| Literature DB >> 17016726 |
Doreen Jung1, Jens Peter Teifke, Axel Karger, Kathrin Michael, Simone Venz, Wolfgang Wittmann, Katharina Kindermann, Karsten Nöckler, Egbert Mundt.
Abstract
The complete gene encoding the 53-kDa protein derived from Trichinella spiralis was cloned and expressed using a baculovirus-based system. Characterization of a purified fusion protein consisting of the 53-kDa protein and the glutathione S-transferase protein showed unspecific reactivity with swine pre-immune serum in both enzyme-linked immunosorbent assay (ELISA) and Western blot analysis. Subsequently, a purified C-terminal 6xHis-tagged 53-kDa protein was used in an ELISA. The evaluation of the test using a negative serum panel showed a high specificity for the ELISA. Serum panels of pigs infected with T. spiralis of two independent experiments showed that pigs of one experiment were tested positive by the ELISA, whereas all sera of the second experiment were negative, indicating a low sensitivity of the ELISA. Furthermore, experimental evidence was found by using mass spectroscopy and Western blot analysis that the 53-kDa protein was not part of the excretory/secretory antigen of T. spiralis as shown in this study.Entities:
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Year: 2006 PMID: 17016726 DOI: 10.1007/s00436-006-0296-7
Source DB: PubMed Journal: Parasitol Res ISSN: 0932-0113 Impact factor: 2.289