ArticleJournal of virology1999
Stoichiometry of monoclonal antibody neutralization of T-cell line-adapted human immunodeficiency virus type 1.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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.
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Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Using Computational Modeling To Optimize the Design of Antibodies That Trap Viruses in Mucus.ACS infectious diseases · 2016Article
- Transient antibody-mucin interactions produce a dynamic molecular shield against viral invasion.Biophysical journal · 2014Article
- Article
- Virus neutralisation: new insights from kinetic neutralisation curves.PLoS computational biology · 2013Article
- Article
- Analysis of the subunit stoichiometries in viral entry.PloS one · 2012Article
- Intraprotomer masking of third variable loop (V3) epitopes by the first and second variable loops (V1V2) within the native HIV-1 envelope glycoprotein trimer.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16.Journal of virology · 2010Article
- Neutralization efficiency is greatly enhanced by bivalent binding of an antibody to epitopes in the V4 region and the membrane-proximal external region within one trimer of human immunodeficiency virus type 1 glycoproteins.Journal of virology · 2010Article
- Estimating the stoichiometry of HIV neutralization.PLoS computational biology · 2010Article
- Estimating the stoichiometry of human immunodeficiency virus entry.Journal of virology · 2009Article
- Relationship of HIV-1 and SIV envelope glycoprotein trimer occupation and neutralization.Virology · 2008Article
- Article
- The stoichiometry of antibody-mediated neutralization and enhancement of West Nile virus infection.Cell host & microbe · 2007Article
- Stoichiometry of murine leukemia virus envelope protein-mediated fusion and its neutralization.Journal of virology · 2006Article
- Antibody binding is a dominant determinant of the efficiency of human immunodeficiency virus type 1 neutralization.Journal of virology · 2006Article
- Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1.Journal of virology · 2005Article
- Stoichiometry of antibody neutralization of human immunodeficiency virus type 1.Journal of virology · 2005Article
- Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1.Journal of virology · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order to study the stoichiometry of monoclonal antibody (MAb) neutralization of T-cell line-adapted human immunodeficiency virus type 1 (HIV-1) in antibody excess and under equilibrium conditions, we exploited the ability of HIV-1 to generate mixed oligomers when different env genes are coexpressed. By the coexpression of Env glycoproteins that either can or cannot bind a neutralizing MAb in an env transcomplementation assay, virions were generated in which the proportion of MAb binding sites could be regulated. As the proportion of MAb binding sites in Env chimeric virus increased, MAb neutralization gradually increased. Virus neutralization by virion aggregation was minimal, as MAb binding to HIV-1 Env did not interfere with an AMLV Env-mediated infection by HIV-1(AMLV/HIV-1) pseudotypes of CD4(-) HEK293 cells. MAb neutralization of chimeric virions could be described as a third-order function of the proportion of Env antigen refractory to MAb binding. This scenario is consistent with the Env oligomer constituting the minimal functional unit and neutralization occurring incrementally as each Env oligomer binds MAb. Alternatively, the data could be fit to a sigmoid function. Thus, these data could not exclude the existence of a threshold for neutralization. However, results from MAb neutralization of chimeric virus containing wild-type Env and Env defective in CD4 binding was readily explained by a model of incremental MAb neutralization. In summary, the data indicate that MAb neutralization of T-cell line-adapted HIV-1 is incremental rather than all or none and that each MAb binding an Env oligomer reduces the likelihood of infection.
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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.