Abstract |
The genus Henipavirus in the family Paramyxoviridae compromises two newly identified dangerous pathogens, Nipah virus and Hendra virus. Phosphoprotein of the two viruses is one of the major immunodominant antigens and the most divergent protein in the viral genomes. We have now expressed two pairs of truncated phosphoproteins of the two viruses in Escherichia coli in a soluble form using a vector tailored from pET32a. The truncated recombinant phosphoproteins were purified with His-Tag affinity chromatography and their antigenicity was determined by western blotting and ELISA. The longer pair of truncated recombinant phosphoproteins, covering amino acid residues 4-550, was more antigenic than the shorter one and of potential utility in the serological differentiation of henipavirus infections.
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Authors | Ji-Ming Chen, Koon Chu Yaiw, Meng Yu, Lin-Fa Wang, Qing-Hua Wang, Gary Crameri, Zhi-Liang Wang |
Journal | Biotechnology letters
(Biotechnol Lett)
Vol. 29
Issue 6
Pg. 871-5
(Jun 2007)
ISSN: 0141-5492 [Print] Netherlands |
PMID | 17322967
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Phosphoproteins
- Recombinant Proteins
- Viral Proteins
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Topics |
- Blotting, Western
- Enzyme-Linked Immunosorbent Assay
- Escherichia coli
(genetics, metabolism)
- Gene Expression
- Hendra Virus
(genetics, metabolism)
- Mutation
- Nipah Virus
(genetics, metabolism)
- Phosphoproteins
(genetics, immunology, metabolism)
- Recombinant Proteins
(genetics, immunology, metabolism)
- Species Specificity
- Viral Proteins
(genetics, immunology, metabolism)
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