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  • The text references a correction to a previously published research article identified by its DOI: 10.1371/journal.ppat.1009101.
  • It implies there were errors or updates that needed to be addressed in the original article.
  • The correction may affect the findings or interpretations presented in the original publication.

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[This corrects the article DOI: 10.1371/journal.ppat.1009101.].

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7924741PMC
http://dx.doi.org/10.1371/journal.ppat.1009386DOI Listing

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Article Synopsis
  • The text references a correction to a previously published research article identified by its DOI: 10.1371/journal.ppat.1009101.
  • It implies there were errors or updates that needed to be addressed in the original article.
  • The correction may affect the findings or interpretations presented in the original publication.
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Fragments of the V1/V2 domain of HIV-1 glycoprotein 120 engineered for improved binding to the broadly neutralizing PG9 antibody.

Mol Immunol

September 2016

Department of Biomolecular Engineering, Baskin School of Engineering, University of California, 1156 High Street, MS-SOE2, Santa Cruz, CA 95064, United States. Electronic address:

The V1/V2 domain of the HIV-1 envelope protein gp120 possesses two important epitopes: a glycan-dependent epitope recognized by the prototypic broadly neutralizing monoclonal antibody (bN-mAb), PG9, as well as an epitope recognized by non-neutralizing antibodies that has been associated with protection from HIV infection in the RV144 HIV vaccine trial. Because both of these epitopes are poorly immunogenic in the context of full length envelope proteins, immunization with properly folded and glycosylated fragments (scaffolds) represents a potential way to enhance the immune response to these specific epitopes. Previous studies showed that V1/V2 domain scaffolds could be produced from a few selected isolates, but not from many of the isolates that would be advantageous in a multivalent vaccine.

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The RV144 clinical trial showed the partial efficacy of a vaccine regimen with an estimated vaccine efficacy (VE) of 31% for protecting low-risk Thai volunteers against acquisition of HIV-1. The impact of vaccine-induced immune responses can be investigated through sieve analysis of HIV-1 breakthrough infections (infected vaccine and placebo recipients). A V1/V2-targeted comparison of the genomes of HIV-1 breakthrough viruses identified two V2 amino acid sites that differed between the vaccine and placebo groups.

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Lessons learned from HIV-1 vaccine trials: new priorities and directions.

Nat Immunol

April 2012

Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, University of Oxford, Oxford, UK.

A vaccine against human immunodeficiency virus (HIV) seems to be on the horizon. Correlates of risk of infection for [corrected] the RV144 vaccine trial have been found. There is understanding of what makes HIV envelope-specific antibodies broadly neutralizing and new T cell vaccine approaches can overcome virus variability.

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