ISSN:
1432-1955
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Abstract The carbohydrates on the surface ofHymenolepis diminuta were analyzed with gold-labelled lectins, and it was found that the surface coat of the anterior body differs from that of the strobila in its lectin-binding properties. Binding sites for lectins fromAbrus precatorius (APA),Arachis hypogaea (PNA),Glycine max (SBA) and for wheat germ agglutinin (WGA) and succinylated WGA were located on the scolex and strobilation zone. Lectin-gold particles attached mainly to the electron-dense spines. The surface coat may therefore expose sugar residues of theN-acetylglucosamine and galactose types. In contrast, the strobila had few binding sites for the above-mentioned lectins but bound concanavalin A (ConA). Lectins fromDolichos biflorus (DBA) andUlex europaeus (UEA-I) were not bound toH. diminuta. In juvenile worms from rats, the extension of the WGA- and SBA-positive region of the strobilation zone increased in length with the development of the worms. Lectin binding in juveniles from mice was similar when the mice had been immunosuppressed with cortisone. After the onset of the immune defense againstH. diminuta in nontreated mice, a moderate expression of lectin-binding substance also occurred on the strobila. Destrobilated worms were entirely covered with theN-acetylglucosamine- and galactose-containing glycoconjugates, and it is suggested that these worm remnants correspond to the lectin-binding part of normal, growing juveniles. The presence of the carbohydrates is discussed with respect to the relative resistance of the scolex-strobilation zone ofH. diminuta to immune rejection.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00932716
