Evidence map›Paper›PMID 28784139›Full record

ArticleMicrobial cell factories2017

Structure and application of antifreeze proteins from Antarctic bacteria.

Patricio A Muñoz, Sebastián L Márquez, Fernando D González-Nilo, Valeria Márquez-Miranda, Jenny M Blamey

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 86 citations in OpenAlex.

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  17. The EndophyticPlants (Basel, Switzerland) · 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

5 authors at 2 institutions in 1 country.

Patricio A MuñozFundación Científica y Cultural Biociencia, José Domingo Cañas, 2280, Ñuñoa, Santiago, Chile. pmunoz@bioscience.cl.
Sebastián L MárquezFundación Científica y Cultural Biociencia, José Domingo Cañas, 2280, Ñuñoa, Santiago, Chile.
Fernando D González-NiloCenter for Bioinformatics and Integrative Biology (CBIB), Facultad de Ciencias Biológicas, Universidad Andres Bello, Avenida Republica 239, Santiago, Chile.
Valeria Márquez-MirandaCenter for Bioinformatics and Integrative Biology (CBIB), Facultad de Ciencias Biológicas, Universidad Andres Bello, Avenida Republica 239, Santiago, Chile.
Jenny M BlameyFundación Científica y Cultural Biociencia, José Domingo Cañas, 2280, Ñuñoa, Santiago, Chile. jblamey@bioscience.cl.
Universidad Andrés Bello · CLUniversidad de Santiago de Chile · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAntifreeze proteins (AFPs) production is a survival strategy of psychrophiles in ice. These proteins have potential in frozen food industry avoiding the damage in the structure of animal or vegetal foods. Moreover, there is not much information regarding the interaction of Antarctic bacterial AFPs with ice, and new determinations are needed to understand the behaviour of these proteins at the water/ice interface.

resultsDifferent Antarctic places were screened for antifreeze activity and microorganisms were selected for the presence of thermal hysteresis in their crude extracts. Isolates GU1.7.1, GU3.1.1, and AFP5.1 showed higher thermal hysteresis and were characterized using a polyphasic approach. Studies using cucumber and zucchini samples showed cellular protection when samples were treated with partially purified AFPs or a commercial AFP as was determined using toluidine blue O and neutral red staining. Additionally, genome analysis of these isolates revealed the presence of genes that encode for putative AFPs. Deduced amino acids sequences from GU3.1.1 (gu3A and gu3B) and AFP5.1 (afp5A) showed high similarity to reported AFPs which crystal structures are solved, allowing then generating homology models. Modelled proteins showed a triangular prism form similar to β-helix AFPs with a linear distribution of threonine residues at one side of the prism that could correspond to the putative ice binding side. The statistically best models were used to build a protein-water system. Molecular dynamics simulations were then performed to compare the antifreezing behaviour of these AFPs at the ice/water interface. Docking and molecular dynamics simulations revealed that gu3B could have the most efficient antifreezing behavior, but gu3A could have a higher affinity for ice.

conclusionsAFPs from Antarctic microorganisms GU1.7.1, GU3.1.1 and AFP5.1 protect cellular structures of frozen food showing a potential for frozen food industry. Modeled proteins possess a β-helix structure, and molecular docking analysis revealed the AFP gu3B could be the most efficient AFPs in order to avoid the formation of ice crystals, even when gu3A has a higher affinity for ice. By determining the interaction of AFPs at the ice/water interface, it will be possible to understand the process of adaptation of psychrophilic bacteria to Antarctic ice.

Indexed as

Amino Acid SequenceAntarctic RegionsAntifreeze ProteinsBacteriaBacterial ProteinsBinding SitesCucurbitaCucurbitaceaeDNA, BacterialMolecular Docking SimulationMolecular Dynamics SimulationProtein Structure, TertiarySequence AlignmentSequence Analysis, DNAWhole Genome SequencingAntifreeze ProteinsBacterial ProteinsDNA, BacterialAntarcticaAntifreeze proteinsFrozen foodIce binding proteinsPsychrophiles

Identifiers

PMID28784139
PMCPMC5547475
OpenAlexW2743704417

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.