User:Wade Cook/Sandbox 1: Difference between revisions

In the figure above, [A] shows the amino acid residues located within the active site of eukaryotic topoisomerase 1B. [B] shows the amino acid residues located within the active site of viral topoisomerase 1B. Both active sites contain similar residues and are highly conserved among the different species. Researchers have proven that an asparagine residue can replace the histidine residue in the active site of both eukaryotic and viral topoisomerase, and the enzyme will still undergo the same cleavage mechanism. This suggests that the same cleavage and reliagation mechanisms are the same in all topoisomerase 1B’s (Baker et al, 2009).Type IB topoisomerase is a key target for research against the spread of smallpox because it is integral for the viruses replication process. The replication of smallpox is complicated since it doesn’t hijack the host’s genetic machinery to reproduce, this makes the disease highly virulent, and hard to specifically target for elimination by antiviral drugs (Berwald, 2004).

Smallpox is a highly contagious disease, which accounts for its massive epidemics killing millions around the world. Although smallpox was declared eradicated by the WHO in 1980, there has been recent public concern about the use of smallpox as a biological weapon. This represents a serious threat to civilian populations, which stresses the importance of understanding molecular dynamics, mechanism and, risk, in order to prevent and control it in case of an outbreak.