id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-257190-iesysf3l	Eshaghi, Majid	Purification of the extra-cellular domain of Nipah virus glycoprotein produced in Escherichia coli and possible application in diagnosis	2005-03-30		.txt	text/plain	2907	149	51	The purified protein showed significant reactivity with the antibodies present in the sera of NiV-infected swine, as demonstrated in Western blot analysis and enzyme-linked immunosorbent assay (ELISA). The purified product was used as the capturing antigen in an enzyme-linked immunosorbent assay (ELISA) to determine the presence of the anti-NiV antibodies in serum samples collected from naturally infected swine. It was found that the purified G protein reacted only with antibodies in NiV positive samples, suggesting a potential replacement for currently used whole virus antigen that requires containment facilities. An immunoreactive band of approximately 57 kDa was detected by the pooled anti-NiV sera on a Western blot (Fig. 1B) , confirming the expression of the recombinant G protein. In order to determine the specificity and sensitivity of the recombinant G protein as antigen for detecting antibodies in NiV positive swine sera a quantitive immunoassay was carried out.	./cache/cord-257190-iesysf3l.txt	./txt/cord-257190-iesysf3l.txt