An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Microbiology (medical),Genetics,Applied Microbiology and Biotechnology,Immunology,Microbiology
Link
http://www.nature.com/articles/nmicrobiol2016199.pdf
Reference56 articles.
1. Burton, D. R. & Mascola, J. R. Antibody responses to envelope glycoproteins in HIV-1 infection. Nat. Immunol. 16, 571–576 (2015).
2. Doria-Rose, N. A. et al. Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies. J. Virol. 83, 188–199 (2009).
3. Simek, M. D. et al. HIV-1 elite neutralizers: individuals with broad and potent neutralizing activity identified using a high throughput neutralization assay together with an analytical selection algorithm. J. Virol. 83, 7337–7348 (2009).
4. Euler, Z. & Schuitemaker, H. Cross-reactive broadly neutralizing antibodies: timing is everything. Front. Immunol. 3, 215 (2012).
5. van Gils, M. J. & Sanders, R. W. In vivo protection by broadly neutralizing HIV antibodies. Trends Microbiol. 22, 550–551 (2014).
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