@article{2981530,
    title = "Molecular characterization of recombinant Mus a 5 allergen from banana fruit",
    author = "Mrkic, I. and Abughren, M. and Nikolic, J. and Andjelkovic, U. and Vassilopoulou, E. and Sinaniotis, A. and Petersen, A. and Papadopoulos, N.G. and Gavrovic-Jankulovic, M.",
    journal = "Molecular Biotechnology",
    year = "2014",
    volume = "56",
    number = "6",
    pages = "498-506",
    publisher = "Humana Press Inc.",
    issn = "1073-6085, 1559-0305",
    doi = "10.1007/s12033-013-9719-8",
    keywords = "Allergens;  Circular dichroism spectroscopy;  Escherichia coli;  Fruits;  Ion exchange;  Proteins, Food allergies;  Glucanase;  Glutathione-S-transferase;  IgE reactivities;  Molecular characterization;  Mus a 5;  Reversed phase chromatography;  Secondary structures, Allergies, allergen;  immunoglobulin E;  immunoglobulin G;  recombinant allergen;  recombinant mus a 5;  recombinant protein;  unclassified drug;  allergen;  glucan 1,3 beta glucosidase, affinity chromatography;  amino acid sequence;  amino terminal sequence;  article;  banana;  circular dichroism;  degradation kinetics;  enzyme linked immunosorbent assay;  immunoblotting;  immunoglobulin structure;  immunoreactivity;  ion exchange chromatography;  molecular dynamics;  nucleotide sequence;  protein secondary structure;  reversed phase liquid chromatography;  animal;  Europe;  food allergy;  fruit;  genetics;  human;  immunology;  mouse;  Musa, Escherichia coli, Allergens;  Amino Acid Sequence;  Animals;  Europe;  Food Hypersensitivity;  Fruit;  Glucan 1,3-beta-Glucosidase;  Humans;  Mice;  Musa;  Recombinant Proteins",
    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. © 2013 Springer Science+Business Media."
}