Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer
2013
Julien, Jean-Philippe | Cupo, Albert | Sok, Devin | Stanfield, Robyn L. | Lyumkis, Dmitry | Deller, Marc C. | Klasse, Per-Johan | Burton, Dennis R. | Sanders, Rogier W. | Moore, John P. | Ward, Andrew B. | Wilson, I. A. (Ian A.)
Knowing the Enemy Infection of host cells by HIV-1 is mediated by an envelope glycoprotein (Env) trimeric spike on the surface of the virus. Proteins comprising the Env trimer must be cleaved for infectivity, and thus viral fusion involves three Env conformations. The flexibility of the Env trimer has made it a challenge to determine a high-resolution structure, although such a structure is key both for understanding trimer function and for guiding vaccine design. Lyumkis et al. (p. 1484) and Julien et al. (p. 1477) studied soluble cleaved trimers stabilized by specific mutations but that have kept a near-native antigenicity profile. Lyumkis et al. present a high-resolution structure of the trimer in complex with a broadly neutralizing antibody, and Julien et al. present a crystal structure of the trimer in complex with another broadly neutralizing antibody.
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