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Department of Parasitology, Gifu University Graduate School of Medicine, Yanagido 1-1, Gifu, 501-1194 Japan
* To whom correspondence should be addressed. Email: isao{at}gifu-u.ac.jp.
| Abstract |
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The 53 kDa proteins in larval excretory-secretory (E-S) products were expressed from five Trichinella species (T. spiralis, T. britovi, T. nativa, T. pseudospiralis and T. papuae,) using the Escherichia coli expression system, and the antibody responses to the 53 kDa recombinant proteins in mice infected with Trichinella sp. were analyzed by Western blotting. The 53 kDa protein is conserved among the five Trichinella species, with >60% similarity in amino acid sequences. The 53 kDa recombinant proteins of T. spiralis and T. pseudospiralis reacted to sera from mice infected with T. spiralis and T. pseudospiralis at 8 days post infection (PI), respectively. An antibody against the 53 kDa recombinant protein of T. spiralis recognized the 53 kDa protein in the crude extracts from adult worms and 30 days PI muscle larvae, and E-S products from muscle larvae of T. spiralis, but did not recognize any proteins from T. pseudospiralis. The sera from the mice infected with T. spiralis strongly reacted with the 53 kDa recombinant protein of T. spiralis, but did not react with the 53 kDa recombinant proteins of T. britovi, T. nativa, T.pseudospiralis and T. papuae. Similarly, the sera from mice infected with T. britovi, T. nativa, T.pseudospiralis or T. papuae strongly reacted with the 53 kDa recombinant proteins of T. britovi, T. nativa, T.pseudospiralis or T. papuae, respectively. These results showed that the 53 kDa recombinant proteins provide early and species-specific antibody responses in mice infected with Trichinella sp.
| Antimicrob. Agents Chemother. | Clin. Microbiol. Rev. | Infect. Immun. |
|---|---|---|
| J. Clin. Microbiol. | J. Virol. | ALL ASM JOURNALS |