ArticleJournal of virology2005
Stoichiometry of antibody neutralization of human immunodeficiency virus type 1.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 61 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
61 citing papers in PubMed.
- Potent human immunodeficiency virus-neutralizing and complement lysis activities of antibodies are not obligatorily linked.Journal of virology · 2008Trial
- Article
- Structural and genetic convergence of HIV-1 neutralizing antibodies in vaccinated non-human primates.PLoS pathogens · 2021Article
- A biophysical perspective on receptor-mediated virus entry with a focus on HIV.Biochimica et biophysica acta. Biomembranes · 2020Review
- Structural Basis for Epitopes in the gp120 Cluster A Region that Invokes Potent Effector Cell Activity.Viruses · 2019Review
- Predicting HIV-1 transmission and antibody neutralization efficacy in vivo from stoichiometric parameters.PLoS pathogens · 2017Article
- Deconstructing the Antiviral Neutralizing-Antibody Response: Implications for Vaccine Development and Immunity.Microbiology and molecular biology reviews : MMBR · 2016Review
- Using Computational Modeling To Optimize the Design of Antibodies That Trap Viruses in Mucus.ACS infectious diseases · 2016Article
- Mathematical model of multivalent virus-antibody complex formation in humans following acute and chronic HIV infections.Journal of mathematical biology · 2015Article
- Mutations in HIV-1 envelope that enhance entry with the macaque CD4 receptor alter antibody recognition by disrupting quaternary interactions within the trimer.Journal of virology · 2015Article
- Different infectivity of HIV-1 strains is linked to number of envelope trimers required for entry.PLoS pathogens · 2015Article
- Molecular determinants of the ratio of inert to infectious virus particles.Progress in molecular biology and translational science · 2015Review
- Antibody responses during hepatitis B viral infection.PLoS computational biology · 2014Article
- Antibody to gp41 MPER alters functional properties of HIV-1 Env without complete neutralization.PLoS pathogens · 2014Article
- Transient antibody-mucin interactions produce a dynamic molecular shield against viral invasion.Biophysical journal · 2014Article
- Article
- Modeling virus- and antibody-specific factors to predict human immunodeficiency virus neutralization efficiency.Cell host & microbe · 2013Article
- Inhibition of the HIV-1 spike by single-PG9/16-antibody binding suggests a coordinated-activation model for its three protomeric units.Journal of virology · 2013Article
- The highly conserved layer-3 component of the HIV-1 gp120 inner domain is critical for CD4-required conformational transitions.Journal of virology · 2013Article
- Virus neutralisation: new insights from kinetic neutralisation curves.PLoS computational biology · 2013Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
Abstract
The human immunodeficiency virus envelope glycoproteins function as trimers on the viral surface, where they are targeted by neutralizing antibodies. Different monoclonal antibodies neutralize human immunodeficiency virus type 1 (HIV-1) infectivity by binding to structurally and functionally distinct moieties on the envelope glycoprotein trimer. By measuring antibody neutralization of viruses with mixtures of neutralization-sensitive and neutralization-resistant envelope glycoproteins, we demonstrate that the HIV-1 envelope glycoprotein trimer is inactivated by the binding of a single antibody molecule. Virus neutralization requires essentially all of the functional trimers to be occupied by at least one antibody. This model applies to antibodies differing in neutralizing potency and to virus isolates with various neutralization sensitivities. Understanding these requirements for HIV-1 neutralization by antibodies will assist in establishing goals for an effective AIDS vaccine.
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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.