Insights into the trimeric HIV-1 envelope glycoprotein structure

• We examine the recent structures of the HIV-1 Env glycoprotein trimer.
• Broadly neutralizing antibodies play a key role in HIV-1 Env structural studies.
• The antigenic surface of HIV-1 Env is a complex landscape of both glycans and peptides.

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.