Evidence map›Paper›PMID 22759232›Full record

ArticleBioconjugate chemistry2012

M13 bacteriophage display framework that allows sortase-mediated modification of surface-accessible phage proteins.

Gaelen T Hess, Juan J Cragnolini, Maximilian W Popp, Mark A Allen, Stephanie K Dougan, Eric Spooner, Hidde L Ploegh, Angela M Belcher, Carla P Guimaraes

Abstract read
In one paragraph

Article in Bioconjugate chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

47 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. Chemical reviews · 2026
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  10. Preparation of Bioconjugates of Chimeric M13 Phage and Gold Nanorods.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
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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

9 authors at 3 institutions in 1 country.

Gaelen T HessThe David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Juan J Cragnolini
Maximilian W Popp
Mark A Allen
Stephanie K Dougan
Eric Spooner
Hidde L Ploegh
Angela M Belcher
Carla P Guimaraes
Whitehead Institute for Biomedical Research · USMassachusetts Institute of Technology · USHarvard University · US

Funding

Sortase-mediated protein engineering for the study of host-pathogen interactionsR01AI087879 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 2010 to 2019
$4.5M
NIAID NIH HHS R01 AI087879
6 · The paper itself

Abstract

We exploit bacterial sortases to attach a variety of moieties to the capsid proteins of M13 bacteriophage. We show that pIII, pIX, and pVIII can be functionalized with entities ranging from small molecules (e.g., fluorophores, biotin) to correctly folded proteins (e.g., GFP, antibodies, streptavidin) in a site-specific manner, and with yields that surpass those of any reported using phage display technology. A case in point is modification of pVIII. While a phage vector limits the size of the insert into pVIII to a few amino acids, a phagemid system limits the number of copies actually displayed at the surface of M13. Using sortase-based reactions, a 100-fold increase in the efficiency of display of GFP onto pVIII is achieved. Taking advantage of orthogonal sortases, we can simultaneously target two distinct capsid proteins in the same phage particle and maintain excellent specificity of labeling. As demonstrated in this work, this is a simple and effective method for creating a variety of structures, thus expanding the use of M13 for materials science applications and as a biological tool.

Indexed as

AminoacyltransferasesAnimalsBacterial ProteinsBacteriophage M13Capsid ProteinsCell Surface Display TechniquesCysteine EndopeptidasesMiceMice, Inbred C57BLSurface PropertiesAminoacyltransferasesBacterial ProteinsCapsid ProteinsCysteine Endopeptidasessortase A

Identifiers

PMID22759232
PMCPMC3564602
OpenAlexW2305040510

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.