Molecular Characteristics of the Fatty-Acid-Binding Protein (FABP) Family in Spirometra mansoni―A Neglected Medical Tapeworm

• Published in: Animals (Basel) Vol. 13; no. 18; p. 2855
• Main Authors: Liu, Shinan, Gao, Fei, Wang, Ruijie, Li, Wen, Wang, Siyao, Zhang, Xi
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 08.09.2023; MDPI
• Subjects: Animals; Cloning; Fatty acids; fatty-acid-binding protein; gene expression; Genes; Genomes; Lipids; molecular characterization; Oxidation; Parasites; Phylogenetics; Proteins; Software; Spirometra mansoni; tapeworm; Worms
• ISSN: 2076-2615; 2076-2615
• DOI: 10.3390/ani13182855

The plerocercoid larva of the tapeworm Spirometra mansoni can parasitize humans and animals, causing serious parasitic zoonosis. The molecular characteristics and adaptive parasitism mechanism of Spirometra tapeworms are still unknown. In this study, 11 new members of the fatty-acid-binding protein (FABP) family were characterized in S. mansoni. A clustering analysis showed 11 SmFABPs arranged into two groups, and motif patterns within each group had similar organizations. RT–qPCR showed that SmFABPs were highly expressed in the adult stage, especially in gravid proglottid. A high genetic diversity of SmFABPs and relative conservation of FABPs in medical platyhelminthes were observed in the phylogenetic analysis. Immunolocalization revealed that natural SmFABP is mainly located in the tegument and parenchymal tissue of the plerocercoid and the uterus, genital pores, and cortex of adult worms. rSmFABP can build a more stable holo form when binding with palmitic acid to protect the hydrolytic sites of the protein. A fatty acid starvation induction test suggested that SmFABP might be involved in fatty acid absorption, transport, and metabolism in S. mansoni. The findings in this study will lay the foundation to better explore the underlying mechanisms of FABPs involved in Spirometra tapeworms as well as related taxa.