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Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus.

Publication ,  Journal Article
Liao, H-X; Lynch, R; Zhou, T; Gao, F; Alam, SM; Boyd, SD; Fire, AZ; Roskin, KM; Schramm, CA; Zhang, Z; Zhu, J; Shapiro, L; Mullikin, JC ...
Published in: Nature
April 25, 2013

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.

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Published In

Nature

DOI

EISSN

1476-4687

Publication Date

April 25, 2013

Volume

496

Issue

7446

Start / End Page

469 / 476

Location

England

Related Subject Headings

  • Protein Structure, Tertiary
  • Phylogeny
  • Neutralization Tests
  • Mutation
  • Molecular Sequence Data
  • Models, Molecular
  • Humans
  • HIV-1
  • HIV Envelope Protein gp120
  • HIV Antibodies
 

Citation

APA
Chicago
ICMJE
MLA
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Liao, H.-X., Lynch, R., Zhou, T., Gao, F., Alam, S. M., Boyd, S. D., … Haynes, B. F. (2013). Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature, 496(7446), 469–476. https://doi.org/10.1038/nature12053
Liao, Hua-Xin, Rebecca Lynch, Tongqing Zhou, Feng Gao, S Munir Alam, Scott D. Boyd, Andrew Z. Fire, et al. “Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus.Nature 496, no. 7446 (April 25, 2013): 469–76. https://doi.org/10.1038/nature12053.
Liao H-X, Lynch R, Zhou T, Gao F, Alam SM, Boyd SD, et al. Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature. 2013 Apr 25;496(7446):469–76.
Liao, Hua-Xin, et al. “Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus.Nature, vol. 496, no. 7446, Apr. 2013, pp. 469–76. Pubmed, doi:10.1038/nature12053.
Liao H-X, 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 S-M, Montefiori DC, Parks R, Lloyd KE, Scearce RM, Soderberg KA, Cohen M, Kamanga G, Louder MK, Tran LM, Chen Y, Cai F, Chen S, Moquin S, Du X, Joyce MG, Srivatsan S, Zhang B, Zheng A, Shaw GM, Hahn BH, Kepler TB, Korber BTM, Kwong PD, Mascola JR, Haynes BF. Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature. 2013 Apr 25;496(7446):469–476.
Journal cover image

Published In

Nature

DOI

EISSN

1476-4687

Publication Date

April 25, 2013

Volume

496

Issue

7446

Start / End Page

469 / 476

Location

England

Related Subject Headings

  • Protein Structure, Tertiary
  • Phylogeny
  • Neutralization Tests
  • Mutation
  • Molecular Sequence Data
  • Models, Molecular
  • Humans
  • HIV-1
  • HIV Envelope Protein gp120
  • HIV Antibodies