Glycosylation changes in different developmental stages of Trichinella

Abstract

Abstract:The in situ identification of carbohydrate structures in Trichinella spiralis intestinal larvae, adults and L1 muscular larvae was carried out by lectin histochemistry, with emphasis on the O-linked glycans. The absence of reactivity with two lectins-TML and MAL indicated thatTrichinella spiralis does not synthesize sialic acid. Reactivity with HPA, VVL-B4, PNA and UEA-I staining suggested that T. spiralis synthesizes and expresses on its cuticle O-linked glycans analogous to Tn-antigen (GalNAc-α-Ser/Thr), T-antigen (Gal-β1,3-GalNAc-α-Ser/Thr) and also structures analogous to A-blood group antigens (GalNAc-α1,3-Gal-β1,3(4)-(Fuc-α1,2-)-R). Expression of the saccharidic moieties is stage-specific. Blood group-A and T-antigen structures were identified on the cuticle of the intestinal and muscular larvae. The Tn-antigen structure was missing in the intestinal larvae. Appropriate ligands for WGA were not identified in the adult individuals. The obtained results may contribute to a better understanding of the glycobiology of this parasitic nematode in relation to occupation of its intracellular niche. The presence of saccharidic structures analogous to some of those expressed on the intestinal epithelial cells may serve as a protective shield on the surface of the parasite.

Detection of O-glycosylated proteins from different Trichinella species muscle larvae total extracts

“…This was in accordance with the previous report on the absence of acidic sugars in adult T. spiralis (Morelle et al, 2000). Moreover, alcian-blue staining of T. spiralis muscle larvae tissue sections and histochemistry with the lectins specific for sialic acid also did not show any labeling (Milcheva et al, 2009). The absence of particularly α6-silaylation in T. spiralis muscle larvae ESP has been reported by Gruden-Movsesijan et al (2002).…”

“…since their somatic glycoproteins reacted neither with TML, nor with MAL-II. This was in accordance with the previous report on the absence of acidic sugars in adult T. spiralis (Morelle et al, 2000). Moreover, alcian-blue staining of T. spiralis muscle larvae tissue sections and histochemistry with the lectins specific for sialic acid also did not show any labeling (Milcheva et al, 2009).…”

“…We used HPA in the context of its ability to recognize Tnantigen (Roth, 1984), a feature that resembles the VVL-B 4 affinity ( Table 1). Both lectins showed the same pattern of staining on T. spiralis muscle larvae tissue sections (Milcheva et al, 2009). The lectin-blots however revealed that HPA and VVL-B 4 labeled very different products and the pattern of labeling was different as well ( Fig.…”

“…The glycobiology of Trichinella is becoming a subject of rising interest. N-glycosylation has been characterized in detail in adult T. spiralis total extracts (Morelle et al, 2000) and also in ESP from T. spiralis muscle larvae (Gruden-Movsesijan et al, 2002), in which the presence of the unusual sugar tyvelose has been discovered (Wisnewski et al, 1993;Reason et al, 1994). Except for one report (Gruden-Movesijan et al, 2002), there is virtually no information available on the structure and the synthesis of O-glycans in Trichinella.…”

Biodegradable Chitosan Decreases the Immune Response to Trichinella spiralis in Mice

“…The molecule is highly represented in T. spiralis N -glycans, and is typically found in the terminal position, or combined with N -acetylgalactosamine (GalNAc) in the carbohydrate chain (“LacdiNAC”: GalNAc-b1,4-GlcNAC). Interestingly, only the intestinal and muscular larval stages of T. spiralis synthesize a glycoprotein which specifically binds to a form of lectin known as wheat germ agglutinin (WGA) [ 23 , 24 ]. The structure of carbohydrates is crucial for their interaction with receptors during cell signaling and may induce immunosuppression [ 25 ].…”