Evidence map›Paper›PMID 36966297›Full record

ArticleJournal of nanobiotechnology2023

Bioengineering of air-filled protein nanoparticles by genetic and chemical functionalization.

Ram Karan, Dominik Renn, Shuho Nozue, Lingyun Zhao, Satoshi Habuchi, Thorsten Allers, Magnus Rueping

Open access · goldFull text read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of nanobiotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

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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

7 authors at 3 institutions in 3 countries.

Ram KaranKing Abdullah University of Science and Technology (KAUST), KAUST Catalysis Center, Thuwal, 23955-6900, Saudi Arabia. ram.karan@kaust.edu.sa.
Dominik RennKing Abdullah University of Science and Technology (KAUST), KAUST Catalysis Center, Thuwal, 23955-6900, Saudi Arabia.
Shuho NozueBiological and Environmental Science and Engineering, King Abdullah University of Science and Technology (KAUST), Thuwal, 23955-6900, Saudi Arabia.
Lingyun ZhaoImaging and Characterization Core Lab, King Abdullah University of Science and Technology (KAUST), Thuwal, 23955-6900, Saudi Arabia.
Satoshi HabuchiBiological and Environmental Science and Engineering, King Abdullah University of Science and Technology (KAUST), Thuwal, 23955-6900, Saudi Arabia.
Thorsten AllersSchool of Life Sciences, University of Nottingham, Nottingham, NG7 2UH, UK.
Magnus RuepingKing Abdullah University of Science and Technology (KAUST), KAUST Catalysis Center, Thuwal, 23955-6900, Saudi Arabia. magnus.rueping@kaust.edu.sa.
King Abdullah University of Science and Technology · SARWTH Aachen University · DEUniversity of Nottingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundVarious bacteria and archaea, including halophilic archaeon Halobacterium sp. NRC-1 produce gas vesicle nanoparticles (GVNPs), a unique class of stable, air-filled intracellular proteinaceous nanostructures. GVNPs are an attractive tool for biotechnological applications due to their readily production, purification, and unique physical properties. GVNPs are spindle- or cylinder-shaped, typically with a length of 100 nm to 1.5 μm and a width of 30-250 nm. Multiple monomeric subunits of GvpA and GvpC proteins form the GVNP shell, and several additional proteins are required as minor structural or assembly proteins. The haloarchaeal genetic system has been successfully used to produce and bioengineer GVNPs by fusing several foreign proteins with GvpC and has shown various applications, such as biocatalysis, diagnostics, bioimaging, drug delivery, and vaccine development.

resultsWe demonstrated that native GvpC can be removed in a low salt buffer during the GVNP purification, leaving the GvpA-based GVNP's shell intact and stable under physiological conditions. Here, we report a genetic engineering and chemical modification approach for functionalizing the major GVNP protein, GvpA. This novel approach is based on combinatorial cysteine mutagenesis within GvpA and genetic expansion of the N-terminal and C-terminal regions. Consequently, we generated GvpA single, double, and triple cysteine variant libraries and investigated the impact of mutations on the structure and physical shape of the GVNPs formed. We used a thiol-maleimide chemistry strategy to introduce the biotechnological relevant activity by maleimide-activated streptavidin-biotin and maleimide-activated SpyTag003-SpyCatcher003 mediated functionalization of GVNPs.

conclusionThe merger of these genetic and chemical functionalization approaches significantly extends these novel protein nanomaterials' bioengineering and functionalization potential to assemble catalytically active proteins, biomaterials, and vaccines onto one nanoparticle in a modular fashion.

Indexed as

CysteineNanoparticlesBioengineeringHalobacteriumProteinsCysteineProteinsBioengineeringBiomaterialsExtremophilesGas vesicleHalophilesNanoparticles

Identifiers

PMID36966297
PMCPMC10039352
OpenAlexW4360838461

What OpenQuestion holds

Textfull text, public
LicenceCC BY
reference markers read1
measurements read55
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.