TY  - DATA
AU  - Smiljanić, Katarina
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6462
AB  - This research dataset encompasess the post-translational and protein modificatrion profiles of raw and roasted shrimpts done with tandem mass spectroscopy (Orbitrap Exploris 240) and processed with PEAKS X pro Studio, with its PTM engine. From these level of results (PEAKS PTM) an ptm profiling was extracted and presented here. An .rar file was created containing ptm profile of raw shirmp and prtm profile of the roasted shrimp in an excel format.
PB  - Univerzitet u Beogradu - Hemijski fakultet
T2  - Journal of Functional Foods
T1  - Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052
VL  - 113
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6462
ER  - 

@misc{
author = "Smiljanić, Katarina",
year = "2024",
abstract = "This research dataset encompasess the post-translational and protein modificatrion profiles of raw and roasted shrimpts done with tandem mass spectroscopy (Orbitrap Exploris 240) and processed with PEAKS X pro Studio, with its PTM engine. From these level of results (PEAKS PTM) an ptm profiling was extracted and presented here. An .rar file was created containing ptm profile of raw shirmp and prtm profile of the roasted shrimp in an excel format.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Journal of Functional Foods",
title = "Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052",
volume = "113",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6462"
}

Smiljanić, K.. (2024). Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052. in Journal of Functional Foods
Univerzitet u Beogradu - Hemijski fakultet., 113.
https://hdl.handle.net/21.15107/rcub_cherry_6462

Smiljanić K. Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052. in Journal of Functional Foods. 2024;113.
https://hdl.handle.net/21.15107/rcub_cherry_6462 .

Smiljanić, Katarina, "Research data for: Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods Elsevier., 113, 106052. https://doi.org/10.1016/j.jff.2024.106052" in Journal of Functional Foods, 113 (2024),
https://hdl.handle.net/21.15107/rcub_cherry_6462 .

TY  - CONF
AU  - MIhilović, Jelena
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5739
AB  - Peanut allergy affects approximately up to 3 % of children and up to 2 % of the adult world population, causing reactions ranging from mild to severe. Major peanut allergens are well characterized but little is known about their post-translational modifications and even less is known about the influence of thermal treatment on their profile. Protein post-translational modification patterns may differ between raw and thermally treated peanuts, which could affect its functional properties, such as allergic potential. In this study we combined proteomic and immunological methods to characterize the modifications or proteoforms of four major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in raw and roasted peanut. Bottom-up high-resolution accurate mass spectrometry and a specialized proteomics software package to identify, map and compare modifications of major peanut allergens between differently treated peanut kernels. Modification-specific antibody western blot was used to confirm the presence of modifications on major allergens in both extracts. Twenty different post-translational modifications in four prominent peanut allergens (Ara h 1-3, 6) were identified, while twelve were quantitatively compared between raw and roasted peanuts by high-resolution mass spectrometry and a proprietary proteomics software. post-translational modification specific antibodies confirmed the presence of these modifications in western-blots of raw and roasted peanuts. This study initiates appreciation of modifications and thermal processing affecting food quality, and development of state-of-the-art methodology in the risk assessment of allergen contamination.
C3  - FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia
T1  - Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications
SP  - 27
EP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5739
ER  - 

@conference{
author = "MIhilović, Jelena and Đukić, Teodora and Smiljanić, Katarina and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Peanut allergy affects approximately up to 3 % of children and up to 2 % of the adult world population, causing reactions ranging from mild to severe. Major peanut allergens are well characterized but little is known about their post-translational modifications and even less is known about the influence of thermal treatment on their profile. Protein post-translational modification patterns may differ between raw and thermally treated peanuts, which could affect its functional properties, such as allergic potential. In this study we combined proteomic and immunological methods to characterize the modifications or proteoforms of four major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in raw and roasted peanut. Bottom-up high-resolution accurate mass spectrometry and a specialized proteomics software package to identify, map and compare modifications of major peanut allergens between differently treated peanut kernels. Modification-specific antibody western blot was used to confirm the presence of modifications on major allergens in both extracts. Twenty different post-translational modifications in four prominent peanut allergens (Ara h 1-3, 6) were identified, while twelve were quantitatively compared between raw and roasted peanuts by high-resolution mass spectrometry and a proprietary proteomics software. post-translational modification specific antibodies confirmed the presence of these modifications in western-blots of raw and roasted peanuts. This study initiates appreciation of modifications and thermal processing affecting food quality, and development of state-of-the-art methodology in the risk assessment of allergen contamination.",
journal = "FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia",
title = "Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5739"
}

MIhilović, J., Đukić, T., Smiljanić, K., Apostolović, D., Liu, S., Epstein, M. M.,& Ćirković-Veličković, T.. (2021). Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia, 27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5739

MIhilović J, Đukić T, Smiljanić K, Apostolović D, Liu S, Epstein MM, Ćirković-Veličković T. Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia. 2021;:27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5739 .

MIhilović, Jelena, Đukić, Teodora, Smiljanić, Katarina, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., Ćirković-Veličković, Tanja, "Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications" in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia (2021):27-27,
https://hdl.handle.net/21.15107/rcub_cherry_5739 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5762
AB  - Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress
T1  - Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol
SP  - 126
EP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5762
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress",
title = "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol",
pages = "126-126",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5762"
}

Prodić, I., Smiljanić, K., Nagl, C., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress
Sociedade Portuguesa de Química., 126-126.
https://hdl.handle.net/21.15107/rcub_cherry_5762

Prodić I, Smiljanić K, Nagl C, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress. 2021;:126-126.
https://hdl.handle.net/21.15107/rcub_cherry_5762 .

Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol" in Book of Abstracts of the XXI EuroFoodChem Congress (2021):126-126,
https://hdl.handle.net/21.15107/rcub_cherry_5762 .

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2857
AB  - An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Elsevier
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
VL  - 126
SP  - 644
EP  - 658
DO  - 10.1016/j.envint.2019.03.001
ER  - 

@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Elsevier",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
volume = "126",
pages = "644-658",
doi = "10.1016/j.envint.2019.03.001"
}

Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International
Elsevier., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001

Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International. 2019;126:644-658.
doi:10.1016/j.envint.2019.03.001 .

Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress" in Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 . .