Cloning and functional identification of a novel annexin subfamily in Cysticercus cellulosae.

A novel cDNA was isolated from a library of Cysticercus cellulosae by immunological screening. Sequence analysis reveals that it has typical annexin structures. However, since its N-terminus is distinct and the core domain only has 32-44% amino acid identity to the tetrads of other annexins, the cDNA encodes a member of a novel annexin subfamily, which is designed as annexin B1. The recombinant protein, GST-anxB1, has the phospholipid-binding property and anticoagulatant activity common to annexins.