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For papers that will be published online on 31 March 2010
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A look at clade C HIV-1
DOI: 10.1038/nsmb.1796
The crystal structure of a protein involved in the spread of the most common HIV virus subtype, clade C, is described online in Nature Structural and Molecular Biology this week. Viral glycoprotein gp120 is known to interact with the protein CD4 on the surface of helper T-cells initiating the process of HIV-1 entry into the cell. The new structure captures a clade C HIV-1 gp120 together with CD4 and a patient-derived antibody, and shows that the antibody makes contact with both the foreign protein (gp120) and the human protein (CD4).
Clade C is the most prevalent genetic subtype of HIV-1 in the world today and one of the least studied. It is responsible for the majority of infections in the African continent and other developing regions. The structure, described by Pamela Bjorkman and colleagues, is similar to gp120 structures from other HIV subtypes, but given the public health toll from clade C strains, validating these similarities and defining any differences is an important step in the development of therapeutics. The fact that this antibody reacts with both CD4 and gp120 antigens at the same time suggests that responses to HIV-1 may come at the price of attacking the body’s own cells.
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Pamela Bjorkman (California Institute of Technology, Pasadena, CA, USA)
Tel: +1 626 395 8350; E-mail: [email protected]
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