@article {1161,
	title = {Molecular characterization of recombinant mus a 5 allergen from banana fruit.},
	journal = {Mol Biotechnol},
	volume = {56},
	year = {2014},
	month = {2014 Jun},
	pages = {498-506},
	abstract = {Allergy to banana fruit appears to have become an important cause of fruit allergy in Europe. Among five allergens that have been found, beta-1,3-glucanase denoted as Mus a 5 was identified as a candidate allergen for the component-resolved allergy diagnosis of banana allergy. Because of the variations in protein levels in banana fruit, in this study Mus a 5 was produced as a fusion protein with glutathione-S-transferase in Escherichia coli. The recombinant Mus a 5 was purified under native conditions by a combination of affinity, ion-exchange, and reversed phase chromatography. N-terminal sequence was confirmed by Edman degradation and 55~\% of the primary structure was identified by mass fingerprint, while the secondary structure was assessed by circular dichroism spectroscopy. IgG reactivity of recombinant protein was shown in 2-D immunoblot with anti-Mus a 5 antibodies, while IgG and IgE binding to natural Mus a 5 was inhibited with the recombinant Mus a 5 in immunoblot inhibition test. IgE reactivity of recombinant Mus a 5 was shown in ELISA within a group of ten persons sensitized to banana fruit. Recombinant Mus a 5 is a novel reagent suitable for the component-resolved allergy diagnosis of banana allergy.},
	issn = {1559-0305},
	doi = {10.1007/s12033-013-9719-8},
	author = {Mrkic, Ivan and Abughren, Mohamed and Nikolic, Jasna and Andjelkovic, Uros and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Petersen, Arnd and Papadopoulos, Nikolaos G and Gavrovic-Jankulovic, Marija}
}
