Researchers have discovered a new method of attacking the HIV virus which may offer a solution to drug resistance.

Their method involves targeting the proteins of human cells, which bind with the virus. Many of the antiretroviral drugs that are used to fight HIV, the virus that causes AIDS, attack the proteins that exist on the surface of the virus, rendering it incapable of infecting healthy cells.

But as the virus can mutate, these targets can change and render these medications useless, even when physicians prescribe multi-drug "cocktails" that attack the virus on different fronts.

Plus, these multifaceted approaches often come with unpleasant and toxic side-effects.

On the other hand, proteins on human cells, such as immune cells called T-cells, are much less likely to mutate, making them more reliable therapeutic targets, according to the authors.

In the study conducted by researchers at the National Human Genome Research Institute (NHGRI), and funded by the National Institutes of Health, modification of a human protein called interleukin-2-inducible T-cell kinase (ITK) slowed the infection of healthy immune cells with the virus. Interleukin-2 is a protein that activates T-cells to attack foreign invaders.

T-cells are infected when HIV attacks and their defence role becomes instead a replication of the virus. The researchers found that when the interleukin-2 protein was deactivated, the virus could not commandeer the T-cells as effectively, significantly slowing the spread of the virus.

"Finding a cellular target that can be inhibited so as to block HIV validates a novel concept and is an exciting model for deriving potential new HIV therapies," said NHGRI scientific director Eric Green, in a release.

The protein is already being investigated in the treatment of asthma and other autoimmune illnesses, according to the study.

"We hope that others will extend our findings and that ITK inhibitors will be pursued as HIV therapies," said Pamela Schwartzberg, a senior investigator for the NHGRI.

The findings were published online Monday in the Proceedings of the National Academy of Sciences.