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Two Scientists Just Figured Out How to Stop HIV From Progressing Into AIDS

Two Scientists Just Figured Out How to Stop HIV From Progressing Into AIDS

A closer look at the protein Nef has just changed the landscape of HIV research —  and treatment.

A more sophisticated approach to antiretroviral therapy is in the works, one that focuses on Nef, a protein responsible in the progression from HIV to AIDS. Researcher Mike Kent from Sandia National Laboratories and Northeastern University bioanalytical chemistry professor John Engan combined their scientific methods to find out how to stop Nef (Negative Regulatory Factor) from disrupting the immune system. What they discovered was mind blowing.

First of all, let’s talk about how Nef is able to turn HIV into AIDS. What you need to know about Nef is that it’s a shape shifter; it has to change its shape, otherwise it will not be able to interact with host proteins. Once it shapes itself, Nef is able to bind to an infected cell’s membrane, where it basically corrupts cellular communications (like all viruses do), making it a lot easier for the virus to multiply.

The shape shifting abilities of Nef is key to corrupting its host, according to the findings. In fact, it’s so important that when rhesus monkeys were infected with an AIDS-related virus that did not contain Nef, they never developed immune deficiency symptoms. Without its ability to shape shift, Nef cannot corrupt more cells.

By combining their individual expertise, Kent and Engan were able to get to the heart of the matter. Kent’s forte is in neutron reflectometry, a method that scales film and biological membrane information down to nanometers (or one-billionth of a meter). Engan’s expertise is in hydrogen-deuterium exchange mass spectrometry, a method that calculates the local structure and flexibility of proteins. It was only a matter of time before these methods found each other. 

Along with their team, Kent and Engan are using their knowledge to discover how Nef can change its shape, but more importantly how to stop it in its tracks.

“We studied [Nef] alone,” Kent said in a Sandia statement. “Now we want to study it with its binding partners, with the host proteins and the complexes that it forms, and in the presence of drug molecules or inhibitors. Stopping it from binding with its partners or inhibiting it from adopting the conformation that leads to receptor degradation would have important medical implications.”

If all goes according to plan, Kent and Engan’s findings will expose a construct of how HIV and other viruses are spread. Their hybrid method is the first of its kind to get this type of direct information about membrane proteins, and in the future it has the potential of solving other cellular dysfunctions — like cholesterol regulation and cancer.

Kent says he hopes to apply the hybrid method “beyond just one HIV protein.” Now that science has cracked a window into the future of cell analysis, perhaps we might see more advances in HIV research.

Gotta love science. 

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David Artavia

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