Molecular characteristics of Echinococcus multilocularis FABP1 and its regulatory functions on murine macrophages.
Acta Trop
; 255: 107247, 2024 Jul.
Article
en En
| MEDLINE
| ID: mdl-38729330
ABSTRACT
Fatty acid binding proteins (FABPs) have emerged as attractive vaccination candidates for several platyhelminth species. To explore the physiological functions of Echinococcus multilocularis (E. multilocularis) FABP, the molecular characteristics of EmFABP1 were analyzed by online software, and the regulatory roles of rEmFABP1 protein in murine macrophages were further investigated. The emfabp1 gene encodes 133 amino acids with the characteristic ß-barrel shape of the cytoplasmic FABP family. Natural EmFABP1 protein is predominantly expressed in protoscoleces tegument and germinal layer cells and is also detected in cyst fluid and exosomes of E. multilocularis. rEmFABP1 protein demonstrated a notable suppression of phagocytic activity and nitric oxide production in murine macrophages. Additionally, the protein was observed to promote apoptosis and regulate cytokine expression in macrophages. These findings suggested that E. multilocularis FABP1 is critical in modifying macrophage physiological processes and that this protein may have immunomodulatory roles during infection.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Fagocitosis
/
Proteínas del Helminto
/
Echinococcus multilocularis
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Proteínas de Unión a Ácidos Grasos
/
Macrófagos
Límite:
Animals
Idioma:
En
Revista:
Acta Trop
Año:
2024
Tipo del documento:
Article
País de afiliación:
China