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Gene Expression Level, Immunolocalization, and Function of Fatty Acid-Binding Protein from Schistosoma japonicum
- Source :
- Journal of Parasitology. 107
- Publication Year :
- 2021
- Publisher :
- American Society of Parasitologists, 2021.
-
Abstract
- The Schistosoma japonicum fatty acid-binding protein (FABP) is used in the cell membrane to absorb and transport fatty acids, which cannot be resynthesized by the organism and combined with hydrophobic ligands. Among the 5 stages of the worm life cycle examined, FABP messenger ribonucleic acid (mRNA) expression was highest in male adult worms, followed by the liver-stage schistosome, and was the lowest in the lung-stage schistosome. The fabp gene-coding region was cloned and expressed to obtain recombinant S. japonicum FABP (rSjFABP) with a molecular weight of approximately 18 kDa. Mice were then immunized against rSjFABP to prepare anti-FABP serum. Using immunohistochemical techniques, FABP protein was found to localize to the eggshell, parenchyma, and digestive tract. Double-stranded RNA-mediated knockdown of FABP mRNA by RNA interference decreased the number of transcripts by >70%. Moreover, the egg production rate decreased, whereas the abnormal egg ratio was significantly increased in the FABP-silenced group compared with the negative control group (P < 0.05). These results demonstrate that FABP localizes in adults and in various stages. FABP contributes to the egg-laying capacity of adults, which may be related to the reproductive function of S. japonicum.
- Subjects :
- Male
Biology
Fatty Acid-Binding Proteins
Real-Time Polymerase Chain Reaction
Schistosoma japonicum
Fatty acid-binding protein
law.invention
Mice
law
RNA interference
Parenchyma
Animals
RNA, Messenger
Lung
Ecology, Evolution, Behavior and Systematics
Mice, Inbred BALB C
Gene knockdown
Messenger RNA
Helminth Proteins
biology.organism_classification
Immunohistochemistry
Molecular biology
Gene Expression Regulation
Liver
Recombinant DNA
Female
lipids (amino acids, peptides, and proteins)
Parasitology
Subjects
Details
- ISSN :
- 00223395
- Volume :
- 107
- Database :
- OpenAIRE
- Journal :
- Journal of Parasitology
- Accession number :
- edsair.doi.dedup.....108fb738c17752b05d40c7d271a9c354
- Full Text :
- https://doi.org/10.1645/19-42