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Identification and characterization of a putative agglutination/immobilization antigen on the surface of Cryptocaryon irritans

Published online by Cambridge University Press:  20 April 2007

A. HATANAKA*
Affiliation:
Central Research Laboratories of Nippon Suisan Kaisha Ltd, 559-6 Kitano-Machi, Hachioji, Tokyo 192-0906, Japan
N. UMEDA
Affiliation:
Marine Biological Technology Center of Nippon Suisan Kaisha Ltd, 508-8 Ariakeura Tsurumi, Saiki-Shi, Oita 876-1204, Japan
S. YAMASHITA
Affiliation:
Central Research Laboratories of Nippon Suisan Kaisha Ltd, 559-6 Kitano-Machi, Hachioji, Tokyo 192-0906, Japan
N. HIRAZAWA
Affiliation:
Central Research Laboratories of Nippon Suisan Kaisha Ltd, 559-6 Kitano-Machi, Hachioji, Tokyo 192-0906, Japan
*
*Corresponding author: Central Research Laboratories of Nippon Suisan Kaisha Ltd, 559-6 Kitano-Machi, Hachioji, Tokyo 192-0906, Japan. Tel: +81 426 56 5195. Fax: +81 426 56 5188. E-mail: [email protected]

Summary

The ciliated protozoan Cryptocaryon irritans, a parasite of seawater fishes, was found to express an antigen that elicits antibodies in rabbits and tiger puffer (Takifugu ruburipes). Serum from rabbits and fish immunized with theronts had agglutination/immobilization activity against theronts in vitro; fish serum antibody levels (measured by enzyme-linked immunosorbent assays: ELISA) correlated with this activity. Anti-theront antibody levels in fish were significantly higher in the immunized group as compared with control fish at 2 weeks after booster immunization (injection of bovine serum albumin; Student's t-test, P<0·01). Biochemical analyses indicated that a Triton X-114-soluble 32 kDa theront integral membrane protein may be the agglutination/immobilization antigen. Indirect immunofluorescence staining of theronts suggested that this 32 kDa antigen was expressed on the surface of cilia. The full-length 32 kDa antigen cDNA contained 1147 basepairs, encoding a 328-amino acid protein including hydrophobic N- and C-termini. As with Tetrahymena and Paramecium spp., TAA and TAG appear to be used as glutamine codons in the 32 kDa antigen gene.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2007

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