Secretion of Truncated Recombinant Rabies Virus Glycoprotein with Preserved Antigenic Properties Using a Co-Expression System in Hansenula polymorpha

Weidong Qian; Frank Aguilar; Ting Wang; Bingsheng Qiu

doi:10.1007/s12275-013-2337-0

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Research Support, Non-U.S. Gov't
Secretion of Truncated Recombinant Rabies Virus Glycoprotein with Preserved Antigenic Properties Using a Co-Expression System in Hansenula polymorpha: Weidong Qian ¹, Frank Aguilar ², Ting Wang ³, Bingsheng Qiu ⁴; Journal of Microbiology 2013;51(2):234-240.
DOI: https://doi.org/10.1007/s12275-013-2337-0
Published online: April 27, 2013

¹Life Science and Engineering School, Shaanxi University of Science and Technology, Xi’an 710021, P. R. China, ²Northwestern University, Chicago, IL, USA, ³Medical Technology and Engineering School, Henan University of Science and Technology, Luoyang 471003, P. R. China, ⁴Center for Agricultural Biotechnology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, P. R. China¹Life Science and Engineering School, Shaanxi University of Science and Technology, Xi’an 710021, P. R. China, ²Northwestern University, Chicago, IL, USA, ³Medical Technology and Engineering School, Henan University of Science and Technology, Luoyang 471003, P. R. China, ⁴Center for Agricultural Biotechnology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, P. R. China

Corresponding author: Bingsheng Qiu , Tel: +86-10-64807463,

Received: 4 July 2012 • Accepted: 5 October 2012

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Abstract

Rabies virus infection remains a serious public health threat in the developing world, where cost-concerns make widescale public health interventions impractical. The development of novel and inexpensive ELISA diagnostic antigens is critical in early detection and prevention of complications. The transmembrane glycoprotein (G) of rabies virus (RV) contains an external domain capable of inducing the synthesis of anti-rabies, virus-neutralizing antibodies, in infected or immunized hosts. In our study, the external G domain was synthesized and fused in-frame with a polyhistidine-tag coding sequence present in the expression plasmid. Soluble truncated recombinant G was secreted in Hansenula polymorpha (H. polymorpha) using H. polymorpha-derived calnexin (HpCNE1) overproduction and found to be correctly N-glycosylated. The truncated recombinant G was purified from cell culture supernatant by Ni-agarose affinity chromatography and when compared with the full-length glycoprotein, found to be similarly immunogenic in vaccinated rabbits. These results subsequently led us to explore the potential of truncated recombinant G as a diagnostic antigen in ELISA. Our results show that the truncated recombinant G can detect antibodies directed to both whole virion and native glycoprotein. More sophisticated applications of truncated recombinant G would profit from the correctly N-glycosylated and soluble monomer.

Keywords: Rabies virus;glycoprotein;secretion;Hansenula polymorpha

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Secretion of Truncated Recombinant Rabies Virus Glycoprotein with Preserved Antigenic Properties Using a Co-Expression System in Hansenula polymorpha

J. Microbiol. 2013;51(2):234-240. Published online April 27, 2013

DOI: https://doi.org/10.1007/s12275-013-2337-0

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