Enzyme Treatment Removes HIV DNA from Infected Cells

A recent report described the use of a tailored, recombinant enzyme to remove fragments of the human immunodeficiency virus (HIV) genome from the cells of individuals infected with the virus.

HIV succeeds in infiltrating the host immune system by integrating its DNA into the host's T-cell genome. An enzyme called integrase is responsible for this process. HIV integrase is a 32-kDa protein produced from the C-terminal portion of the Pol gene product. It catalyzes two reactions: 3'-end processing, in which two deoxynucleotides are removed from the 3' ends of the viral DNA; and the strand transfer reaction, in which the processed 3' ends of the viral DNA are covalently ligated to the host chromosomal DNA.

Investigators at the Max Planck Institute for Molecular Cell Biology and Genetics (Dresden, Germany) and the University of Hamburg (Germany) worked with a bacterial recombinase, a DNA-cutting enzyme that had been adapted for adding and subtracting genes from mice and other multi-celled organisms. They treated cultured T-cells that contained HIV genes with various versions of mutated recombinase.

Results published in the June 29, 2007, issue of the journal Science revealed that one mutant, Tre recombinase, was able to remove the HIV genes from the T-cells. The researchers concluded, "Although a long way from use in the clinic, we speculate that this type of technology might be adapted in future antiretroviral therapies, among other possible uses.”


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Max Planck Institute for Molecular Cell Biology and Genetics
University of Hamburg