Evidence map›Paper›PMID 41082564›Full record

ArticlePLoS neglected tropical diseases2025

Characterization and ligand binding properties of a fatty acid- and retinol- binding protein (Hp-FAR-2) from Heligmosomoides polygyrus.

Pakeeza Azizpor, Janice Montoya, Fayez Eyabi, Jose Ramirez, Tara Hill, Robert Pena, Manisha Mishra, Martin J Boulanger, Adler R Dillman

Abstract read
In one paragraph

Article in PLoS neglected tropical diseases, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

9 authors.

Pakeeza AzizporDepartment of Nematology, University of California, Riverside, California, United States of America.
Janice MontoyaDepartment of Nematology, University of California, Riverside, California, United States of America.
Fayez EyabiDepartment of Nematology, University of California, Riverside, California, United States of America.
Jose RamirezDepartment of Nematology, University of California, Riverside, California, United States of America.
Tara HillDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, Canada.
Robert PenaDepartment of Nematology, University of California, Riverside, California, United States of America.
Manisha MishraDepartment of Nematology, University of California, Riverside, California, United States of America.
Martin J BoulangerDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, Canada.
Adler R DillmanDepartment of Nematology, University of California, Riverside, California, United States of America.ORCID 0000-0001-7171-4332

Funding

Molecular mayhem: Immune modulation and eicosanoid signaling during infectionR35GM137934 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI Adler Ray Dillman · 2020 to 2026
$2.3M
NIGMS NIH HHS R35 GM137934
6 · The paper itself

Abstract

Parasitic nematodes are major pathogens of humans, animals, and plants, contributing to global health challenges and substantial agricultural losses. Fatty acid- and retinol-binding proteins (FARs), secreted by parasitic nematodes, are believed to play key roles in host-pathogen interactions, including immune modulation and nutrient acquisition. In this study, we characterize a FAR protein from the gastrointestinal nematode Heligmosomoides polygyrus, Hp-FAR-2. Hp-FAR-2, unlike FARs from Caenorhabditis elegans, Steinernema carpocapsae, and Ancylostoma ceylanicum, did not influence immunity or survival in a Drosophila melanogaster infection model, suggesting functional divergence within the FAR family. Competitive lipid-binding assays revealed a preference for omega-3 and omega-6 polyunsaturated fatty acids, indicating selective binding to bioactive lipids that may modulate immunity. Using RAW 264.7 macrophages, we found that Hp-FAR-2 suppresses the expression of both M1-associated (TNF-α, IL-6) and M2-associated (Chil3) markers during polarization, implicating it as a broad immunomodulator that may inhibit inflammatory responses and tissue repair mechanisms to promote chronic infection. Our findings support a model in which Hp-FAR-2 disrupts host lipid signaling and immune function to favor parasite persistence, suggesting its potential role in the excretory/secretory products of H. polygyrus. These findings enhance our understanding of FAR-mediated host manipulation and may inform the development of novel anthelmintic or immunoregulatory therapies.

Indexed as

Fatty Acid-Binding ProteinsHelminth ProteinsNematospiroides dubiusRetinol-Binding ProteinsAnimalsDrosophila melanogasterLigandsMacrophagesMiceProtein BindingRAW 264.7 CellsStrongylida InfectionsFatty Acid-Binding ProteinsHelminth ProteinsLigandsRetinol-Binding Proteins

Identifiers

PMID41082564
PMCPMC12543159

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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.