id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-103509-hynnba03	Wong, Ten-Tsao	A self-assembled protein nanoparticle serving as a one-shot vaccine carrier	2020-09-18		.txt	text/plain	3187	148	48	From these two clues, it was hypothesized that AH3-GFP fusion protein form stable protein complex through hydrophobic interaction mediated by N-terminal AH3 peptide. Using the same protocol, AH3-GFP was found to co-sedimented with the bacterial membrane (Fig. S3A) as well as the AH3-sfGFP-hM2e fusion protein but not a free GFP protein (Fig S3B) These results are consistent with our protein structure modeling that Arg11 serves as a main contact point for dimer stacking also it mediates the electrostatic interaction with mutated Glu13 (Fig. 3E ). These results suggest that the two point mutations of AH3 in I8L and K13E enable the formation of a stable, high antigenic protein complex that stimulates long lasting immune responses in a single immunization. The result suggests that although carrier protein AH3-sfGFP also has high antigenicity, it did not interfere with the immune response against the heterologous protein, hM2e (Fig. 5B, 5C) 	./cache/cord-103509-hynnba03.txt	./txt/cord-103509-hynnba03.txt