id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-270514-36k9xo7f	van der Woude, Roosmarijn	Drivers of recombinant soluble influenza A virus hemagglutinin and neuraminidase expression in mammalian cells	2020-08-14		.txt	text/plain	3966	249	49	Recombinant soluble trimeric influenza A virus hemagglutinins (HA) and tetrameric neuraminidases (NAs) have proven to be excellent tools to decipher biological properties. The two surface envelope proteins of IAV have opposing functions; the trimeric hemagglutinin (HA) binds to sialic acid containing glycans to enable the virus to enter cells, 1,2 the tetrameric neuraminidase (NA) cleaves sialic acids to release new viral particles from the membrane. However, we observed a significant increase in expression yields and determined that it reduced the use of expensive antibodies and provided an excellent handle, as well as an internal read out, of a glycan binding protein. The N-terminal sfGFP increases yields, maintains biological activity, structure and antigenicity, and aids protein quantitation during expression and purification. To determine that sfGFP-NA fusions are enzymatically, antigenically and structurally similar to their non-fused counterparts, we analyzed the GCN4, TB, and sfGFP-TB-N2 proteins with MUNANA and NA specific antibodies (Figure 3 ).	./cache/cord-270514-36k9xo7f.txt	./txt/cord-270514-36k9xo7f.txt