Mrkić, Ivan

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orcid::0000-0002-0262-3741
  • Mrkić, Ivan (4)
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Author's Bibliography

Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy

Mrkić, Ivan; Minić, Rajna; Popović, Dragan; Zivkovic, Irena; Gavrović-Jankulović, Marija

(Oxford : Pergamon-Elsevier Science Ltd, 2018)

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Popović, Dragan
AU  - Zivkovic, Irena
AU  - Gavrović-Jankulović, Marija
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2380
AB  - Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.
PB  - Oxford : Pergamon-Elsevier Science Ltd
T2  - Life Sciences
T1  - Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy
VL  - 213
SP  - 158
EP  - 165
DO  - 10.1016/j.lfs.2018.10.036
ER  - 
@article{
author = "Mrkić, Ivan and Minić, Rajna and Popović, Dragan and Zivkovic, Irena and Gavrović-Jankulović, Marija",
year = "2018",
abstract = "Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.",
publisher = "Oxford : Pergamon-Elsevier Science Ltd",
journal = "Life Sciences",
title = "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy",
volume = "213",
pages = "158-165",
doi = "10.1016/j.lfs.2018.10.036"
}
Mrkić, I., Minić, R., Popović, D., Zivkovic, I.,& Gavrović-Jankulović, M.. (2018). Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences
Oxford : Pergamon-Elsevier Science Ltd., 213, 158-165.
https://doi.org/10.1016/j.lfs.2018.10.036
Mrkić I, Minić R, Popović D, Zivkovic I, Gavrović-Jankulović M. Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences. 2018;213:158-165.
doi:10.1016/j.lfs.2018.10.036 .
Mrkić, Ivan, Minić, Rajna, Popović, Dragan, Zivkovic, Irena, Gavrović-Jankulović, Marija, "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy" in Life Sciences, 213 (2018):158-165,
https://doi.org/10.1016/j.lfs.2018.10.036 . .
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Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy

Mrkić, Ivan; Minić, Rajna; Popović, Dragan; Zivkovic, Irena; Gavrović-Jankulović, Marija

(Oxford : Pergamon-Elsevier Science Ltd, 2018)

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Popović, Dragan
AU  - Zivkovic, Irena
AU  - Gavrović-Jankulović, Marija
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4288
AB  - Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.
PB  - Oxford : Pergamon-Elsevier Science Ltd
T2  - Life Sciences
T1  - Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy
VL  - 213
SP  - 158
EP  - 165
DO  - 10.1016/j.lfs.2018.10.036
ER  - 
@article{
author = "Mrkić, Ivan and Minić, Rajna and Popović, Dragan and Zivkovic, Irena and Gavrović-Jankulović, Marija",
year = "2018",
abstract = "Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.",
publisher = "Oxford : Pergamon-Elsevier Science Ltd",
journal = "Life Sciences",
title = "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy",
volume = "213",
pages = "158-165",
doi = "10.1016/j.lfs.2018.10.036"
}
Mrkić, I., Minić, R., Popović, D., Zivkovic, I.,& Gavrović-Jankulović, M.. (2018). Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences
Oxford : Pergamon-Elsevier Science Ltd., 213, 158-165.
https://doi.org/10.1016/j.lfs.2018.10.036
Mrkić I, Minić R, Popović D, Zivkovic I, Gavrović-Jankulović M. Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences. 2018;213:158-165.
doi:10.1016/j.lfs.2018.10.036 .
Mrkić, Ivan, Minić, Rajna, Popović, Dragan, Zivkovic, Irena, Gavrović-Jankulović, Marija, "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy" in Life Sciences, 213 (2018):158-165,
https://doi.org/10.1016/j.lfs.2018.10.036 . .
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Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit

Mrkić, Ivan; Abughren, Mohamed; Nikolić, Jasna; Anđelković, Uroš; Vassilopoulou, Emilia; Sinaniotis, Athanassios; Petersen, Arnd; Papadopoulos, Nikolaos G.; Gavrović-Jankulović, Marija

(Humana Press Inc, Totowa, 2014)

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Abughren, Mohamed
AU  - Nikolić, Jasna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1579
AB  - 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.
PB  - Humana Press Inc, Totowa
T2  - Molecular Biotechnology
T1  - Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit
VL  - 56
IS  - 6
SP  - 498
EP  - 506
DO  - 10.1007/s12033-013-9719-8
ER  - 
@article{
author = "Mrkić, Ivan and Abughren, Mohamed and Nikolić, Jasna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2014",
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.",
publisher = "Humana Press Inc, Totowa",
journal = "Molecular Biotechnology",
title = "Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit",
volume = "56",
number = "6",
pages = "498-506",
doi = "10.1007/s12033-013-9719-8"
}
Mrkić, I., Abughren, M., Nikolić, J., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2014). Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit. in Molecular Biotechnology
Humana Press Inc, Totowa., 56(6), 498-506.
https://doi.org/10.1007/s12033-013-9719-8
Mrkić I, Abughren M, Nikolić J, Anđelković U, Vassilopoulou E, Sinaniotis A, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit. in Molecular Biotechnology. 2014;56(6):498-506.
doi:10.1007/s12033-013-9719-8 .
Mrkić, Ivan, Abughren, Mohamed, Nikolić, Jasna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit" in Molecular Biotechnology, 56, no. 6 (2014):498-506,
https://doi.org/10.1007/s12033-013-9719-8 . .
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Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae)

Vujisić, Ljubodrag V.; Vučković, Ivan; Makarov, Slobodan E.; Ilic, Bojan S.; Antic, Dragan Z.; Jadranin, Milka; Todorović, Nina; Mrkić, Ivan; Vajs, Vlatka; Lučić, Luka; Curcic, Bozidar P. M.; Mitic, Bojan M.

