Dimitrijević, Rajna

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  • Dimitrijević, Rajna (2)
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Author's Bibliography

Molecular and immunological characterization of Mus a 5 allergen from banana fruit

Aleksić, Ivana; Popović, Milica; Dimitrijević, Rajna; Anđelković, Uroš; Vassilopoulou, Emilia; Sinaniotis, Athanassios; Atanasković-Marković, Marina; Lindner, Buko; Petersen, Arnd; Papadopoulos, Nikolaos G.; Gavrović-Jankulović, Marija

(Wiley-Blackwell, Malden, 2012)

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1024
AB  - Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.
PB  - Wiley-Blackwell, Malden
T2  - Molecular Nutrition & Food Research
T1  - Molecular and immunological characterization of Mus a 5 allergen from banana fruit
VL  - 56
IS  - 3
SP  - 446
EP  - 453
DO  - 10.1002/mnfr.201100541
ER  - 
@article{
author = "Aleksić, Ivana and Popović, Milica and Dimitrijević, Rajna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.",
publisher = "Wiley-Blackwell, Malden",
journal = "Molecular Nutrition & Food Research",
title = "Molecular and immunological characterization of Mus a 5 allergen from banana fruit",
volume = "56",
number = "3",
pages = "446-453",
doi = "10.1002/mnfr.201100541"
}
Aleksić, I., Popović, M., Dimitrijević, R., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Atanasković-Marković, M., Lindner, B., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2012). Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition & Food Research
Wiley-Blackwell, Malden., 56(3), 446-453.
https://doi.org/10.1002/mnfr.201100541
Aleksić I, Popović M, Dimitrijević R, Anđelković U, Vassilopoulou E, Sinaniotis A, Atanasković-Marković M, Lindner B, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition & Food Research. 2012;56(3):446-453.
doi:10.1002/mnfr.201100541 .
Aleksić, Ivana, Popović, Milica, Dimitrijević, Rajna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular and immunological characterization of Mus a 5 allergen from banana fruit" in Molecular Nutrition & Food Research, 56, no. 3 (2012):446-453,
https://doi.org/10.1002/mnfr.201100541 . .
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Evaluation of the thermal stability and digestibility of heterologously produced banana lectin

Dimitrijević, Rajna; Jadranin, Milka; Burazer, Lidija; Ostojić, Sanja; Gavrović-Jankulović, Marija

(Elsevier Sci Ltd, Oxford, 2010)

TY  - JOUR
AU  - Dimitrijević, Rajna
AU  - Jadranin, Milka
AU  - Burazer, Lidija
AU  - Ostojić, Sanja
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/743
AB  - The thermal stability of recombinant mannose-specific banana lectin (rBanLec), as well as its stability under conditions of simulated gastro-intestinal fluid (SGF), was investigated. rBanLec was heterologously produced in Escherichia coli, Molecular mass of rBanLec, assessed by ESI-TOF mass spectrometry, was 15972.2 Da. Thermodynamic parameters for rBanLec denaturation, obtained by differential scanning calorimetry (DSC), revealed a transition maximum temperature (T-m) of 60.8 degrees C, calorimetric enthalpy (H-cal) of 136.17 kcal/mol and van't Hoff enthalpy (H-VH) of 50.27 kcal/mol. rBanLec was stable following an incubation for 2 h in SGF, and then for I h, in the simulated intestinal fluid (SIF). Intact primary structure, biological and immunological reactivity of rBanLec were all preserved following treatment under SGF and SIF conditions. In conclusion, rBanLec is a good candidate for the novel bioadhesive lectin-based drug delivery systems to the gastro-intestinal tract (GIT).
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Evaluation of the thermal stability and digestibility of heterologously produced banana lectin
VL  - 120
IS  - 4
SP  - 1113
EP  - 1118
DO  - 10.1016/j.foodchem.2009.11.062
ER  - 
@article{
author = "Dimitrijević, Rajna and Jadranin, Milka and Burazer, Lidija and Ostojić, Sanja and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "The thermal stability of recombinant mannose-specific banana lectin (rBanLec), as well as its stability under conditions of simulated gastro-intestinal fluid (SGF), was investigated. rBanLec was heterologously produced in Escherichia coli, Molecular mass of rBanLec, assessed by ESI-TOF mass spectrometry, was 15972.2 Da. Thermodynamic parameters for rBanLec denaturation, obtained by differential scanning calorimetry (DSC), revealed a transition maximum temperature (T-m) of 60.8 degrees C, calorimetric enthalpy (H-cal) of 136.17 kcal/mol and van't Hoff enthalpy (H-VH) of 50.27 kcal/mol. rBanLec was stable following an incubation for 2 h in SGF, and then for I h, in the simulated intestinal fluid (SIF). Intact primary structure, biological and immunological reactivity of rBanLec were all preserved following treatment under SGF and SIF conditions. In conclusion, rBanLec is a good candidate for the novel bioadhesive lectin-based drug delivery systems to the gastro-intestinal tract (GIT).",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Evaluation of the thermal stability and digestibility of heterologously produced banana lectin",
volume = "120",
number = "4",
pages = "1113-1118",
doi = "10.1016/j.foodchem.2009.11.062"
}
Dimitrijević, R., Jadranin, M., Burazer, L., Ostojić, S.,& Gavrović-Jankulović, M.. (2010). Evaluation of the thermal stability and digestibility of heterologously produced banana lectin. in Food Chemistry
Elsevier Sci Ltd, Oxford., 120(4), 1113-1118.
https://doi.org/10.1016/j.foodchem.2009.11.062
Dimitrijević R, Jadranin M, Burazer L, Ostojić S, Gavrović-Jankulović M. Evaluation of the thermal stability and digestibility of heterologously produced banana lectin. in Food Chemistry. 2010;120(4):1113-1118.
doi:10.1016/j.foodchem.2009.11.062 .
Dimitrijević, Rajna, Jadranin, Milka, Burazer, Lidija, Ostojić, Sanja, Gavrović-Jankulović, Marija, "Evaluation of the thermal stability and digestibility of heterologously produced banana lectin" in Food Chemistry, 120, no. 4 (2010):1113-1118,
https://doi.org/10.1016/j.foodchem.2009.11.062 . .
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