ArticleJournal of virology2010
Protease cleavage sites in HIV-1 gp120 recognized by antigen processing enzymes are conserved and located at receptor binding sites.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
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
21 citing papers in PubMed, 27 citations in OpenAlex.
- Analysis of HLA A*02 association with vaccine efficacy in the RV144 HIV-1 vaccine trial.Journal of virology · 2014Trial
- Article
- Mimicking SIV chimpanzee viral evolution toward HIV-1 during cross-species transmission.Journal of medical primatology · 2020Article
- Cross-Species Transmission and Evolution of SIV Chimpanzee Progenitor Viruses Toward HIV-1 in Humanized Mice.Frontiers in microbiology · 2020Article
- Identification and CRISPR/Cas9 Inactivation of the C1s Protease Responsible for Proteolysis of Recombinant Proteins Produced in CHO Cells.Biotechnology and bioengineering · 2019Article
- Unusual Cysteine Content in V1 Region of gp120 From an Elite Suppressor That Produces Broadly Neutralizing Antibodies.Frontiers in immunology · 2019Article
- CRISPR/Cas9 gene editing for the creation of an MGAT1-deficient CHO cell line to control HIV-1 vaccine glycosylation.PLoS biology · 2018Article
- cGMP production and analysis of BG505 SOSIP.664, an extensively glycosylated, trimeric HIV-1 envelope glycoprotein vaccine candidate.Biotechnology and bioengineering · 2018Article
- Effects of Cross-Presentation, Antigen Processing, and Peptide Binding in HIV Evasion of T Cell Immunity.Journal of immunology (Baltimore, Md. : 1950) · 2018Article
- Glycan modifications to the gp120 immunogens used in the RV144 vaccine trial improve binding to broadly neutralizing antibodies.PloS one · 2018Article
- Fragments of the V1/V2 domain of HIV-1 glycoprotein 120 engineered for improved binding to the broadly neutralizing PG9 antibody.Molecular immunology · 2016Article
- Article
- HIV-1 envelope proteins and V1/V2 domain scaffolds with mannose-5 to improve the magnitude and quality of protective antibody responses to HIV-1.The Journal of biological chemistry · 2014Article
- The Quest for an HIV-1 Vaccine Adjuvant: Bacterial Toxins as New Potential Platforms.Journal of clinical & cellular immunology · 2014Article
- Increased functional stability and homogeneity of viral envelope spikes through directed evolution.PLoS pathogens · 2013Article
- Stabilizing exposure of conserved epitopes by structure guided insertion of disulfide bond in HIV-1 envelope glycoprotein.PloS one · 2013Article
- Targeting a Neutralizing Epitope of HIV Envelope Gp120 by Immune Complex Vaccine.Journal of AIDS & clinical research · 2012Article
- Retrovirus entry by endocytosis and cathepsin proteases.Advances in virology · 2012Article
- Glycoform and net charge heterogeneity in gp120 immunogens used in HIV vaccine trials.PloS one · 2012Article
- HIV-1 envelope resistance to proteasomal cleavage: implications for vaccine induced immune responses.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The identification of vaccine immunogens able to elicit broadly neutralizing antibodies (bNAbs) is a major goal in HIV vaccine research. Although it has been possible to produce recombinant envelope glycoproteins able to adsorb bNAbs from HIV-positive sera, immunization with these proteins has failed to elicit antibody responses effective against clinical isolates of HIV-1. Thus, the epitopes recognized by bNAbs are present on recombinant proteins, but they are not immunogenic. These results led us to consider the possibility that changes in the pattern of antigen processing might alter the immune response to the envelope glycoprotein to better elicit protective immunity. In these studies, we have defined protease cleavage sites on HIV gp120 recognized by three major human proteases (cathepsins L, S, and D) important for antigen processing and presentation. Remarkably, six of the eight sites identified in gp120 were highly conserved and clustered in regions of the molecule associated with receptor binding and/or the binding of neutralizing antibodies. These results suggested that HIV may have evolved to take advantage of major histocompatibility complex (MHC) class II antigen processing enzymes in order to evade or direct the antiviral immune response.
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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.