TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Burazer, Lidija
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1189
AB  - Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 mu g/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling post-harvest diseases and maintaining food quality.
PB  - Oxford : Pergamon-Elsevier Science Ltd
T2  - Phytochemistry
T1  - Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)
VL  - 94
SP  - 53
EP  - 59
DO  - 10.1016/j.phytochem.2013.06.006
ER  - 

@article{
author = "Popović, Milica and Anđelković, Uroš and Burazer, Lidija and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 mu g/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling post-harvest diseases and maintaining food quality.",
publisher = "Oxford : Pergamon-Elsevier Science Ltd",
journal = "Phytochemistry",
title = "Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)",
volume = "94",
pages = "53-59",
doi = "10.1016/j.phytochem.2013.06.006"
}

Popović, M., Anđelković, U., Burazer, L., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2013). Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry
Oxford : Pergamon-Elsevier Science Ltd., 94, 53-59.
https://doi.org/10.1016/j.phytochem.2013.06.006

Popović M, Anđelković U, Burazer L, Lindner B, Petersen A, Gavrović-Jankulović M. Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry. 2013;94:53-59.
doi:10.1016/j.phytochem.2013.06.006 .

Popović, Milica, Anđelković, Uroš, Burazer, Lidija, Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)" in Phytochemistry, 94 (2013):53-59,
https://doi.org/10.1016/j.phytochem.2013.06.006 . .

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 . .