Production of the matrix protein of nipah virus in escherichia coli: virus-like particles and possible application in diagnosis.

• Main Authors: Senthil, Kumar Subramanian, Tey, Beng Ti, Hamid, Muhajir, Tan, Wen Siang
• Format: Article
• Language: English
• Published: Elsevier Ltd. 2009
• Online Access: http://psasir.upm.edu.my/id/eprint/16364/
• Institution: Universiti Putra Malaysia

The broad species tropism of Nipah virus (NiV) coupled with its high pathogenicity demand a rapid search for a new biomarker candidate for diagnosis. The matrix (M) protein was expressed in Escherichia coli and purified using a Ni-NTA affinity column chromatography and sucrose density gradient centrifugation. The recombinant M protein with the molecular mass (Mr) of about 43 kDa was detected by anti-NiV serum and anti-myc antibody. About 50% of the M protein was found to be soluble and localized in cytoplasm when the cells were grown at 30 degrees C. Electron microscopic analysis showed that the purified M protein assembled into spherical particles of different sizes with diameters ranging from 20 to 50 nm. The purified M protein showed significant reactivity with the swine sera collected during the NiV outbreak, demonstrating its potential as a diagnostic reagent.