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Characterization of highly concentrated serum lectins in spotted halibut Verasper variegatus

Published online by Cambridge University Press:  13 December 2007

A. HATANAKA ,
N. UMEDA  and
N. HIRAZAWA
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
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: hatanaka@nissui.co.jp
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Summary

Mannose-binding lectins were purified from flatfish spotted halibut (Verasper variegatus) serum. These lectins, which we named VVL (Verasper variegatus lectin)-α (~33 kDa) and VVL-β (~30 kDa) (VVLs), under non-reducing SDS-PAGE, were surprisingly highly concentrated in serum (1·92±0·55 mg/ml; n=5), compared with other serum lectins. Both VVLs are heterodimers comprised of 2 types of subunit via inter-subunit disulfide bonds, and one subunit of VVL-α has a N-linked sugar chain. Based on N-terminal amino acid sequences, the nucleotide sequences of one subunit of VVL cDNAs were determined by 3′- and 5′-rapid amplification of the cDNA ends. The full-length VVL subunit cDNAs contained 489 bp, encoding an open reading frame of 163 amino acids. We found that VVLs bind to an ~8 kDa ciliary surface glycoprotein (a putative agglutination/immobilization antigen that we reported previously) of the fish parasite Neobenedenia girellae, and agglutinate this parasite in vitro.

Keywords

spotted halibutVerasper variegatesserum lectinagglutination/immobilizationfish parasiteNeobenedenia girellae
Type
Original Articles
Information
Parasitology , Volume 135 , Issue 3 , March 2008 , pp. 359 - 369
Copyright
Copyright © Cambridge University Press 2007

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