Research Press Release

Playing offense to HIV’s defense

Nature Biotechnology

October 7, 2013

An approach which resurrects the potency of therapeutic antibodies against which HIV has developed resistance is reported in a paper published in Nature Biotechnology this week. In addition to describing a method to engineer an antibody that appears effective against a large number of HIV-1 strains, the authors suggest that the engineering strategy presented might be useful for improving other therapeutic antibodies.

The antibody described in the study, ibalizumab, acts by blocking a receptor that HIV-1 uses to enter cells. However, HIV-1 strains in some patients treated with ibalizumab acquire particular mutations that make them resistant to the antibody. Structural studies have showed that these mutations loosen the interaction between HIV-1 and ibalizumab by introducing a gap between the virus and the antibody.

Suspecting that this gap contributes to HIV-1 resistance, David Ho and colleagues reasoned that ‘refilling’ it would counter the virus’ evasive maneuver. To test this theory they tagged ibalizumab with a carbohydrate near its site of interaction with the virus. The carbohydrate-tagged antibody neutralized 100% of tested HIV-1 strains, including strains resistant to the unmodified antibody.


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