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Molecular characterization of Trichinella spiralis galectin and its participation in larval invasion of host’s intestinal epithelial cells
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Molecular characterization of Trichinella spiralis galectin and its participation in larval invasion of host’s intestinal epithelial cells
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Journal Article
Molecular characterization of Trichinella spiralis galectin and its participation in larval invasion of host’s intestinal epithelial cells
2018
Overview
The aim of this study was to study the molecular characteristics of
Trichinella spiralis
galectin (Tsgal) and interactions between Tsgal and host’s intestinal epithelial cells (IECs). The functional domain of Tsgal was cloned and expressed in an
E. coli
system. The Tsgal was 97.1% identity to the galectin of
T. nativa
and 20.8% identity to the galectin-8 of humans. Conserved domain analysis revealed that Tsgal belongs to TR-type galectin and has two carbon recognized domain. The rTsgal with 29.1 kDa could be recognized by
T. spiralis
-infected mice at 42 days post-infection (dpi). The transcription and expression of Tsgal gene was detected by RT-PCR and Western blotting in all
T. spiralis
developmental stages (intestinal infective larvae, adult worms, newborn larvae, and muscle larvae). The IFA results revealed that Tsgal was mainly located at the cuticles and stichosomes of
T. spiralis
larvae (ML, IIL and NBL). The rTsgal had hemagglutinating function for erythrocytes from human, rabbit and mouse. The results of Far Western blot and confocal microscopy indicated there was specific binding between rTsgal and IECs, and the binding was located the membrane and cytoplasm of the IECs. Out of four sugars (sucrose, glucose, lactose and maltose), only lactose was able to inhibit the rTsgal agglutinating role for human type B erythrocytes. Moreover, the rTsgal could promote the larval invasion of IECs, while the anti-rTsgal serum inhibited the larval invasion. These results demonstrated that Tsgal might participate in the
T. spiralis
invasion of intestinal epithelium in early infection stage.
Publisher
BioMed Central,BioMed Central Ltd,Springer Nature B.V,BMC
Subject
/ Animals
/ carbon
/ Female
/ genes
/ glucose
/ Helminth Proteins - chemistry
/ Helminth Proteins - genetics
/ Helminth Proteins - metabolism
/ humans
/ Intestinal Mucosa - parasitology
/ Lactose
/ Larva - growth & development
/ Male
/ maltose
/ Mammals
/ Medicine
/ Mice
/ neonates
/ Proteins
/ rabbits
/ reverse transcriptase polymerase chain reaction
/ Rodents
/ sucrose
/ Trichinella spiralis - growth & development
/ Trichinella spiralis - physiology
/ Trichinellosis - parasitology
/ Vaccines
/ Veterinary Medicine/Veterinary Science
/ Virology
/ Zoonoses
