Premium
Localization of carbohydrate terminals on Tetracapsuloides bryosalmonae using lectin histochemistry and immunogold electron microscopy
Author(s) -
Morris D J,
Adams A
Publication year - 2004
Publication title -
journal of fish diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.819
H-Index - 85
eISSN - 1365-2761
pISSN - 0140-7775
DOI - 10.1046/j.1365-2761.2003.00509.x
Subject(s) - biology , immunogold labelling , lectin , glycoconjugate , ultrastructure , staining , glycocalyx , parasite hosting , myxosporea , cytochemistry , microbiology and biotechnology , pathology , anatomy , biochemistry , medicine , genetics , world wide web , computer science , spore
Tetracapsuloides bryosalmonae is the myxozoan parasite that causes the commercially important proliferative kidney disease (PKD) in salmonid aquaculture. Previous studies on the binding of lectins to T. bryosalmonae identified Griffonia simplificola agglutinin I (GS I) as useful for parasite identification. This lectin was also implicated as recognizing antigenic structures on the parasite. Here, we examine the histochemical staining and ultrastructural localization of a panel of 21 lectins on the extrasporogonic stage of T. bryosalmonae . The histochemical staining studies indicated that the majority of lectins bound to the renal stages of T. bryosalmonae , however not all of these lectins could be successfully localized using immunogold electron microscopy. Of the lectins that were localized many, including GS I, bound to membranes associated with the lysosomal pathway within the extrasporogonic primary cell of the parasite, indicating that these organelles are rich in glycoconjugates. The histochemical staining of Erythrina cristagalli ECL was unique and highlighted a different distribution of glycoconjugates in the periphery of some extrasporogonic parasites within the renal sinuses when compared with stages in the interstitium, suggesting the presence of distinct blood forms of T. bryosalmonae .