Evidence map›Paper›PMID 26734040›Full record

ArticleFrontiers in plant science2015

Modified TMV Particles as Beneficial Scaffolds to Present Sensor Enzymes.

Claudia Koch, Katrin Wabbel, Fabian J Eber, Peter Krolla-Sidenstein, Carlos Azucena, Hartmut Gliemann, Sabine Eiben, Fania Geiger, Christina Wege

Abstract read
In one paragraph

Article in Frontiers in plant science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

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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.

Claudia KochDepartment of Molecular Biology and Plant Virology, Institute of Biomaterials and Biomolecular Systems, University of Stuttgart Stuttgart, Germany.
Katrin WabbelDepartment of Molecular Biology and Plant Virology, Institute of Biomaterials and Biomolecular Systems, University of Stuttgart Stuttgart, Germany.
Fabian J EberDepartment of Molecular Biology and Plant Virology, Institute of Biomaterials and Biomolecular Systems, University of Stuttgart Stuttgart, Germany.
Peter Krolla-SidensteinChemistry of Oxydic and Organic Interfaces, Karlsruhe Institute of Technology, Institute of Functional Interfaces Karlsruhe, Germany.
Carlos AzucenaChemistry of Oxydic and Organic Interfaces, Karlsruhe Institute of Technology, Institute of Functional Interfaces Karlsruhe, Germany.
Hartmut GliemannChemistry of Oxydic and Organic Interfaces, Karlsruhe Institute of Technology, Institute of Functional Interfaces Karlsruhe, Germany.
Sabine EibenDepartment of Molecular Biology and Plant Virology, Institute of Biomaterials and Biomolecular Systems, University of Stuttgart Stuttgart, Germany.
Fania GeigerDepartment of New Materials and Biosystems, Max-Planck-Institute for Intelligent Systems Stuttgart, Germany.
Christina WegeDepartment of Molecular Biology and Plant Virology, Institute of Biomaterials and Biomolecular Systems, University of Stuttgart Stuttgart, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tobacco mosaic virus (TMV) is a robust nanotubular nucleoprotein scaffold increasingly employed for the high density presentation of functional molecules such as peptides, fluorescent dyes, and antibodies. We report on its use as advantageous carrier for sensor enzymes. A TMV mutant with a cysteine residue exposed on every coat protein (CP) subunit (TMVCys) enabled the coupling of bifunctional maleimide-polyethylene glycol (PEG)-biotin linkers (TMVCys/Bio). Its surface was equipped with two streptavidin [SA]-conjugated enzymes: glucose oxidase ([SA]-GOx) and horseradish peroxidase ([SA]-HRP). At least 50% of the CPs were decorated with a linker molecule, and all thereof with active enzymes. Upon use as adapter scaffolds in conventional "high-binding" microtiter plates, TMV sticks allowed the immobilization of up to 45-fold higher catalytic activities than control samples with the same input of enzymes. Moreover, they increased storage stability and reusability in relation to enzymes applied directly to microtiter plate wells. The functionalized TMV adsorbed to solid supports showed a homogeneous distribution of the conjugated enzymes and structural integrity of the nanorods upon transmission electron and atomic force microscopy. The high surface-increase and steric accessibility of the viral scaffolds in combination with the biochemical environment provided by the plant viral coat may explain the beneficial effects. TMV can, thus, serve as a favorable multivalent nanoscale platform for the ordered presentation of bioactive proteins.

Indexed as

biotemplateenzyme cascade systemenzyme shelf-lifeglucose sensorreusabilityscaffoldsurface immobilizationtobacco mosaic virus (TMV)

Identifiers

PMID26734040
PMCPMC4689848

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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.