Accumulation of α-2,6-sialyoglycoproteins in the muscle sarcoplasm due to Trichinella sp. invasion

Author:

Milcheva Rositsa12,Janega Pavol3,Celec Peter4,Petkova Svetlozara2,Hurniková Zuzana5,Izrael-Vlková Barbora4,Todorova Katerina2,Babál Pavel3

Affiliation:

1. Department of Pathology, IEMPAM, Bulgarian Academy of Sciences, ‘’Acad. G. Bonchev’’ Str. 25, 1113, Sofia, Bulgaria

2. Institute of Experimental Morphology, Pathology and Anthropology with Museum (IEMPAM), Bulgarian Academy of Sciences, “Acad. G. Bonchev” Str. 25, 1113Sofia, Bulgaria

3. Department of Pathology, Faculty of Medicine, Comenius University in Bratislava, Sasinkova 4, 81372Bratislava, Slovakia

4. Department of Molecular Biomedicine, Faculty of Medicine, Comenius University in Bratislava, Sasinkova 4, 81372Bratislava, Slovakia

5. Institute of Parasitology, Slovak Academy of Sciences, Hlinkova 3, 040 01Košice, Slovak Republic

Abstract

AbstractThe sialylation of the glycoproteins in skeletal muscle tissue is not well investigated, even though the essential role of the sialic acids for the proper muscular function has been proven by many researchers. The invasion of the parasitic nematode Trichinella spiralis in the muscles with subsequent formation of Nurse cell-parasite complex initiates increased accumulation of sialylated glycoproteins within the affected area of the muscle fiber. The aim of this study is to describe some details of the α-2,6-sialylation in invaded muscle cells. Asynchronous invasion with infectious T. spiralis larvae was experimentally induced in mice. The areas of the occupied sarcoplasm were reactive towards α-2,6-sialic acid specific Sambucus nigra agglutinin during the whole process of transformation to a Nurse cell.The cytoplasm of the developing Nurse cell reacted with Helix pomatia agglutinin, Arachis hypogea agglutinin and Vicia villosa lectin-B4 after neuraminidase pretreatment.Up-regulation of the enzyme ST6GalNAc1 and down-regulation of the enzyme ST6GalNAc3 were detected throughout the course of this study. The results from our study assumed accumulation of sialyl-Tn-Ag, 6`-sialyl lactosamine, SiA-α-2,6-Gal-β-1,3-GalNAc-α-Ser/Thr and Gal-β-1,3-GalNAc(SiA-α-2,6-)-α-1-Ser/Thr oligosaccharide structures into the occupied sarcoplasm. Further investigations in this domain will develop the understanding about the amazing adaptive capabilities of skeletal muscle tissue.

Publisher

Walter de Gruyter GmbH

Subject

General Agricultural and Biological Sciences,General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Neuroscience

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