Molecular and Sugar-Binding Heterogeneity of C-Type Lectins from Osmerus (Spirinchus) lanceolatus Eggs(Biochemistry/Molecular Biology)

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Two C-type lectins (OLLafs and OLLafl) were isolated from Osmerus (Spirinchus) lanceolatus eggs using asialofetuin-Sepharose column. OLLafs and OLLafl were eluted with 0.2M sucrose and 0.2M lactose from the same column, respectively. OLLafl has been estimated to be a heterodimeric protein composed of H- and L-subunit and involved C-type lectin like domain (CTLD). In this study we revealed that OLLafs was a homodimeric protein composed of L-subunit of OLLafl. Although adding EDTA diminished the hemagglutinating activity of OLLafs, the activity of OLLafl was not influenced. Recombinant lectins (rOLLafl-H and -L) and mutant lectins replaced Cys^<123, 131 and 136> with Ala (mOLLafl-L^<123, 131 and 136>) were established. The activity of mOLLafl-L^<136> was comparable to rOLLafl-L, and rOLLafl-H was 15 times lower than rOLLafl-L. On the other hand, the activity of mOLLafl-L^<123> and mOLLafl-L^<131> were lower than that of rOLLafl-H. Therefore, Cys^<136> may not participate in hemagglutinating activity of rOLLafl-L. In contrast, Cys^<123> and Cys^<131> may partially contribute this activity. Although hemagglutination inhibition profiles of rOLLafl-L, rOLLafl-H and mOLLafl-L^<136> were similar, mOLLafl-L^<131>-induced hemagglutination was not inhibited by any sugars tested even at a concentration of 150mM. Then, Cys^<131> may directly contribute to the sugar-binding capacity of OLLafl. Affinities of mOLLafl-L^<123> for these sugars were lower than the others. These results suggest that Cys^<136> might contribute to the intermolecular disulfide bond in the rOLLafl-L dimer, and that the intramolecular disulfide bond concerning Cys^<131> might important for lectin activity.
公益社団法人日本薬学会の論文
2005-05-01

Molecular and Sugar-Binding Heterogeneity of C-Type Lectins from Osmerus (Spirinchus) lanceolatus Eggs(Biochemistry/Molecular Biology)

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