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Purification of p24 protein expressed in Bacillus subtilis and evaluation of its immunogenicity in mice

Tuom Thi Tinh Truong 1, *
Trang Thi Phuong Phan 1
Hoang Duc Nguyen 1
  1. University of Science, VNU-HCM
Correspondence to: Tuom Thi Tinh Truong, University of Science, VNU-HCM. Email: Nghiado@sci.edu.vn.
Volume & Issue: Vol. 1 No. T1 (2017) | Page No.: 69-79 | DOI: 10.32508/stdjns.v1iT1.436
Published: 2017-03-31

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This article is published with open access by Viet Nam National University Ho Chi Minh City, Viet Nam. This article is distributed under the terms of the Creative Commons Attribution License (CC-BY 4.0) which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.

Abstract

p24 protein is a component of the HIV particle capsid. It plays an essential role in HIV to infect into the host cell and in the cycle life of virus. Therefore, this protein can be used in the orientative study “to create and produce HIV’s vaccine”. This study created the new Bacillus subtilis strain which expressed p24 protein. B. subtilis a safety and non-toxic bacteria strain for humans and animals, has system expression to allow over expression recombinant protein up to 10-30 % of total proteins. Plasmid pHT1537 was cloned successfully, containing lysSN-6his-gagp24 gene to encode p24 protein fused with LysSN protein and to allow the expression of p24 protein in B. subtilis by IPTG inducer. The target protein in the cell was cheked by SDS-PAGE. The p24 fused protein was parified from His Trap column which contained Ni2+. Evaluation of the ability to produce antibody against p24 protein in mice by ELISA and Western blot was caried out.

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