Abstract:
:Current human immunodeficiency virus-1 (HIV-1) vaccines elicit strain-specific neutralizing antibodies. However, cross-reactive neutralizing antibodies arise in approximately 20% of HIV-1-infected individuals, and details of their generation could provide a blueprint for effective vaccination. Here we report the isolation, evolution and structure of a broadly neutralizing antibody from an African donor followed from the time of infection. The mature antibody, CH103, neutralized approximately 55% of HIV-1 isolates, and its co-crystal structure with the HIV-1 envelope protein gp120 revealed a new loop-based mechanism of CD4-binding-site recognition. Virus and antibody gene sequencing revealed concomitant virus evolution and antibody maturation. Notably, the unmutated common ancestor of the CH103 lineage avidly bound the transmitted/founder HIV-1 envelope glycoprotein, and evolution of antibody neutralization breadth was preceded by extensive viral diversification in and near the CH103 epitope. These data determine the viral and antibody evolution leading to induction of a lineage of HIV-1 broadly neutralizing antibodies, and provide insights into strategies to elicit similar antibodies by vaccination.
journal_name
Naturejournal_title
Natureauthors
Liao HX,Lynch R,Zhou T,Gao F,Alam SM,Boyd SD,Fire AZ,Roskin KM,Schramm CA,Zhang Z,Zhu J,Shapiro L,NISC Comparative Sequencing Program.,Mullikin JC,Gnanakaran S,Hraber P,Wiehe K,Kelsoe G,Yang G,Xia SM,Montefiori DCdoi
10.1038/nature12053subject
Has Abstractpub_date
2013-04-25 00:00:00pages
469-76issue
7446eissn
0028-0836issn
1476-4687pii
nature12053journal_volume
496pub_type
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