Evidence map›Paper›PMID 27966523›Full record

ArticleNature communications2016

Functional screening for anti-CMV biologics identifies a broadly neutralizing epitope of an essential envelope protein.

Thomas J Gardner, Kathryn R Stein, J Andrew Duty, Toni M Schwarz, Vanessa M Noriega, Thomas Kraus, Thomas M Moran, Domenico Tortorella

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

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  18. Zika Virus Specific Diagnostic Epitope Discovery.Journal of visualized experiments : JoVE · 2017
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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

8 authors at 1 institution in 1 country.

Thomas J GardnerDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.
Kathryn R SteinDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.
J Andrew DutyDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.
Toni M SchwarzDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.
Vanessa M NoriegaDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.
Thomas KrausCenter for Therapeutic Antibody Development, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.
Thomas M MoranDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.
Domenico TortorellaDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.
Icahn School of Medicine at Mount Sinai · US

Funding

TRAINING PROGRAM: MECHANISMS OF VIRUS-HOST INTERACTIONST32AI007647 · NIAID · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI Domenico Tortorella · 2000 to 2026
$11.5M
Assay development to discover therapeutics against human cytomegalovirusR01AI101820 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI TORTORELLA, DOMENICO · 2013 to 2015
$962k
Functional screening for neutralizing antibodies targeting CMV entry factorsR21AI112318 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI TORTORELLA, DOMENICO · 2014 to 2015
$466k
NIAID NIH HHS R01 AI101820NIAID NIH HHS R21 AI112318NIAID NIH HHS T32 AI007647
6 · The paper itself

Abstract

The prototypic β-herpesvirus human cytomegalovirus (CMV) establishes life-long persistence within its human host. The CMV envelope consists of various protein complexes that enable wide viral tropism. More specifically, the glycoprotein complex gH/gL/gO (gH-trimer) is required for infection of all cell types, while the gH/gL/UL128/130/131a (gH-pentamer) complex imparts specificity in infecting epithelial, endothelial and myeloid cells. Here we utilize state-of-the-art robotics and a high-throughput neutralization assay to screen and identify monoclonal antibodies (mAbs) targeting the gH glycoproteins that display broad-spectrum properties to inhibit virus infection and dissemination. Subsequent biochemical characterization reveals that the mAbs bind to gH-trimer and gH-pentamer complexes and identify the antibodies' epitope as an 'antigenic hot spot' critical for virus entry. The mAbs inhibit CMV infection at a post-attachment step by interacting with a highly conserved central alpha helix-rich domain. The platform described here provides the framework for development of effective CMV biologics and vaccine design strategies.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, NeutralizingCell LineCytomegalovirusCytomegalovirus InfectionsHumansMiceViral Envelope ProteinsViral VaccinesVirus InternalizationAntibodies, MonoclonalAntibodies, Neutralizingglycoprotein H, CytomegalovirusViral Envelope ProteinsViral Vaccines

Identifiers

PMID27966523
PMCPMC5171902
OpenAlexW2561022569

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.