of malaria as Plasmodium falciparum it can be fatal even after treatment with conventional parasite killing drugs. This is due to persistent cyto-adhesion of infectious erythrocytes even though existing parasites within the red blood cells are dead.

Because vaccines for malaria have been less than moderately effective, and for the treatment of these difficult cases of P. falciparum malaria, new pathways are urgently needed. The latest estimates show that more than 500 million cases of malaria and more than 400,000 deaths are reported worldwide each year. Anti-adhesion drugs may be a key way to significantly improve survival rates.

Using poisons from Conus nux, species of sea snail, a first-class study from Florida Atlantic University’s Schmidt College of Medicine in collaboration with FAU’s Charles E. Schmidt College of Science and Department of Chemical Sciences, National Institute of Standards and Technology, U.S. Department of Commerce, suggest that these conotoxins may treat malaria.

The study provides important directions towards the development of novel and cost-effective anti-adhesion medications or blockade-therapy aimed at combating the pathology of malignant malaria.

Results, published in the Iris of Proteomics, expanding pharmacological availability of conotoxins / conopeptides by demonstrating the ability to inhibit protein-protein and protein-polysaccharide interactions that directly contribute to the disease.

Similarly, mitigation of emerging diseases such as AIDS and COVID-19 may also benefit from conotoxins as potential inhibitors of protein-protein interactions as a treatment. Venom peptides from cone snails have the ability to treat innumerable diseases using preventive therapies.

Molecular stability, small size, flexibility, intravenous delivery, or immunogenic response make conotoxins excellent candidates for therapeutic inhibition. Conotoxins have been strongly studied for decades as molecular probes and drug drivers targeting the major nervous systems. They should also be examined for novel applications aimed at inhibiting amiss cellular responses or attenuating host parasite interactions through binding to endogenous and exogenous proteins.

Further research is likely to rule out breakdowns in areas that are continuously needed for more effective therapeutic approaches such as cancer, autoimmune diseases, emerging viral infections as well as malaria where whether natural poison-based peptidic products can be applied. “

Andrew V. Oleinikov, Ph.D., Corresponding Author Study and Professor of Biomedical Science, Schmidt College of Medicine, Atlantic University of Florida

The interaction of protein-proteins with conotoxins is an extension of their well-known inhibitory action in many ion channels and receptors. Eliminating prey by altering their nervous system in particular is a governing principle in the mode of action of toxins.

“More than 850 species of cone snails include hundreds of thousands of miscellaneous poisonous exopeptides selected through several million years of evolution to capture their prey and deter predators,” said Frank Marí, Ph.D., associate author and senior consultant for biochemical sciences at the National Institute of General Technology. “They do so by targeting several surface proteins present in excitable target cells. This large biomolecular library of conopeptides can be studied for use as therapeutic guidelines against chronic and developing diseases. emerges that affect non-restrictive systems. “

For the study, researchers used high-throughput evaluations for analysis Conus nux collected off the Pacific coast of Costa Rica. They appeared the in vitro the ability of cone snail poisons to inhibit protein-protein and protein-polysaccharide interactions that directly contribute to the pathology of P. falciparum malaria. They concluded that six fractions from the toxin inhibit adherence P. falciparum erythrocyte membrane protein domains 1 (PfEMP-1) to their corresponding receptors, which express the endothelial and placenta microvasculature.

The results are noteworthy as each of the six toxin fractions, consisting mainly or very little of a set of peptides, is associated with a link between domains with different receptor specificity and the co-receptors. corresponding to them, which are proteins (CD36 and ICAM-1), and polysaccharide.

This activity profile suggests that the peptides in these conotoxin fractions either bind to common structural elements in the different PfEMP1 regions, or that several different peptides in the proportion may interact to h -efficient (the density of each is lower depending on the complexity) with different ranges.