TY  - JOUR
AU  - Stanić, Dragana
AU  - Burazer, Lidija M.
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4327
AB  - Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen, a significant cause of hay fever all over Europe. Specific immunotherapy is the only treatment modality for allergic disease. Application of modified allergens makes the treatment safer and more efficient. In this work, two out of three (citraconic anhydride, cis-aconitic anhydride, 2,3-dimethylmaleic anhydride) tested anhydrides were proven to be suitable for chemical modifications of allergens. Art v 1 was modified by cis-aconitylation and citraconylation in order to obtain derivatives of Art v I that may be suitable for further immunological testing. Acylation of Art v 1 gave derivatives (caaArt v 1 and citArt v 1) with about 80 % modified ammo groups. The derivatives were in the monomeric form and had dramatically reduced pI values. Both derivatives were relatively stable at neutral pH values, while the acyl groups undergo hydrolysis under acidic conditions. Modification of allergens by cis-aconitylation and citraconylation could be a new tool for obtaining allergoids.
AB  - Art v1 je glavni alergen polena crnog pelina (Artemisia vulgaris), značajnog uzročnika polenske groznice širom Evrope. Alergen-specifična imunoterapija je za sada jedini delotvoran način za tretiranje alergija, pri čemu primena modifikovanih alergena čini ovakav tretman bezbednijim i efikasnijim. U ovom radu, dva od tri (anhidrid cis-akonitne, citrakonske i 2,3-dimetilmaleinske kiseline) ispitivana anhidrida su se pokazala pogodnim za hemijske modifikacije alergena. Art v 1 je modifikovan cis-akonitilovanjem i citrakonilovanjem u cilju dobijanja derivata Art v 1 pogodnih za dalje imunološke testove. Acilovanjem Art v 1 dobijeni su derivati (caaArt v 1 i citArt v 1) sa oko 80 % izmodifikovanih amino grupa. Dobijeni derivati su monomerni, sa molekulskom masom sličnom nativnom Art v 1, ali sa dramatično smanjenim pI vrednostima. Oba derivata su relativno stabilna u neutralnoj, dok se u kiseloj sredini acil grupe hidrolizuju. Modifikacija alergena cis-akonitilovanjem i citrakonilovanjem može biti novi način za dobijanje alergoida.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation
T1  - Hemijske modifikacije Art v 1, glavnog alergena Artemisia vulgaris, cis-akonitilovanjem i citrakonilovanjem
VL  - 74
IS  - 4
SP  - 359
EP  - 366
DO  - 10.2298/JSC0904359S
ER  - 

@article{
author = "Stanić, Dragana and Burazer, Lidija M. and Gavrović-Jankulović, Marija and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen, a significant cause of hay fever all over Europe. Specific immunotherapy is the only treatment modality for allergic disease. Application of modified allergens makes the treatment safer and more efficient. In this work, two out of three (citraconic anhydride, cis-aconitic anhydride, 2,3-dimethylmaleic anhydride) tested anhydrides were proven to be suitable for chemical modifications of allergens. Art v 1 was modified by cis-aconitylation and citraconylation in order to obtain derivatives of Art v I that may be suitable for further immunological testing. Acylation of Art v 1 gave derivatives (caaArt v 1 and citArt v 1) with about 80 % modified ammo groups. The derivatives were in the monomeric form and had dramatically reduced pI values. Both derivatives were relatively stable at neutral pH values, while the acyl groups undergo hydrolysis under acidic conditions. Modification of allergens by cis-aconitylation and citraconylation could be a new tool for obtaining allergoids., Art v1 je glavni alergen polena crnog pelina (Artemisia vulgaris), značajnog uzročnika polenske groznice širom Evrope. Alergen-specifična imunoterapija je za sada jedini delotvoran način za tretiranje alergija, pri čemu primena modifikovanih alergena čini ovakav tretman bezbednijim i efikasnijim. U ovom radu, dva od tri (anhidrid cis-akonitne, citrakonske i 2,3-dimetilmaleinske kiseline) ispitivana anhidrida su se pokazala pogodnim za hemijske modifikacije alergena. Art v 1 je modifikovan cis-akonitilovanjem i citrakonilovanjem u cilju dobijanja derivata Art v 1 pogodnih za dalje imunološke testove. Acilovanjem Art v 1 dobijeni su derivati (caaArt v 1 i citArt v 1) sa oko 80 % izmodifikovanih amino grupa. Dobijeni derivati su monomerni, sa molekulskom masom sličnom nativnom Art v 1, ali sa dramatično smanjenim pI vrednostima. Oba derivata su relativno stabilna u neutralnoj, dok se u kiseloj sredini acil grupe hidrolizuju. Modifikacija alergena cis-akonitilovanjem i citrakonilovanjem može biti novi način za dobijanje alergoida.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation, Hemijske modifikacije Art v 1, glavnog alergena Artemisia vulgaris, cis-akonitilovanjem i citrakonilovanjem",
volume = "74",
number = "4",
pages = "359-366",
doi = "10.2298/JSC0904359S"
}

