|Title||Insights into the trimeric HIV-1 envelope glycoprotein structure.|
|Publication Type||Journal Article|
|Year of Publication||2015|
|Authors||Ward AB, Wilson IA|
|Journal||Trends Biochem Sci|
The HIV-1 envelope glycoprotein (Env) trimer is responsible for receptor recognition and viral fusion with CD4(+) T cells, and is the sole target for neutralizing antibodies. Thus, understanding its molecular architecture is of significant interest. However, the Env trimer has proved to be a challenging target for 3D structure determination. Recent electron microscopy (EM) and X-ray structures have at last enabled us to decipher the structural complexity and unique features of the Env trimer, and how it is recognized by an ever-expanding arsenal of potent broadly neutralizing antibodies. We describe our current knowledge of the Env trimer structure in the context of exciting recent developments in the identification and characterization of HIV broadly neutralizing antibodies.
|Alternate Journal||Trends Biochem. Sci.|
|Grant List||P01 AI082362 / AI / NIAID NIH HHS / United States |
R01 AI084817 / AI / NIAID NIH HHS / United States
UM1 AI100663 / AI / NIAID NIH HHS / United States
Insights into the trimeric HIV-1 envelope glycoprotein structure.