Publikationsdatenbank

Molecular and cellular characterization of equine Vanins:
putative biomolecules in equine asthma (2025)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Landmann, K. (WE 12)

Bartenschlager, F. (WE 12)

Schnabel, C.

Zeyner, A.

Mundhenk, L. (WE 12)

Quelle

Journal of comparative pathology

Bandzählung: 222

Seiten: 54

ISSN: 0021-9975

Sprache

Englisch

Verweise

URL (Volltext): https://linkinghub.elsevier.com/retrieve/pii/S0021997525003792

DOI: 10.1016/j.jcpa.2025.10.089

Kontakt

Institut für Tierpathologie

Robert-von-Ostertag-Str. 15
14163 Berlin
+49 30 838 62450
pathologie@vetmed.fu-berlin.de

Abstract / Zusammenfassung

Background
Equine asthma (EA) is the most common chronic respiratory disease in horses, often associated with hypercrinia and mucus plugging. Recent proteomic data revealed an enrichment of Vanin-1 (VNN1) in the mucus of horses affected by severe EA. VNN1 is associated with chronic respiratory diseases in humans and encodes a pantetheinase, a branch of the Nitrilase superfamily, which can release cysteamine. Cysteamine as a pharmacological compound can prevent asthma development. However, Vanins in horses remain entirely uncharacterized.
Materials & Methods
Equine Vanin genes were identified in silico and analyzed for structural proteomic features using SOSUI, SignalP, PredGPI, and NetNGlyc. Tissue samples from various organs and airway regions of healthy horses were collected post-mortem for RT-qPCR (n = 5) and in-situ hybridization (n = 3) to analyze the tissue and cellular expression patterns. The cloned coding sequences were transfected into HEK293 cells to study the cellular transport of the proteins. Their post-translational glycosylation pattern was identified via Endo-H and PNGase-F treatment.
Results
In silico analysis identified three equine Vanin genes (eVNN1, eVNN2, eVNN3) clustered on chromosome 10, encoding canonical Nitrilase superfamily domains. All genes exhibited broad tissue expression, but distinct respiratory localization, with eVNN1 and eVNN2 in respiratory epithelium and eVNN3 in submucosal glands. The glycosylated eVNN1 and eVNN3 were secreted by the cells, while the glycosylated eVNN2 remained cell-associated.
Conclusion
The three equine Vanins seem to cover different functional niches in equine airways. This paves the way for future research into their putative role in EA.