Evidence map›Paper›PMID 36264000›Full record

ArticleACS applied bio materials2022

Kathryn A Hufziger, Emma L Farquharson, Brenda G Werner, Qingmin Chen, Julie M Goddard, Sam R Nugen

Open access · greenAbstract read
In one paragraph

Article in ACS applied bio materials, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 26% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Nanoparticle-based approaches for bacterial detection and therapy.Applied microbiology and biotechnology · 2026
    Review
  3. Bacteriophage-mediated approaches for biofilm control.Frontiers in cellular and infection microbiology · 2024
    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

6 authors at 1 institution in 1 country.

Kathryn A HufzigerDepartment of Food Science, Cornell University, Ithaca, New York 14853, United States.
Emma L FarquharsonDepartment of Food Science, Cornell University, Ithaca, New York 14853, United States.
Brenda G WernerDepartment of Food Science, Cornell University, Ithaca, New York 14853, United States.
Qingmin ChenDepartment of Food Science, Cornell University, Ithaca, New York 14853, United States.
Julie M GoddardDepartment of Food Science, Cornell University, Ithaca, New York 14853, United States.ORCID 0000-0002-3644-0732
Sam R NugenDepartment of Food Science, Cornell University, Ithaca, New York 14853, United States.ORCID 0000-0003-3638-1776
Cornell University · US

Funding

Accelerating phage evolution and tools via synthetic biology and machine learningR01EB027895 · NIBIB · CORNELL UNIVERSITY · PI NUGEN, SAM R · 2019 to 2024
$2.6M
NIBIB NIH HHS R01 EB027895
6 · The paper itself

Abstract

The current state-of-the-art in bacteriophage (phage) immobilization onto magnetic particles is limited to techniques that are less expensive and/or facile but nonspecific or those that are more expensive and/or complicated but ensure capsid-down orientation of the phages, as necessary to preserve infectivity and performance in subsequent applications (e.g., therapeutics, detection). These cost, complexity, and effectiveness limitations constitute the major hurdles that limit the scale-up of phage-based strategies and thus their accessibility in low-resource settings. Here, we report a plasmid-based technique that incorporates a silica-binding protein, L2, into the T7 phage capsid, during viral assembly, with and without inclusion of a flexible linker peptide, allowing for targeted binding of the phage capsid to silica without requiring the direct modification of the phage genome. L2-tagged phages were then immobilized onto silica-coated magnetic nanoparticles. Inclusion of the flexible linker between the phage capsid protein and the L2 protein improved immobilization density compared to both wild type T7 phages and L2-tagged phages without the flexible linker. Taken together, this work demonstrates phage capsid modification without engineering the phage genome, which provides an important step toward reducing the cost and increasing the specificity/directionality of phage immobilization methods and could be more broadly applied in the future for other phages for a range of other capsid tags and nanomaterials.

Indexed as

BacteriophagesCapsidCapsid ProteinsSilicon DioxideVirus AssemblyCapsid ProteinsSilicon Dioxidein vitro phage engineeringmagnetic nanoparticlesphage technologyplasmid-based capsid taggingsilica bindingT7tailed phages

Identifiers

PMID36264000
PMCPMC10184791
OpenAlexW4306874531

What OpenQuestion holds

Textmetadata
LicenceTDM
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.