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  - 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 . .