Evidence map›Paper›PMID 23671563›Full record

ArticlePloS one2013

Human rotavirus VP6-specific antibodies mediate intracellular neutralization by binding to a quaternary structure in the transcriptional pore.

Mohammed S Aiyegbo, Gopal Sapparapu, Benjamin W Spiller, Ilyas M Eli, Dewight R Williams, Robert Kim, David E Lee, Tong Liu, Sheng Li, Virgil L Woods and 4 more

Abstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

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  18. Review
  19. Structural basis for norovirus neutralization by an HBGA blocking human IgA antibody.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. Characterization of a genetically heterogeneous porcine rotavirus C, and other viruses present in the fecal virome of a non-diarrheic Belgian piglet.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2016
    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

14 authors.

Mohammed S AiyegboDepartment of Pathology, Microbiology and Immunology, Vanderbilt Medical Center, Nashville, Tennessee, USA.
Gopal Sapparapu
Benjamin W Spiller
Ilyas M Eli
Dewight R Williams
Robert Kim
David E Lee
Tong Liu
Sheng Li
Virgil L Woods
David P Nannemann
Jens Meiler
Phoebe L Stewart
James E Crowe

Funding

Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
Clonal Analysis of the Human B Cell Response to HIVU01AI078407 · NIAID · VANDERBILT UNIVERSITY · PI CROWE, JAMES E · 2008 to 2012
$3.9M
Epitope shifting and Antibody Maturation during Rotavirus InfectionR21AI092268 · NIAID · VANDERBILT UNIVERSITY · PI SPILLER, BENJAMIN W · 2011 to 2012
$429k
Rotavirus VP6 Specific Human IgA AntibodiesR21AI083574 · NIAID · VANDERBILT UNIVERSITY · PI CROWE, JAMES E · 2009 to 2010
$426k
NIAID NIH HHS R21 AI083574NIAID NIH HHS R21 AI092268NIAID NIH HHS U01 AI078407NIAID NIH HHS U01 AI078407-03S2NIDDK NIH HHS DK058404NIDDK NIH HHS P30 DK058404
6 · The paper itself

Abstract

Several live attenuated rotavirus (RV) vaccines have been licensed, but the mechanisms of protective immunity are still poorly understood. The most frequent human B cell response is directed to the internal protein VP6 on the surface of double-layered particles, which is normally exposed only in the intracellular environment. Here, we show that the canonical VP6 antibodies secreted by humans bind to such particles and inhibit viral transcription. Polymeric IgA RV antibodies mediated an inhibitory effect against virus replication inside cells during IgA transcytosis. We defined the recognition site on VP6 as a quaternary epitope containing a high density of charged residues. RV human mAbs appear to bind to a negatively-charged patch on the surface of the Type I channel in the transcriptionally active particle, and they sterically block the channel. This unique mucosal mechanism of viral neutralization, which is not apparent from conventional immunoassays, may contribute significantly to human immunity to RV.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalAntibodies, ViralAntigens, ViralB-LymphocytesCaco-2 CellsCapsid ProteinsCell LineEpitopesHEK293 CellsHost-Pathogen InteractionsHumansImmunoglobulin AModels, MolecularMolecular Sequence DataAntibodies, MonoclonalAntibodies, ViralAntigens, ViralCapsid ProteinsEpitopesImmunoglobulin AVP6 protein, Rotavirus

Identifiers

PMID23671563
PMCPMC3650007

What OpenQuestion holds

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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.