Premium
Purification and characterization of a specific antigen from Echinococcus multilocularis
Author(s) -
GOTTSTEIN B.
Publication year - 1985
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1111/j.1365-3024.1985.tb00070.x
Subject(s) - echinococcus multilocularis , metacestode , antigen , echinococcus granulosus , biology , isoelectric point , microbiology and biotechnology , echinococcosis , helminths , immunology , cestoda , biochemistry , zoology , enzyme
Summary A polypeptide (Em2a) purified by affinity chromatography from the Echinococcus multilocularis metacestode showed a high degree of purity as assayed by SDS‐PAGE and analytical isoelectrical focusing. A minor contamination with host albumin was revealed. Estimation of relative mol. mass gave a value of 54,000. The isoelectric point was found to be 4·8. Antigenic activity of the polypeptide was demonstrated by immunoprecipitation and western blotting. In these assays the protein was recognized only by homologous sera from patients infected with larval E. multilocularis . This antigen (Em2a) did not react in the ELISA with sera from patients infected with heterologous helminths; these sera were highly cross‐reacting with antigen from E. granulosus hydatid fluid. Seventy‐three (94%) from 78 investigated patients (alveolar echinococcosis) showed a seropositive reaction with the polypeptide Em2a.