Evidence map›Paper›PMID 24920809›Full record

ArticleJournal of virology2014

Vaccine-induced HIV-1 envelope gp120 constant region 1-specific antibodies expose a CD4-inducible epitope and block the interaction of HIV-1 gp140 with galactosylceramide.

S Moses Dennison, Kara M Anasti, Frederick H Jaeger, Shelley M Stewart, Justin Pollara, Pinghuang Liu, Erika L Kunz, Ruijun Zhang, Nathan Vandergrift, Sallie Permar and 12 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 33% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Trial
  2. Review
  3. Ceramide and Related Molecules in Viral Infections.International journal of molecular sciences · 2021
    Review
  4. Article
  5. Maspin binds to cardiolipin in mitochondria and triggers apoptosis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

22 authors at 5 institutions in 2 countries.

S Moses DennisonDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA.
Kara M AnastiDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA.
Frederick H JaegerDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA.
Shelley M StewartDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA.
Justin PollaraDepartment of Surgery, Duke University School of Medicine, Durham, North Carolina, USA.
Pinghuang LiuDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA.
Erika L KunzDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA.
Ruijun ZhangDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA.
Nathan VandergriftDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA.
Sallie PermarDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA Department of Immunology, Duke University School of Medicine, Durham, North Carolina, USA Department of Pediatrics, Duke University School of Medicine, Durham, North Carolina, USA Department of Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, North Carolina, USA.
Guido FerrariDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA Department of Surgery, Duke University School of Medicine, Durham, North Carolina, USA.
Georgia D TomarasDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA Department of Immunology, Duke University School of Medicine, Durham, North Carolina, USA Department of Surgery, Duke University School of Medicine, Durham, North Carolina, USA Department of Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, North Carolina, USA.
Mattia BonsignoriDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA Department of Medicine, Duke University School of Medicine, Durham, North Carolina, USA.
Nelson L MichaelU.S. Military HIV Research Program, Walter Reed Army Institute of Research, Silver Spring, Maryland, USA.
Jerome H KimU.S. Military HIV Research Program, Walter Reed Army Institute of Research, Silver Spring, Maryland, USA.
Jaranit KaewkungwalTropical Hygiene, Mahidol University, Bangkok, Thailand.
Sorachai NitayaphanArmed Forces Research Institute of Medical Sciences, Bangkok, Thailand.
Punnee PitisuttithumClinical Tropical Medicine, Mahidol University, Bangkok, Thailand.
Supachai Rerks-NgarmDepartment of Disease Control, Ministry of Public Health, Nonthaburi, Thailand.
Hua-Xin LiaoDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA Department of Medicine, Duke University School of Medicine, Durham, North Carolina, USA.
Barton F HaynesDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA Department of Medicine, Duke University School of Medicine, Durham, North Carolina, USA Department of Immunology, Duke University School of Medicine, Durham, North Carolina, USA alam0004@mc.duke.edu hayne002@mc.duke.edu.
S Munir AlamDuke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, USA Department of Medicine, Duke University School of Medicine, Durham, North Carolina, USA Department of Pathology, Duke University School of Medicine, Durham, North Carolina, USA alam0004@mc.duke.edu hayne002@mc.duke.edu.
Duke University · USMahidol University · THWalter Reed Army Institute of Research · USArmed Forces Research Institute of Medical Science · THMinistry of Public Health · TH

Funding

Viral Sequencing CoreU19AI067854 · NIAID · DUKE UNIVERSITY · PI LETVIN, NORMAN L · 2006 to 2011
$290.5M
Virus biology scientific research support componentUM1AI100645 · NIAID · DUKE UNIVERSITY · PI MCMICHAEL, ANDREW JAMES · 2012 to 2018
$204.7M
Viral and Host Determinants of HIV-1 TransmissionU01AI067854 · NIAID · DUKE UNIVERSITY · PI HAYNES, BARTON F · 2005 to 2005
$14.9M
NIAID NIH HHS U01 AI067854NIAID NIH HHS U19 AI067854NIAID NIH HHS UM1 AI100645NIAID NIH HHS UM1AI100645-01
6 · The paper itself

Abstract

unlabelledMucosal epithelial cell surface galactosylceramide (Galcer) has been postulated to be a receptor for HIV-1 envelope (Env) interactions with mucosal epithelial cells. Disruption of the HIV-1 Env interaction with such alternate receptors could be one strategy to prevent HIV-1 entry through the mucosal barrier. To study antibody modulation of HIV-1 Env-Galcer interactions, we used Galcer-containing liposomes to assess whether natural- and vaccine-induced monoclonal antibodies can block HIV-1 Env binding to Galcer. HIV-1 Env gp140 proteins bound to Galcer liposomes with Kds (dissociation constants) in the nanomolar range. Several HIV-1 ALVAC/AIDSVAX vaccinee-derived monoclonal antibodies (MAbs) specific for the gp120 first constant (C1) region blocked Galcer binding of a transmitted/founder HIV-1 Env gp140. Among the C1-specific MAbs that showed Galcer blocking, the antibody-dependent cellular cytotoxicity-mediating CH38 IgG and its natural IgA isotype were the most potent blocking antibodies. C1-specific IgG monoclonal antibodies that blocked Env binding to Galcer induced upregulation of the gp120 CD4-inducible (CD4i) epitope bound by MAb 17B, demonstrating that a conformational change in gp120 may be required for Galcer blocking. However, the MAb 17B itself did not block Env-Galcer binding, suggesting that the C1 antibody-induced gp120 conformational changes resulted in alteration in a Galcer binding site distant from the CD4i 17B MAb binding site. IMPORTANCE: Galactosyl ceramide, a glycosphingolipid, has been postulated to be a receptor for the HIV-1 envelope glycoprotein (Env) interaction with mucosal epithelial cells. Here, we have mimicked this interaction by using an artificial membrane containing synthetic Galcer and recombinant HIV-1 Env proteins to identify antibodies that would block the HIV-1 Env-Galcer interaction. Our study revealed that a class of vaccine-induced human antibodies potently blocks HIV-1 Env-Galcer binding by perturbing the HIV-1 Env conformation.

Indexed as

AIDS VaccinesAntibodies, MonoclonalAntibody-Dependent Cell CytotoxicityBinding SitesCD4 Antigensenv Gene Products, Human Immunodeficiency VirusEpitopesGalactosylceramidesHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansImmunoglobulin GLiposomesProtein BindingAIDS VaccinesAIDSVAXAntibodies, MonoclonalCD4 Antigensenv Gene Products, Human Immunodeficiency VirusEpitopesGalactosylceramidesgp140 envelope protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp120Immunoglobulin GLiposomes

Identifiers

PMID24920809
PMCPMC4136246
OpenAlexW2137619501

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.