Evidence map›Paper›PMID 25046154›Full record

ArticleVirology2014

Eliciting neutralizing antibodies with gp120 outer domain constructs based on M-group consensus sequence.

Yali Qin, Marisa Banasik, SoonJeung Kim, Adam Penn-Nicholson, Habtom H Habte, Celia LaBranche, David C Montefiori, Chong Wang, Michael W Cho

Abstract read
In one paragraph

Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
  2. HIV-1 prehairpin intermediate inhibitors show efficacy independent of neutralization tier.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

9 authors.

Yali QinDepartment of Biomedical Sciences, Iowa State University, Ames, IA 50011, United States; Center for Advanced Host Defenses, Immunobiotics and Translational Comparative Medicine, Iowa State University, Ames, IA 50011, United States.
Marisa BanasikDepartment of Biomedical Sciences, Iowa State University, Ames, IA 50011, United States; Center for Advanced Host Defenses, Immunobiotics and Translational Comparative Medicine, Iowa State University, Ames, IA 50011, United States.
SoonJeung KimCase Western Reserve University, Department of Physiology and Biophysics, School of Medicine, Cleveland, Ohio 44106, United States.
Adam Penn-NicholsonSouth African Tuberculosis Vaccine Initiative, Institute of Infectious Disease & Molecular Medicine and School of Child and Adolescent Health, University of Cape Town, Cape Town, South Africa.
Habtom H HabteDepartment of Biomedical Sciences, Iowa State University, Ames, IA 50011, United States; Center for Advanced Host Defenses, Immunobiotics and Translational Comparative Medicine, Iowa State University, Ames, IA 50011, United States.
Celia LaBrancheDepartment of Surgery, Duke University, Durham, NC 27710, United States.
David C MontefioriDepartment of Surgery, Duke University, Durham, NC 27710, United States.
Chong WangDepartment of Statistics, Iowa State University, Ames, IA 50011, United States; Veterinary Diagnostic and Production Animal Medicine, Iowa State University, Ames, IA 50011, United States.
Michael W ChoDepartment of Biomedical Sciences, Iowa State University, Ames, IA 50011, United States; Center for Advanced Host Defenses, Immunobiotics and Translational Comparative Medicine, Iowa State University, Ames, IA 50011, United States. Electronic address: mcho@iastate.edu.

Funding

Structural Evaluation of HIV-1 Envelope GycoproteinP01AI074286 · NIAID · IOWA STATE UNIVERSITY · PI SHI, WUXIAN · 2008 to 2012
$5.0M
NIAID NIH HHS AI074286NIAID NIH HHS HHSN272201100016CNIAID NIH HHS P01 AI074286PHS HHS HHSN27201100016C
6 · The paper itself

Abstract

One strategy being evaluated for HIV-1 vaccine development is focusing immune responses towards neutralizing epitopes on the gp120 outer domain (OD) by removing the immunodominant, but non-neutralizing, inner domain. Previous OD constructs have not elicited strong neutralizing antibodies (nAbs). We constructed two immunogens, a monomeric gp120-OD and a trimeric gp120-OD×3, based on an M group consensus sequence (MCON6). Their biochemical and immunological properties were compared with intact gp120. Results indicated better preservation of critical neutralizing epitopes on gp120-OD×3. In contrast to previous studies, our immunogens induced potent, cross-reactive nAbs in rabbits. Although nAbs primarily targeted Tier 1 viruses, they exhibited significant breadth. Epitope mapping analyses indicated that nAbs primarily targeted conserved V3 loop elements. Although the potency and breadth of nAbs were similar for all three immunogens, nAb induction kinetics indicated that gp120-OD×3 was superior to gp120-OD, suggesting that gp120-OD×3 is a promising prototype for further gp120 OD-based immunogen development.

Indexed as

Consensus SequenceAnimalsAntibodies, NeutralizingEpitope MappingEpitopesFemaleHIV-1HIV AntibodiesHIV Envelope Protein gp120RabbitsAntibodies, NeutralizingEpitopesgp120 protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp120gp120HIV-1Neutralizing antibodyOuter domainV3Vaccine

Identifiers

PMID25046154
PMCPMC4125429

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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.