Evidence map›Paper›PMID 39613868›Full record

ArticleNature chemistry2025

Phase separation and ageing of glycine-rich protein from tick adhesive.

Ketan A Ganar, Manali Nandy, Polina Turbina, Chang Chen, Dennis Suylen, Elisa Nihoul, Emily Louise Pascoe, Stan van der Beelen, Maarten Plaum, Leendert van den Bos and 3 more

Abstract read
In one paragraph

Article in Nature chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Review
  2. A biofilm-derived peptide as an underwater adhesive.bioRxiv : the preprint server for biology · 2026
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  15. bioRxiv : the preprint server for biology · 2025
    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

13 authors.

Ketan A Ganar *Laboratory of Physical Chemistry and Soft Matter, Wageningen University and Research, Wageningen, the Netherlands.
Manali Nandy *Laboratory of Physical Chemistry and Soft Matter, Wageningen University and Research, Wageningen, the Netherlands.ORCID 0000-0002-6316-178X
Polina Turbina *Laboratory of Physical Chemistry and Soft Matter, Wageningen University and Research, Wageningen, the Netherlands.ORCID 0009-0003-0116-041X
Chang ChenLaboratory of Physical Chemistry and Soft Matter, Wageningen University and Research, Wageningen, the Netherlands.ORCID 0000-0001-5040-8547
Dennis SuylenDepartment of Biochemistry, Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, Maastricht, the Netherlands.
Elisa NihoulDepartment of Biochemistry, Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, Maastricht, the Netherlands.ORCID 0009-0009-8929-9697
Emily Louise PascoeLaboratory of Entomology, Wageningen University and Research, Wageningen, the Netherlands.ORCID 0000-0003-3493-3485
Stan van der BeelenEnzyTag BV, Nuth, the Netherlands.
Maarten PlaumEnzyTag BV, Nuth, the Netherlands.
Leendert van den BosEnzyTag BV, Nuth, the Netherlands.
Constantianus J M KoenraadtLaboratory of Entomology, Wageningen University and Research, Wageningen, the Netherlands.
Ingrid DijkgraafDepartment of Biochemistry, Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, Maastricht, the Netherlands. i.dijkgraaf@maastrichtuniversity.nl.ORCID 0000-0003-4586-3646
Siddharth DeshpandeLaboratory of Physical Chemistry and Soft Matter, Wageningen University and Research, Wageningen, the Netherlands. siddharth.deshpande@wur.nl.ORCID 0000-0002-7137-8962

Funding

Nederlandse Organisatie voor Wetenschappelijk Onderzoek (Netherlands Organisation for Scientific Research) OCENW.KLEIN.465
6 · The paper itself

Abstract

Hard ticks feed on their host for multiple days. To ensure firm attachment, they secrete a protein-rich saliva that eventually forms a solid cement cone. The underlying mechanism of this liquid-to-solid transition is currently not understood. This study focuses on the phase transitions of a disordered glycine-rich protein (GRP) found in tick saliva. We show that GRP undergoes liquid-liquid phase separation via simple coacervation to form biomolecular condensates in salty environments. Cation-π and π-π interactions mediated by periodically placed arginine and aromatic amino-acid residues are the primary driving forces that promote phase separation. Interestingly, GRP condensates exhibit ageing by undergoing liquid-to-gel transition over time and exhibit adhesive properties, similar to the naturally occurring cement cone. Finally, we provide evidence for protein-rich condensates in natural tick saliva. Our findings provide a starting point to gain further insights into the bioadhesion of ticks, to develop novel tick control strategies, and towards achieving biomedical applications such as tissue sealants.

Indexed as

AdhesivesGlycineSalivary Proteins and PeptidesTicksAnimalsPhase SeparationPhase TransitionSalivaAdhesivesGlycineSalivary Proteins and Peptides

Identifiers

PMID39613868
PMCPMC11794139

What OpenQuestion holds

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Registered trials

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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.