| Literature DB >> 26787154 |
Xingju Song1, Dandan Hu1, Xiuqin Zhong1, Ning Wang1, Xiaobin Gu1, Tao Wang1, Xuerong Peng1, Guangyou Yang2.
Abstract
Cystic echinococcosis, caused by Echinococcus granulosus, is a widespread parasitic zoonosis causing economic loss and public health problems. Annexins are important proteins usually present in the plasma membrane, but previous studies have shown that an annexin B33 protein of E. granulosus (Eg-ANX) could be detected in the excretory/secretory products and cyst fluid. In this study, we cloned and characterized Eg-ANX. In silico analysis showed that the amino acid sequence of Eg-ANX was conserved and lacked any signal peptides. The phospholipid-binding activity of recombinant Eg-ANX (rEg-ANX) was tested; liposomes could bind to rEg-ANX only in the presence of Ca(2+). In addition, we performed western blotting and immunohistochemical analyses to further validate the secretory properties of Eg-ANX. The protein could be detected in the cyst fluid of E. granulosus and was also present in the intermediate host tissues, which suggested that Eg-ANX might play an important role in parasite-host interaction. © The American Society of Tropical Medicine and Hygiene.Entities:
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Year: 2016 PMID: 26787154 PMCID: PMC4775900 DOI: 10.4269/ajtmh.15-0452
Source DB: PubMed Journal: Am J Trop Med Hyg ISSN: 0002-9637 Impact factor: 2.345