Stanić, D., Burazer, L. M., Gavrović-Jankulović, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 74(4), 359-366.
https://doi.org/10.2298/JSC0904359S

Stanić D, Burazer LM, Gavrović-Jankulović M, Jankov RM, Ćirković-Veličković T. Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation. in Journal of the Serbian Chemical Society. 2009;74(4):359-366.
doi:10.2298/JSC0904359S .

Stanić, Dragana, Burazer, Lidija M., Gavrović-Jankulović, Marija, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation" in Journal of the Serbian Chemical Society, 74, no. 4 (2009):359-366,
https://doi.org/10.2298/JSC0904359S . .

TY  - JOUR
AU  - Perovic, I.
AU  - Milovanovic, M.
AU  - Stanić, Dragana
AU  - Burazer, Lidija M.
AU  - Petrović, D.
AU  - Milčić-Matić, Natalija
AU  - Gafvelin, Guro
AU  - van Hage, Marianne
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4324
AB  - Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.
PB  - Wiley-Blackwell Publishing, Inc, Malden
T2  - Clinical and Experimental Allergy
T1  - Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation
VL  - 39
IS  - 3
SP  - 435
EP  - 446
DO  - 10.1111/j.1365-2222.2008.03158.x
ER  - 

@article{
author = "Perovic, I. and Milovanovic, M. and Stanić, Dragana and Burazer, Lidija M. and Petrović, D. and Milčić-Matić, Natalija and Gafvelin, Guro and van Hage, Marianne and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Clinical and Experimental Allergy",
title = "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation",
volume = "39",
number = "3",
pages = "435-446",
doi = "10.1111/j.1365-2222.2008.03158.x"
}

Perovic, I., Milovanovic, M., Stanić, D., Burazer, L. M., Petrović, D., Milčić-Matić, N., Gafvelin, G., van Hage, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy
Wiley-Blackwell Publishing, Inc, Malden., 39(3), 435-446.
https://doi.org/10.1111/j.1365-2222.2008.03158.x

Perovic I, Milovanovic M, Stanić D, Burazer LM, Petrović D, Milčić-Matić N, Gafvelin G, van Hage M, Jankov RM, Ćirković-Veličković T. Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy. 2009;39(3):435-446.
doi:10.1111/j.1365-2222.2008.03158.x .

Perovic, I., Milovanovic, M., Stanić, Dragana, Burazer, Lidija M., Petrović, D., Milčić-Matić, Natalija, Gafvelin, Guro, van Hage, Marianne, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation" in Clinical and Experimental Allergy, 39, no. 3 (2009):435-446,
https://doi.org/10.1111/j.1365-2222.2008.03158.x . .

TY  - JOUR
AU  - Ahmedi, Khaled S. O. H
AU  - Milosavić, Nenad
AU  - Popović, Milica
AU  - Prodanović, Radivoje M.
AU  - Knežević-Jugović, Zorica D.
AU  - Jankov, Ratko M.
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4302
AB  - α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase.
AB  - Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae
T1  - Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae
VL  - 72
IS  - 12
SP  - 1255
EP  - 1263
DO  - 10.2298/JSC0712255A
ER  - 

@article{
author = "Ahmedi, Khaled S. O. H and Milosavić, Nenad and Popović, Milica and Prodanović, Radivoje M. and Knežević-Jugović, Zorica D. and Jankov, Ratko M.",
year = "2007",
abstract = "α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase., Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae, Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae",
volume = "72",
number = "12",
pages = "1255-1263",
doi = "10.2298/JSC0712255A"
}

Ahmedi, K. S. O. H., Milosavić, N., Popović, M., Prodanović, R. M., Knežević-Jugović, Z. D.,& Jankov, R. M.. (2007). Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 72(12), 1255-1263.
https://doi.org/10.2298/JSC0712255A

Ahmedi KSOH, Milosavić N, Popović M, Prodanović RM, Knežević-Jugović ZD, Jankov RM. Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society. 2007;72(12):1255-1263.
doi:10.2298/JSC0712255A .

Ahmedi, Khaled S. O. H, Milosavić, Nenad, Popović, Milica, Prodanović, Radivoje M., Knežević-Jugović, Zorica D., Jankov, Ratko M., "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae" in Journal of the Serbian Chemical Society, 72, no. 12 (2007):1255-1263,
https://doi.org/10.2298/JSC0712255A . .