ArticleProceedings of the National Academy of Sciences of the United States of America2013
Molecular structures of trimeric HIV-1 Env in complex with small antibody derivatives.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 38 citations in OpenAlex.
- Cryo-electron microscopy in the study of virus entry and infection.Frontiers in molecular biosciences · 2024Review
- Human parainfluenza virus fusion complex glycoproteins imaged in action on authentic viral surfaces.PLoS pathogens · 2020Article
- HIV-1 Envelope and MPER Antibody Structures in Lipid Assemblies.Cell reports · 2020Article
- Cryo-EM Studies of Virus-Antibody Immune Complexes.Virologica Sinica · 2020Review
- Rapid Elimination of Broadly Neutralizing Antibodies Correlates with Treatment Failure in the Acute Phase of Simian-Human Immunodeficiency Virus Infection.Journal of virology · 2019Article
- Nanobodies that Neutralize HIV.Vaccines · 2019Review
- Super Potent Bispecific Llama VHH Antibodies Neutralize HIV via a Combination of gp41 and gp120 Epitopes.Antibodies (Basel, Switzerland) · 2019Article
- Article
- Computational study of HIV gp120 as a target for polyanionic entry inhibitors: Exploiting the V3 loop region.PloS one · 2018Article
- Saturation Mutagenesis of the HIV-1 Envelope CD4 Binding Loop Reveals Residues Controlling Distinct Trimer Conformations.PLoS pathogens · 2016Article
- PRISM-EM: template interface-based modelling of multi-protein complexes guided by cryo-electron microscopy density maps.Acta crystallographica. Section D, Structural biology · 2016Article
- CD4-Induced Antibodies Promote Association of the HIV-1 Envelope Glycoprotein with CD4-Binding Site Antibodies.Journal of virology · 2016Article
- Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design.Annual review of immunology · 2016Review
- Germlining of the HIV-1 broadly neutralizing antibody domain m36.Antiviral research · 2015Article
- Homology models of the HIV-1 attachment inhibitor BMS-626529 bound to gp120 suggest a unique mechanism of action.Proteins · 2015Article
- Griffithsin tandemers: flexible and potent lectin inhibitors of the human immunodeficiency virus.Retrovirology · 2015Article
- Article
- A fusion intermediate gp41 immunogen elicits neutralizing antibodies to HIV-1.The Journal of biological chemistry · 2014Article
- Rational design and characterization of the novel, broad and potent bispecific HIV-1 neutralizing antibody iMabm36.Journal of acquired immune deficiency syndromes (1999) · 2014Article
- Progress in HIV-1 vaccine development.The Journal of allergy and clinical immunology · 2014Review
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
The extensive carbohydrate coat, the variability of protein structural features on HIV-1 envelope glycoproteins (Env), and the steric constraints of the virus-cell interface during infection, present challenges to the elicitation of effective full-length (~150 kDa), neutralizing antibodies against HIV. These hurdles have motivated the engineering of smaller antibody derivatives that can bind Env and neutralize the virus. To further understand the mechanisms by which these proteins neutralize HIV-1, we carried out cryoelectron tomography of native HIV-1 BaL virions complexed separately to two small (~15 kDa) HIV-neutralizing proteins: A12, which binds the CD4-binding site on Env, and m36, whose binding to Env is enhanced by CD4 binding. We show that despite their small size, the presence of these proteins and their effects on the quaternary conformation of trimeric Env can be visualized in molecular structures derived by cryoelectron tomography combined with subvolume averaging. Binding of Env to A12 results in a conformational change that is comparable to changes observed upon its binding to the CD4-binding site antibody, b12. In contrast, binding of Env to m36 results in an "open" quaternary conformation similar to that seen with binding of soluble CD4 or the CD4i antibody, 17b. Because these small neutralizing proteins are less sterically hindered than full-length antibodies at zones of virus-cell contact, the finding that their binding has the same structural consequences as that of other broadly neutralizing antibodies highlights their potential for use in therapeutic applications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.