Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer.

HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo–electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science , this issue p. [1043][1] [1]: /lookup/volpage/351/1043?iss=6277