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Structure of Key Protein in Common HIV Subgroup Uncovered

Scientists from the California Institute of Technology (Caltech) have provided the first-ever glimpse of the structure of a key protein -- gp120 -- found on the surface of a specific subgroup of the human immunodeficiency virus, HIV-1. In addition, they demonstrated that a particular antibody to gp120 makes contact not only with the protein, but with the CD4 receptor that gp120 uses to gain entrance into the body's T cells.

This three-dimensional understanding of how gp120 is built is more than just a basic scientific advance. "There's a tremendous continuing effort to develop a vaccine for HIV," says Caltech postdoctoral scholar Ron Diskin, "and most of those efforts use gp120. Having more structural information will facilitate better vaccine design."

The findings are detailed in a paper published in the advance online edition of the journal Nature Structural & Molecular Biology.

The team looked specifically at gp120 from what is known as clade C HIV-1. To explain what that means, here's a brief HIV family history: Most people who get HIV and proceed to AIDS are infected with a member of the HIV-1 family of viruses. HIV-1 is divided into groups; most AIDS-related strains of the virus come from group M. The groups are further subdivided into what are known as clades.
 
 

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