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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Annexin B1 from Taenia solium metacestodes is a newly characterized member of the annexin family

Yi Zhang1 / Kai-Hui Wang2 / Ying-Jun Guo3 / Yi-Ming Lu4 / Hong-Li Yan5 / Yun-Long Song6 / Fang Wang7 / Fei-Xiang Ding8 / Shu-Han Sun9

1Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China
The first two authors contributed equally to this work.

2Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China

3Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China

4Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China

5Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China

6Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China

7Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China

8Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China

9Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China

Corresponding author

Citation Information: Biological Chemistry. Volume 388, Issue 6, Pages 601–610, ISSN (Online) 14316730, ISSN (Print) 14374315, DOI: 10.1515/BC.2007.071, June 2007

Publication History:
Received:
2007-02-05
Accepted:
2007-03-14
Published Online:
2007-06-01

Abstract

We previously reported cloning of the Taenia solium annexin B1 gene from a metacestode cDNA expression library and demonstrated that it acts as a protective antigen for effective vaccine development against cysticercosis. In the present study we produced recombinant annexin B1 and antiserum against the protein to investigate its structural and functional properties. Western blotting of metacestode fractions indicated that T. solium annexin B1, similar to vertebrate annexins, associates with acid phospholipids in the presence of Ca2+. This property was confirmed by the recognition of apoptotic cells by labeled annexin B1. CD spectroscopy results demonstrated that α-helices are the main secondary structures of the protein. Ca2+ binding increases the α-helix content and causes significant thermal stabilization with a melting temperature increase of approximately 10°C. Functional Ca2+-dependent phospholipid binding sites of annexin B1 were investigated using mutant proteins. By changing a conserved acidic amino acid residue that putatively combines Ca2+ in each domain of annexin B1 singly or in combination, we found that Ca2+ binding in the first domain is more important than that at the other Ca2+ binding sites. Annexin B1 is a metacestode stage-specific antigen, with the protein being mainly localized in the teguments and surrounding cyst wall of T. solium metacestodes, suggesting a role in the parasite-host interaction.

Keywords: calcium binding; CD spectroscopy; mutagenesis; phospholipid binding; Taenia solium

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