ArticleActa naturae
Broadly Neutralizing Antibodies against HIV-1 As a Novel Aspect of the Immune Response.
Article in Acta naturae. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
15 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Employing Broadly Neutralizing Antibodies as a Human Immunodeficiency Virus Prophylactic & Therapeutic Application.Frontiers in immunology · 2021Pooled it
- Broad and potent cross clade neutralizing antibodies with multiple specificities in the plasma of HIV-1 subtype C infected individuals.Scientific reports · 2017Trial
- HIV envelope pseudotyped virus- an indispensable tool in HIV research.Virus research · 2026Review
- Rapid identification of antigen-specific monoclonal antibodies from HIV-1 elite controllers using the Beacon platform.AIDS research and therapy · 2026Article
- Treatment of Ebola Virus Disease: From Serotherapy to the Use of Monoclonal Antibodies.Antibodies (Basel, Switzerland) · 2025Review
- Signal peptide exchange alters HIV-1 envelope antigenicity and immunogenicity.Frontiers in immunology · 2024Article
- Review
- Therapeutic potential of HIV-1 entry inhibitor peptidomimetics.Experimental biology and medicine (Maywood, N.J.) · 2021Review
- AAV Vectored Immunoprophylaxis for Filovirus Infections.Tropical medicine and infectious disease · 2020Review
- Mapping of Neutralizing Antibody Epitopes on the Envelope of Viruses Obtained from Plasma Samples Exhibiting Broad Cross-Clade Neutralization Potential Against HIV-1.AIDS research and human retroviruses · 2019Article
- Evolution of Neutralization Response in HIV-1 Subtype C-Infected Individuals Exhibiting Broad Cross-Clade Neutralization of HIV-1 Strains.Frontiers in immunology · 2018Article
- Antibody-Mediated Therapy against HIV/AIDS: Where Are We Standing Now?Journal of pathogens · 2018Review
- Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity.The Journal of biological chemistry · 2017Article
- Promise and problems associated with the use of recombinant AAV for the delivery of anti-HIV antibodies.Molecular therapy. Methods & clinical development · 2016Review
- The Structural and Immunological Properties of Chimeric Proteins Containing HIV-1 MPER Sites.Acta naturaeArticle
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human immunodeficiency virus-1 (HIV-1) has the ability to evade the adaptive immune response due to high mutation rates. Soon after the discovery of HIV-1, it was originally proposed that neutralizing of antibodies to the virus occurs rarely or cannot be elicited at all. In the 1990s, there appeared reports that sera of select HIV-1-infected individuals contained antibodies capable of neutralizing different virus subtypes. Such antibodies were named broadly neutralizing antibodies (bNAbs). Since 2009, the development of new cell technologies has intensified research efforts directed at identifying new bNAbs with a neutralization potency of over 90% of primary HIV-1 isolates. These antibodies have unique characteristics which include high levels of somatic mutations and unusually long variable loops that penetrate through the glycan shield of HIV-1 Env to contact the protein surface. In this review, we will attempt to summarize the latest data on bNAbs against HIV-1 in terms of their interactions with the sites of vulnerability on HIV-1 glycoproteins.
Indexed as
Identifiers
26798488PMC4717246What OpenQuestion holds
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.