Abstract
This study was aimed to describe some glycosylation changes in the Nurse cell of Trichinella spiralis in mouse skeletal muscle. Tissue specimens were subjected to lectin histochemistry with Maackia amurensis lectin (MAL), Peanut agglutinin (PNA) and neuraminidase desialylation in order to verify and analyse the structure of α-2,3-sialylated glycoproteins, discovered within the affected sarcoplasm. The expressions of two sialyltransferases were examined by immunohistochemistry. It was found out that the occupied portion of skeletal muscle cell responded with synthesis of presumable sialyl-T-antigen and α-2,3-sialyllactosamine structure, that remained accumulated during the time course of Nurse cell development. The enzymes β-galactoside-α-2,3-sialyltransferases 2 and 4, which could be responsible for the sialylation of each of these structures, were however not present in the invaded muscle portions, although their expressions in the healthy surrounding tissue remained persistent. Our results contribute to the progressive understanding about the amazing abilities of Trichinella spiralis to manipulate the genetic programme of its host.
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