By Topic

Development of a monoclonal antibody that is specific for the Rabies virus phosphoprotein

Sign In

Cookies must be enabled to login.After enabling cookies , please use refresh or reload or ctrl+f5 on the browser for the login options.

Formats Non-Member Member
$31 $13
Learn how you can qualify for the best price for this item!
Become an IEEE Member or Subscribe to
IEEE Xplore for exclusive pricing!
close button

puzzle piece

IEEE membership options for an individual and IEEE Xplore subscriptions for an organization offer the most affordable access to essential journal articles, conference papers, standards, eBooks, and eLearning courses.

Learn more about:

IEEE membership

IEEE Xplore subscriptions

7 Author(s)
Bin Zhao ; Dept. of Pharm. Eng., GuangDong Univ. of Technol., Guangzhou, China ; Hong Huang ; Si-si Zhu ; Su-qing Zhao
more authors

Objective: To develop a monoclonal antibodies against Rabies virus phosphoprotein (P), which has conserved domains, and such regions are potentially interesting targets for the diagnosis. Methodes: In the study, a rabies virus p gene coding for the rabies virus phosphoprotein was amplified by PCR and cloned into the expression vector pET32a (+). The recombinant protein was expressed in Escherichia coli, purified with a HisTrap FF crude prepacked column and used to produce mouse monoclonal antibodies (Mabs). The anti-P Mabs were purified and their specificity was tested by indirect ELISA. One specific Mab was further tested by Western blotting against recombinant P and immunofluorescence analysis on cell monolayers infected with rabies virus. Results: The recombinant viral phosphoprotein was successfully expressed as a 53.8 kDa fusion protein which corresponded to the whole protein of the rabies virus. Of the Mabs that were generated, one (4B5) was shown to be highly specific, and could be used to detect recombinant P and native P in the whole virus. Conclusion: The use of a P protein obtained from heterologous expression in E. coli allowed the development of a Mab that interacted specifically with the P protein. This Mab should be useful for future studies with the rabies virus.

Published in:

IT in Medicine and Education (ITME), 2011 International Symposium on  (Volume:2 )

Date of Conference:

9-11 Dec. 2011