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.
Hongli
Yan
Y
Department of Medical Genetics, The Second Military Medical University, 800 Xiang Yin Road, 200433, Shanghai, People's Republic of China. y_hongli@yahoo.com
Shuhan
Sun
S
Ruiwen
Chen
C
Yingjun
Guo
G
D000595:Amino Acid Sequence; D000818:Animals; D017302:Annexins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D000925:Anticoagulants / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D003001:Cloning, Molecular; D003552:Cysticercus / Q000235:genetics*; D015723:Gene Library; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010743:Phospholipids / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013552:Swine / Q000276:immunology / Q000469:parasitology
D017302:Annexins; D000925:Anticoagulants; D015801:Helminth Proteins; D010743:Phospholipids; C449006:annexin B1, Taenia solium