id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-269862-krcu3hfa	Wang, Shui-Mei	APOBEC3G cytidine deaminase association with coronavirus nucleocapsid protein	2009-05-25		.txt	text/plain	6895	379	58	We previously demonstrated that HIV-1 Gag mutants containing severe acute respiratory syndrome coronavirus nucleocapsid (SARS-CoV N) coding sequences as NC substitutes can effectively assemble VLPs . Given that SARS-CoV N possesses a RNA-binding property, it is likely that assembly-competent chimeras containing a replacement of HIV-1 NC by an SARS-CoV N sequence may support the incorporation of hA3G into VLPs. Here we demonstrate that the carboxyl-terminal half of the SARS-CoV or human coronavirus 229E (HCoV-229E) N protein not only enables efficient VLP production, but also confers the ability to efficiently package human APOBEC3G (hA3G) when substituted for HIV-1 NC. As the results in Fig. 6B indicate, the carboxyl-terminal half of HCoV-229E N (which also contains a putative self-association domain) (Tswen-Kei Tang, 2005) was capable of replacing the HIV-1 NC function with respect to VLP assembly and hA3G packaging-that is, substantial amounts of VLPs and hA3G were detected in NC(229EN2) transfectant supernatant (lane 4).	./cache/cord-269862-krcu3hfa.txt	./txt/cord-269862-krcu3hfa.txt