ArticleJournal of virology2013
Outer domain of HIV-1 gp120: antigenic optimization, structural malleability, and crystal structure with antibody VRC-PG04.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- Structurally related but genetically unrelated antibody lineages converge on an immunodominant HIV-1 Env neutralizing determinant following trimer immunization.PLoS pathogens · 2021Article
- Strategies for inducing effective neutralizing antibody responses against HIV-1.Expert review of vaccines · 2019Review
- Integrity of Glycosylation Processing of a Glycan-Depleted Trimeric HIV-1 Immunogen Targeting Key B-Cell Lineages.Journal of proteome research · 2018Article
- Structural Characterization and Function Prediction of Immunoglobulin-like Fold in Cell Adhesion and Cell Signaling.Journal of chemical information and modeling · 2018Article
- Epitope-focused immunogens against the CD4-binding site of HIV-1 envelope protein induce neutralizing antibodies against auto- and heterologous viruses.The Journal of biological chemistry · 2018Article
- Effect of analytical treatment interruption and reinitiation of antiretroviral therapy on HIV reservoirs and immunologic parameters in infected individuals.PLoS pathogens · 2018Article
- Emerging viral diseases from a vaccinology perspective: preparing for the next pandemic.Nature immunology · 2018Review
- Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo.The Journal of experimental medicine · 2017Article
- Tryptophan 375 stabilizes the outer-domain core of gp120 for HIV vaccine immunogen design.Vaccine · 2017Article
- Insights from NMR Spectroscopy into the Conformational Properties of Man-9 and Its Recognition by Two HIV Binding Proteins.Chembiochem : a European journal of chemical biology · 2017Article
- Paring Down HIV Env: Design and Crystal Structure of a Stabilized Inner Domain of HIV-1 gp120 Displaying a Major ADCC Target of the A32 Region.Structure (London, England : 1993) · 2016Article
- Article
- Maturation and Diversity of the VRC01-Antibody Lineage over 15 Years of Chronic HIV-1 Infection.Cell · 2015Article
- Strategies to guide the antibody affinity maturation process.Current opinion in virology · 2015Review
- Computational tools for epitope vaccine design and evaluation.Current opinion in virology · 2015Review
- Eliciting neutralizing antibodies with gp120 outer domain constructs based on M-group consensus sequence.Virology · 2014Article
- Flow cytometry reveals that H5N1 vaccination elicits cross-reactive stem-directed antibodies from multiple Ig heavy-chain lineages.Journal of virology · 2014Article
- Diverse recombinant HIV-1 Envs fail to activate B cells expressing the germline B cell receptors of the broadly neutralizing anti-HIV-1 antibodies PG9 and 447-52D.Journal of virology · 2014Article
- A mammalian cell based FACS-panning platform for the selection of HIV-1 envelopes for vaccine development.PloS one · 2014Article
- Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer.Science (New York, N.Y.) · 2013Article
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Authors and funding
17 authors at 2 institutions in 1 country.
Funding
Abstract
The outer domain of the HIV-1 gp120 envelope glycoprotein contains the epitope for broadly neutralizing antibodies directed to the CD4-binding site, many of which are able to neutralize over 90% of circulating HIV-1 isolates. While the outer domain is conformationally more stable than other portions of the HIV-1 envelope, efforts to express the outer domain as an immunogen for eliciting broadly neutralizing antibodies have not been successful, potentially because natural outer domain variants do not bind strongly to antibodies such as VRC01. In this study, we optimized the antigenic properties of the HIV-1 Env outer domain to generate OD4.2.2, from the KER2018 strain of clade A HIV-1, enabling it to bind antibodies such as VRC01 with nanomolar affinity. The crystal structure of OD4.2.2 in complex with VRC-PG04 was solved at 3.0-Å resolution and compared to known crystal structures including (i) the structure of core gp120 bound by VRC-PG04 and (ii) a circularly permutated version of the outer domain in complex with antibody PGT128. Much of the VRC-PG04 epitope was preserved in the OD4.2.2 structure, though with altered N and C termini conformations. Overall, roughly one-third of the outer domain structure appeared to be fixed in conformation, independent of alterations in termini, clade, or ligand, while other portions of the outer domain displayed substantial structural malleability. The crystal structure of OD4.2.2 with VRC-PG04 provides atomic-level details for an HIV-1 domain recognized by broadly neutralizing antibodies and insights relevant to the rational design of an immunogen that could elicit such antibodies by vaccination.
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