Evidence map›Paper›PMID 25482819›Full record

ArticleVirology2015

Escherichia coli surface display of single-chain antibody VRC01 against HIV-1 infection.

Lin-Xu Wang, Michael Mellon, Dane Bowder, Meghan Quinn, Danielle Shea, Charles Wood, Shi-Hua Xiang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
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

7 authors.

Lin-Xu WangNebraska Center for Virology, Lincoln, NE, USA; School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68583, USA.
Michael MellonNebraska Center for Virology, Lincoln, NE, USA; School of Veterinary Medicine and Biomedical Sciences, Lincoln, NE, USA.
Dane BowderNebraska Center for Virology, Lincoln, NE, USA; School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68583, USA.
Meghan QuinnNebraska Center for Virology, Lincoln, NE, USA; School of Veterinary Medicine and Biomedical Sciences, Lincoln, NE, USA.
Danielle SheaNebraska Center for Virology, Lincoln, NE, USA; School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68583, USA.
Charles WoodNebraska Center for Virology, Lincoln, NE, USA; School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68583, USA.
Shi-Hua XiangNebraska Center for Virology, Lincoln, NE, USA; School of Veterinary Medicine and Biomedical Sciences, Lincoln, NE, USA. Electronic address: sxiang2@unl.edu.

Funding

Supplement: Fogarty Training in HIV- and AIDS Associated Diseases/MalignanciesD43TW001429 · FIC · UNIVERSITY OF NEBRASKA LINCOLN · PI WOOD, CHARLES · 2000 to 2015
$7.2M
Nebraska Center for VirologyP30GM103509 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI WOOD, CHARLES · 2012 to 2014
$3.3M
Research Training in Comparative Viral PathogenesisT32AI060547 · NIAID · UNIVERSITY OF NEBRASKA LINCOLN · PI WOOD, CHARLES · 2004 to 2013
$2.5M
FIC NIH HHS D43 TW001429FIC NIH HHS D43TW01492NIAID NIH HHS T32 AI060547NIAID NIH HHS T32AI060547NIGMS NIH HHS GM103509NIGMS NIH HHS P30 GM103509
6 · The paper itself

Abstract

Human immunodeficiency virus type 1 (HIV-1) transmission and infection occur mainly via the mucosal surfaces. The commensal bacteria residing in these surfaces can potentially be employed as a vehicle for delivering inhibitors to prevent HIV-1 infection. In this study, we have employed a bacteria-based strategy to display a broadly neutralizing antibody VRC01, which could potentially be used to prevent HIV-1 infection. The VRC01 antibody mimics CD4-binding to gp120 and has broadly neutralization activities against HIV-1. We have designed a construct that can express the fusion peptide of the scFv-VRC01 antibody together with the autotransporter β-barrel domain of IgAP gene from Neisseria gonorrhoeae, which enabled surface display of the antibody molecule. Our results indicate that the scFv-VRC01 antibody molecule was displayed on the surface of the bacteria as demonstrated by flow cytometry and immunofluorescence microscopy. The engineered bacteria can capture HIV-1 particles via surface-binding and inhibit HIV-1 infection in cell culture.

Indexed as

Antibodies, MonoclonalAntibodies, NeutralizingBinding SitesBroadly Neutralizing AntibodiesCD4 AntigensEscherichia coliHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV InfectionsHumansModels, MolecularNeisseria gonorrhoeaeProtein ConformationRecombinant Fusion ProteinsSerine EndopeptidasesAntibodies, MonoclonalAntibodies, NeutralizingBroadly Neutralizing AntibodiesCD4 Antigensgp120 protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp120IgA-specific serine endopeptidaseRecombinant Fusion ProteinsSerine EndopeptidasesSingle-Chain AntibodiesVRC01 monoclonal antibodyAutotransporterE. coli K12 UT5600HIV-1scFv-VRC01Surface displayβ-Barrel domain

Identifiers

PMID25482819
PMCPMC4337897

What OpenQuestion holds

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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.