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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
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1437-4315
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Volume 388, Issue 6 (Jun 2007)

Issues

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

Yi Zhang
  • 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.
  • Other articles by this author:
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/ Kai-Hui Wang
  • 2Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China
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/ Ying-Jun Guo
  • 3Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China
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/ Yi-Ming Lu
  • 4Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China
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/ Hong-Li Yan
  • 5Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China
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/ Yun-Long Song
  • 6Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China
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/ Fang Wang
  • 7Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China
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/ Fei-Xiang Ding
  • 8Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China
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/ Shu-Han Sun
  • 9Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai 200433, P.R. China
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Published Online: 2007-06-01 | DOI: https://doi.org/10.1515/BC.2007.071

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

About the article

Corresponding author


Received: 2007-02-05

Accepted: 2007-03-14

Published Online: 2007-06-01


Citation Information: Biological Chemistry, ISSN (Online) 14316730, ISSN (Print) 14374315, DOI: https://doi.org/10.1515/BC.2007.071.

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