id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-312119-wzcas4zd	Lu, Ti	Mapping the neutralizing epitopes of F18 fimbrial adhesin subunit FedF of enterotoxigenic Escherichia coli (ETEC)	2019-02-06		.txt	text/plain	4588	224	43	A vaccine that induces broad immunity to prevent K88 and F18 fimbrial ETEC bacterial attachment and colonization in pig small intestines and to neutralize enterotoxin enterotoxicity would be effective for PWD. In this study, we in silico identified immunodominant epitopes from F18 FedF subunit, fused individual epitopes to protein carrier CfaB (a structural subunit of heterologous human ETEC fimbria CFA/I), immunized mice with each epitope fusion protein, measured mouse anti-F18 antibody response, and examined epitope-derived antibodies for neutralizing activities against F18 fimbria adherence to determine FedF neutralizing epitopes. Furthermore, CfaB-epitope fusions were examined as competitive agents to prevent anti-F18 antibodies from inhibiting adherence of F18fimbrial bacteria to pig intestine cell line IPEC-2. Competitive ELISA and bacteria adherence inhibition assay to show CfaB-epitope fusion proteins blocking binding of anti-F18 antiserum with F18 fimbriae or F18-fimbrial E. A tripartite fusion, FaeG-FedF-LT(192)A2:B, of enterotoxigenic Escherichia coli (ETEC) elicits antibodies that neutralize cholera toxin, inhibit adherence of K88 (F4) and F18 fimbriae, and protect pigs against K88ac/heat-labile toxin infection	./cache/cord-312119-wzcas4zd.txt	./txt/cord-312119-wzcas4zd.txt