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oai:repisalud.isciii.es:20.500.12105/92552025-04-03T19:04:01Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Sliepen, Kwinten author Han, Byung Woo author Bontjer, Ilja author Mooij, Petra author Garces, Fernando author Behrens, Anna-Janina author Rantalainen, Kimmo author Kumar, Sonu author Sarkar, Anita author Brouwer, Philip J M author Hua, Yuanzi author Tolazzi, Monica author Schermer, Edith author Torres, Jonathan L author Ozorowski, Gabriel author van der Woude, Patricia author Torrents de la Peña, Alba author van Breemen, Mariëlle J author Camacho-Sánchez, Juan Miguel author Burger, Judith A author Medina-Ramírez, Max author Gonzalez-Fernandez, Nuria author Alcamí, José author LaBranche, Celia author Scarlatti, Gabriella author van Gils, Marit J author Crispin, Max author Montefiori, David C author Ward, Andrew B author Koopman, Gerrit author Moore, John P author Shattock, Robin J author Bogers, Willy M author Wilson, Ian A author Sanders, Rogier W author 2019 Stabilized HIV-1 envelope glycoproteins (Env) that resemble the native Env are utilized in vaccination strategies aimed at inducing broadly neutralizing antibodies (bNAbs). To limit the exposure of rare isolate-specific antigenic residues/determinants we generated a SOSIP trimer based on a consensus sequence of all HIV-1 group M isolates (ConM). The ConM trimer displays the epitopes of most known bNAbs and several germline bNAb precursors. The crystal structure of the ConM trimer at 3.9 Å resolution resembles that of the native Env trimer and its antigenic surface displays few rare residues. The ConM trimer elicits strong NAb responses against the autologous virus in rabbits and macaques that are significantly enhanced when it is presented on ferritin nanoparticles. The dominant NAb specificity is directed against an epitope at or close to the trimer apex. Immunogens based on consensus sequences might have utility in engineering vaccines against HIV-1 and other viruses. Nat Commun. 2019 May 29;10(1):2355 10.1038/s41467-019-10262-5 2041-1723 2041-1723 Nature communications 31142746 http://hdl.handle.net/20.500.12105/9255 Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence