Evidence map›Paper›PMID 28612603›Full record

ArticleBioconjugate chemistry2017

Sortase-Mediated Ligation as a Modular Approach for the Covalent Attachment of Proteins to the Exterior of the Bacteriophage P22 Virus-like Particle.

Dustin Patterson, Benjamin Schwarz, John Avera, Brian Western, Matthew Hicks, Paul Krugler, Matthew Terra, Masaki Uchida, Kimberly McCoy, Trevor Douglas

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioconjugate chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  3. Chemical reviews · 2026
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  10. Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 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

10 authors at 2 institutions in 1 country.

Dustin PattersonDepartment of Chemistry & Biochemistry, University of Texas at Tyler , Tyler, Texas 75799, United States.ORCID 0000-0001-5291-2966
Benjamin SchwarzDepartment of Chemistry, Indiana University , Bloomington, Indiana 47407, United States.
John AveraDepartment of Chemistry, Indiana University , Bloomington, Indiana 47407, United States.
Brian WesternDepartment of Chemistry & Biochemistry, University of Texas at Tyler , Tyler, Texas 75799, United States.
Matthew HicksDepartment of Chemistry & Biochemistry, University of Texas at Tyler , Tyler, Texas 75799, United States.
Paul KruglerDepartment of Chemistry & Biochemistry, University of Texas at Tyler , Tyler, Texas 75799, United States.
Matthew TerraDepartment of Chemistry & Biochemistry, University of Texas at Tyler , Tyler, Texas 75799, United States.
Masaki UchidaDepartment of Chemistry, Indiana University , Bloomington, Indiana 47407, United States.
Kimberly McCoyDepartment of Chemistry, Indiana University , Bloomington, Indiana 47407, United States.
Trevor DouglasDepartment of Chemistry, Indiana University , Bloomington, Indiana 47407, United States.
Indiana University Bloomington · USThe University of Texas at Tyler · US

Funding

Engineered virus-like nanoparticles targeting immunity needed for pan flu vaccineR01AI104905 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI DOUGLAS, TREVOR, JUTILA, MARK A · 2013 to 2017
$2.3M
NIAID NIH HHS R01 AI104905
6 · The paper itself

Abstract

Virus-like particles are unique platforms well suited for the construction of nanomaterials with broad-range applications. The research presented here describes the development of a modular approach for the covalent attachment of protein domains to the exterior of the versatile bacteriophage P22 virus-like particle (VLP) via a sortase-mediated ligation strategy. The bacteriophage P22 coat protein was genetically engineered to incorporate an LPETG amino acid sequence on the C-terminus, providing the peptide recognition sequence utilized by the sortase enzyme to catalyze peptide bond formation between the LPETG-tagged protein and a protein containing a polyglycine sequence on the N-terminus. Here we evaluate attachment of green fluorescent protein (GFP) and the head domain of the influenza hemagglutinin (HA) protein by genetically producing polyglycine tagged proteins. Attachment of both proteins to the exterior of the P22 VLP was found to be highly efficient as judged by SDS-PAGE densitometry. These results enlarge the tool kit for modifying the P22 VLP system and provide new insights for other VLPs that have an externally displayed C-terminus that can use the described strategy for the modular modification of their external surface for various applications.

Indexed as

Bacteriophage P22Capsid ProteinsCysteine EndopeptidasesGreen Fluorescent ProteinsHemagglutinins, ViralModels, MolecularProtein DomainsCapsid ProteinsCysteine EndopeptidasesGreen Fluorescent ProteinsHemagglutinins, Viral

Identifiers

PMID28612603
PMCPMC6708598
OpenAlexW2626547112

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.