Jr. Kanwar et R. Kanwar, PURIFICATION AND PARTIAL IMMUNOCHEMICAL CHARACTERIZATION OF A LOW-MOLECULAR-MASS, DIAGNOSTIC ECHINOCOCCUS-GRANULOSUS IMMUNOGEN FOR SHEEP HYDATIDOSIS, FEMS immunology and medical microbiology, 9(2), 1994, pp. 101-107
A hydatid specific antigen of 8 kDa molecular mass was affinity-purifi
ed from crude hydatid cyst fluid. Some of the epitopes recognised by a
ntibodies in the sera from sheep with hydatidosis were periodate-sensi
tive. The purified 8 kDa antigen was observed to be a thermo-stable gl
ycoprotein in its immunochemical characteristics. By immunofluorescenc
e on acetone-fixed protoscolices anti-8 kDa monospecific IgG antibodie
s indicated the existence of the 8 kDa molecule on the hooklets of pro
toscolices. The purified antigen was used in an enzyme-linked immunoso
rbent assay for the detection of specific antibodies in sera from shee
p hydatidosis. Eighteen (90%) of 20 sera from sheep hydatidosis had an
tibodies to purified 8 kDa antigen while none of the sera from other p
arasitic infections or uninfected animals had any detectable levels of
antibodies to 8 kDa antigen. Thus, the data on localization and recog
nition of hydatid specific 8 kDa molecule suggested that this may be o
ne of the major molecules for specific immunodiagnosis and for modulat
ing the hydatid disease process in infected hosts.