(Springer, New York, 2013)

TY  - JOUR
AU  - Vujisić, Ljubodrag V.
AU  - Vučković, Ivan
AU  - Makarov, Slobodan E.
AU  - Ilic, Bojan S.
AU  - Antic, Dragan Z.
AU  - Jadranin, Milka
AU  - Todorović, Nina
AU  - Mrkić, Ivan
AU  - Vajs, Vlatka
AU  - Lučić, Luka
AU  - Curcic, Bozidar P. M.
AU  - Mitic, Bojan M.
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1177
AB  - The geophilomorph centipede, Himantarium gabrielis, when disturbed, discharges a viscous and proteinaceous secretion from the sternal glands. This exudate was found by gas chromatography-mass spectrometry, liquid chromatography-high resolution mass spectrometry, liquid chromatography-mass spectrometry-mass spectrometry and NMR analyses to be composed of hydrogen cyanide, benzaldehyde, benzoyl nitrile, benzyl nitrile, mandelonitrile, mandelonitrile benzoate, 3,7,6O-trimethylguanine (himantarine), farnesyl 2,3-dihydrofarnesoate and farnesyl farnesoate. This is the first report on the presence of benzyl nitrile and mandelonitrile benzoate in secreted substances from centipedes. Farnesyl 2,3-dihydrofarnesoate is a new compound, while himantarine and farnesyl farnesoate were not known as natural products. A post-secretion release of hydrogen cyanide by reaction of mandelonitrile and benzoyl nitrile was observed by NMR, and hydrogen cyanide signals were completely assigned. In addition, a protein component of the secretion was analysed by electrophoresis which revealed the presence of a major 55 kDa protein. Analyses of the defensive exudates of other geophilomorph families should produce further chemical surprises.
PB  - Springer, New York
T2  - Naturwissenschaften
T1  - Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae)
VL  - 100
IS  - 9
SP  - 861
EP  - 870
DO  - 10.1007/s00114-013-1086-6
ER  - 
@article{
author = "Vujisić, Ljubodrag V. and Vučković, Ivan and Makarov, Slobodan E. and Ilic, Bojan S. and Antic, Dragan Z. and Jadranin, Milka and Todorović, Nina and Mrkić, Ivan and Vajs, Vlatka and Lučić, Luka and Curcic, Bozidar P. M. and Mitic, Bojan M.",
year = "2013",
abstract = "The geophilomorph centipede, Himantarium gabrielis, when disturbed, discharges a viscous and proteinaceous secretion from the sternal glands. This exudate was found by gas chromatography-mass spectrometry, liquid chromatography-high resolution mass spectrometry, liquid chromatography-mass spectrometry-mass spectrometry and NMR analyses to be composed of hydrogen cyanide, benzaldehyde, benzoyl nitrile, benzyl nitrile, mandelonitrile, mandelonitrile benzoate, 3,7,6O-trimethylguanine (himantarine), farnesyl 2,3-dihydrofarnesoate and farnesyl farnesoate. This is the first report on the presence of benzyl nitrile and mandelonitrile benzoate in secreted substances from centipedes. Farnesyl 2,3-dihydrofarnesoate is a new compound, while himantarine and farnesyl farnesoate were not known as natural products. A post-secretion release of hydrogen cyanide by reaction of mandelonitrile and benzoyl nitrile was observed by NMR, and hydrogen cyanide signals were completely assigned. In addition, a protein component of the secretion was analysed by electrophoresis which revealed the presence of a major 55 kDa protein. Analyses of the defensive exudates of other geophilomorph families should produce further chemical surprises.",
publisher = "Springer, New York",
journal = "Naturwissenschaften",
title = "Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae)",
volume = "100",
number = "9",
pages = "861-870",
doi = "10.1007/s00114-013-1086-6"
}
Vujisić, L. V., Vučković, I., Makarov, S. E., Ilic, B. S., Antic, D. Z., Jadranin, M., Todorović, N., Mrkić, I., Vajs, V., Lučić, L., Curcic, B. P. M.,& Mitic, B. M.. (2013). Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae). in Naturwissenschaften
Springer, New York., 100(9), 861-870.
https://doi.org/10.1007/s00114-013-1086-6
Vujisić LV, Vučković I, Makarov SE, Ilic BS, Antic DZ, Jadranin M, Todorović N, Mrkić I, Vajs V, Lučić L, Curcic BPM, Mitic BM. Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae). in Naturwissenschaften. 2013;100(9):861-870.
doi:10.1007/s00114-013-1086-6 .
Vujisić, Ljubodrag V., Vučković, Ivan, Makarov, Slobodan E., Ilic, Bojan S., Antic, Dragan Z., Jadranin, Milka, Todorović, Nina, Mrkić, Ivan, Vajs, Vlatka, Lučić, Luka, Curcic, Bozidar P. M., Mitic, Bojan M., "Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae)" in Naturwissenschaften, 100, no. 9 (2013):861-870,
https://doi.org/10.1007/s00114-013-1086-6 . .
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