Evidence map›Paper›PMID 30220462›Full record

ArticleVaccine2018

Design, display and immunogenicity of HIV1 gp120 fragment immunogens on virus-like particles.

Mansi Purwar, Jonathan K Pokorski, Pranveer Singh, Sanchari Bhattacharyya, Heather Arendt, Joanne DeStefano, Celia C La Branche, David C Montefiori, M G Finn, Raghavan Varadarajan

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Vaccine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Advancements in protein nanoparticle vaccine platforms to combat infectious disease.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021
    Review
  2. 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

10 authors at 4 institutions in 2 countries.

Mansi PurwarMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
Jonathan K PokorskiDepartment of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Pranveer SinghMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
Sanchari BhattacharyyaMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
Heather ArendtInternational AIDS Vaccine Initiative, Brooklyn, NY 11226, USA.
Joanne DeStefanoInternational AIDS Vaccine Initiative, Brooklyn, NY 11226, USA.
Celia C La BrancheDepartment of Surgery, Duke University Medical Center, Durham, NC, USA.
David C MontefioriDepartment of Surgery, Duke University Medical Center, Durham, NC, USA.
M G FinnDepartment of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA. Electronic address: mgfinn@gatech.edu.
Raghavan VaradarajanMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India. Electronic address: varadar@mbu.iisc.ernet.in.
Indian Institute of Science Bangalore · INDuke Medical Center · USInternational AIDS Vaccine Initiative · USScripps Research Institute · US

Funding

Genetic and Chemically Programmed Nanoparticles for Prodrug TherapyR01GM101421 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI FINN, M.G. · 2013 to 2016
$1.1M
HIV-1 envelope structure, stability and dynamics probed by saturation mutagenesisR01AI118366 · NIAID · INDIAN INSTITUTE OF SCIENCE · PI VARADARAJAN, RAGHAVAN · 2015 to 2019
$607k
NIAID NIH HHS R01 AI118366NIGMS NIH HHS R01 GM101421
6 · The paper itself

Abstract

The broadly neutralizing antibody against HIV-1, b12, binds to the CD4 binding site (CD4bs) on the outer domain (OD) of the gp120 subunit of HIV-1 Env. We have previously reported the design of an E. coli expressed fragment of HIV-1 gp120, b122a, containing about 70% of the b12 epitope with the idea of focusing the immune response to this structure. Since the b122a structure was found to be only partially folded, as assessed by circular dichroism and protease resistance, we attempted to stabilize it by the introduction of additional disulfide bonds. One such mutant, b122a1-b showed increased stability and bound b12 with 30-fold greater affinity as compared to b122a. Various b122a and OD fragment proteins were displayed on the surface of Qβ virus-like particles. Sera raised against these particles in six-month long rabbit immunization studies could neutralize Tier1 viruses across different subtypes with the best results observed with b122a1-b displayed particles. Significantly higher amounts of antibodies directed towards the CD4bs were also elicited by particles displaying b122a1-b. This study highlights the ability of fragment immunogens to focus the antibody response to the conserved CD4bs of HIV-1.

Indexed as

AnimalsAntibodies, NeutralizingBinding SitesCD4 AntigensEscherichia coliHIV Envelope Protein gp120NanoparticlesProtein StabilityRabbitsSurface Plasmon ResonanceAntibodies, NeutralizingCD4 AntigensHIV Envelope Protein gp120Immune focusingNanoparticlesNeutralizing antibodiesProtein stabilityVaccine

Identifiers

PMID30220462
PMCPMC6364316
OpenAlexW2889598943

What OpenQuestion holds

Textmetadata
LicenceTDM
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.