Evidence map›Paper›PMID 42129291›Full record

ArticleScientific reports2026

Biochemical characterization of a fungal ice nucleation protein from Podila clonocystis.

Brenna J C Walsh, Sarah L Brewer, Andrea J Shepard, Noor Mahmoud, Elizabeth A Robinson, Brooke M Luisi, Joel M Sarapas, William D Stone

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

8 authors.

Brenna J C WalshResearch and Exploratory Development Department, Johns Hopkins Applied Physics Laboratory, Laurel, MD, 20723, USA. Brenna.Walsh@jhuapl.edu.
Sarah L BrewerResearch and Exploratory Development Department, Johns Hopkins Applied Physics Laboratory, Laurel, MD, 20723, USA.
Andrea J ShepardResearch and Exploratory Development Department, Johns Hopkins Applied Physics Laboratory, Laurel, MD, 20723, USA.
Noor MahmoudResearch and Exploratory Development Department, Johns Hopkins Applied Physics Laboratory, Laurel, MD, 20723, USA.
Elizabeth A RobinsonResearch and Exploratory Development Department, Johns Hopkins Applied Physics Laboratory, Laurel, MD, 20723, USA.
Brooke M LuisiResearch and Exploratory Development Department, Johns Hopkins Applied Physics Laboratory, Laurel, MD, 20723, USA.
Joel M SarapasResearch and Exploratory Development Department, Johns Hopkins Applied Physics Laboratory, Laurel, MD, 20723, USA.
William D StoneResearch and Exploratory Development Department, Johns Hopkins Applied Physics Laboratory, Laurel, MD, 20723, USA. William.Stone@jhuapl.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological ice nucleation plays a pivotal role in atmospheric processes, yet the molecular basis of fungal ice nucleation remains poorly understood. We report the biochemical characterization of an ice nucleation protein (PcINP) from the soil-dwelling fungus Podila clonocystis, an organism that has been implicated in ice nuclei production; however, its ice nucleation activity has not been demonstrated. Using sequence similarity networks, we identified PcINP as a putative fungal homolog of bacterial INPs and confirmed its function through recombinant expression in Escherichia coli. We probed the function of PcINP structure through domain truncations and demonstrated that the N-terminal region is not necessary for ice nucleation activity and can be replaced with an expression-enhancing tag that significantly increases the number of active ice nuclei. Finally, we observed that a solution that contains monomeric PcINP has identical activity to solutions containing oligomerized INP, suggesting PcINP utilizes an in vitro aggregation mechanism to generate active oligomers. Our findings establish PcINP as a member of the emerging class of fungal INPs, expanding the known diversity of biological ice nucleators and highlighting their potential for environmental and biotechnological applications.

Indexed as

Fungal ProteinsIceAmino Acid SequenceBacterial Outer Membrane ProteinsEscherichia coliRecombinant ProteinsBacterial Outer Membrane ProteinsFungal ProteinsIceice nucleation proteinRecombinant Proteins

Identifiers

PMID42129291
PMCPMC13365547

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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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 Socratic graph.