ArticleAIDS research and human retroviruses2015
Short Communication: Virion Aggregation by Neutralizing and Nonneutralizing Antibodies to the HIV-1 Envelope Glycoprotein.
Article in AIDS research and human retroviruses, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Engineering a Coiled-Coil Protein for DARPin Presentation as a Potent SARS-CoV-2 Therapeutic.Biomacromolecules · 2025Article
- Glycan heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.PLoS pathogens · 2023Article
- Vaccine-induced V1V2-specific antibodies control and or protect against infection with HIV, SIV and SHIV.Current opinion in HIV and AIDS · 2019Review
- Update on Fc-Mediated Antibody Functions Against HIV-1 Beyond Neutralization.Frontiers in immunology · 2019Review
- Antibody responses to the HIV-1 envelope high mannose patch.Advances in immunology · 2019Review
- A rapid ultrasound particle agglutination method for HIV antibody detection: Comparison with conventional rapid HIV tests.Journal of virological methods · 2017Article
- Non-Neutralizing Antibodies Directed against HIV and Their Functions.Frontiers in immunology · 2017Review
- How to assess the binding strength of antibodies elicited by vaccination against HIV and other viruses.Expert review of vaccines · 2016Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
We used dynamic light scattering to detect aggregation of HIV-1 virions by antibodies (IgG) to the viral envelope glycoprotein (Env). Virions of different strains were inactivated by 2,2'-dithiodipyridine (AT-2), a procedure that abrogates infectivity but preserves the native antigenic structure of Env. Neutralizing antibodies directed to a V3-base- and glycan-dependent epitope on gp120 and to the apex of the Env trimer, as well as nonneutralizing antibodies to the epitope cluster I on the gp41-ectodomain, aggregated virions, but in markedly narrow concentration ranges. In contrast, the neutralizing antibody 2G12, which is specific for a composite glycan-dependent epitope on gp120 and functionally monovalent because of its unusual domain-swap structure, was nonaggregating. These results have potentially complex implications for vaccine development.
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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.