Production of the matrix protein of Nipah virus in Escherichia coli: virus-like particles and possible application for diagnosis.
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.
Subramanian
Senthil Kumar
SK
Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia.
Tey
Beng Ti
BT
Hamid
Muhajir
M
Tan
Wen Siang
WS
D000818:Animals; D000914:Antibodies, Viral / Q000097:blood; D004196:Disease Outbreaks; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D045464:Henipavirus Infections / Q000175:diagnosis / Q000453:epidemiology / Q000662:veterinary* / Q000821:virology; D045405:Nipah Virus / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D013552:Swine; D013553:Swine Diseases / Q000175:diagnosis* / Q000453:epidemiology / Q000821:virology; D014763:Viral Matrix Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D014771:Virion / Q000378:metabolism* / Q000648:ultrastructure
D000914:Antibodies, Viral; D011994:Recombinant Proteins; D014763:Viral Matrix Proteins