Evidence map›Paper›PMID 28035012›Full record

ArticleProtein engineering, design & selection : PEDS2017

Deep sequencing of phage-displayed peptide libraries reveals sequence motif that detects norovirus.

Amy M Hurwitz, Wanzhi Huang, Mary K Estes, Robert L Atmar, Timothy Palzkill

Open access · bronzeAbstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-weighted citation impact, top 30% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

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  5. ACS central science · 2021
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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

5 authors at 1 institution in 1 country.

Amy M HurwitzInterdepartmental Program in Translational Biology & Molecular Medicine, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Wanzhi HuangDepartment of Pharmacology, Baylor College of Medicine, Houston, TX, USA.
Mary K EstesDepartment of Molecular Virology & Microbiology, Baylor College of Medicine, Houston, TX, USA.
Robert L AtmarDepartment of Molecular Virology & Microbiology, Baylor College of Medicine, Houston, TX, USA.
Timothy PalzkillDepartment of Pharmacology, Baylor College of Medicine, Houston, TX, USA timothyp@bcm.edu.
Baylor College of Medicine · US

Funding

X-ray Crystallographic Studies on CalicivirusesP01AI057788 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI ATMAR, ROBERT L., ESTES, MARY KOLB · 2004 to 2024
$34.4M
Training Program in Translational Biology and Molecular MedicineT32GM088129 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI ROONEY, CLIONA M., VAN DEN VEYVER, IGNATIA B · 2010 to 2019
$3.0M
NIAID NIH HHS P01 AI057788NIGMS NIH HHS T32 GM088129
6 · The paper itself

Abstract

Norovirus infections are the leading cause of non-bacterial gastroenteritis and result in about 21 million new cases and $2 billion in costs per year in the United States. Existing diagnostics have limited feasibility for point-of-care applications, so there is a clear need for more reliable, rapid, and simple-to-use diagnostic tools in order to contain outbreaks and prevent inappropriate treatments. In this study, a combination of phage display technology, deep sequencing and computational analysis was used to identify 12-mer peptides with specific binding to norovirus genotype GI.1 virus-like particles (VLPs). After biopanning, phage populations were sequenced and analyzed to identify a consensus peptide motif-YRSWXP. Two 12-mer peptides containing this sequence, NV-O-R5-3 and NV-O-R5-6, were further characterized to evaluate the motif's functional ability to detect VLPs and virus. Results indicated that these peptides effectively detect GI.1 VLPs in solid-phase peptide arrays, ELISAs and dot blots. Further, their specificity for the S-domain of the major capsid protein enables them to detect a wide range of GI and GII norovirus genotypes. Both peptides were able to detect virus in norovirus-positive clinical stool samples. Overall, the work reported here demonstrates the application of phage display coupled with next generation sequencing and computational analysis to uncover peptides with specific binding ability to a target protein for diagnostic applications. Further, the reagents characterized here can be integrated into existing diagnostic formats to detect clinically relevant genotypes of norovirus in stool.

Indexed as

High-Throughput Nucleotide SequencingNucleotide MotifsPeptide LibrarySequence Analysis, DNAAmino Acid SequenceDNA, ViralGenotypeNorovirusOligopeptidesSubstrate SpecificityVirionDNA, ViralOligopeptidesPeptide Librarydiagnosticsinformaticsnoroviruspeptidephage display

Identifiers

PMID28035012
PMCPMC5241761
OpenAlexW2565599656

What OpenQuestion holds

Textmetadata
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.