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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.

Molecular characterization of Trichinella spiralis galectin and its participation in larval invasion of host’s intestinal epithelial cells