INTERACTION OF RECOMBINANT DIPHTHERIA TOXOIDS WITH CELLULAR RECEPTORS in vitro
The aim of the research was to compare in vitro characteristics of reception of the natural diphtheria toxin — DT and its nontoxic recombinant analogs — toxoids. For assessing ligand-receptor interaction the method of immunoenzyme analysis and ELISA was used, where the bonding layer recombinant anal...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry
2016-06-01
|
| Series: | Biotechnologia Acta |
| Subjects: | |
| Online Access: | http://biotechnology.kiev.ua/images/storage/3_2016/manoilov_3_2016.pdf |
| _version_ | 1827854264552128512 |
|---|---|
| author | K. Yu. Manoilov A. Ju. Labyntsev N. V. Korotkevych D. V. Kolibo S. V. Komisarenko |
| author_facet | K. Yu. Manoilov A. Ju. Labyntsev N. V. Korotkevych D. V. Kolibo S. V. Komisarenko |
| author_sort | K. Yu. Manoilov |
| collection | DOAJ |
| description | The aim of the research was to compare in vitro characteristics of reception of the natural diphtheria toxin — DT and its nontoxic recombinant analogs — toxoids. For assessing ligand-receptor interaction the method of immunoenzyme analysis and ELISA was used, where the bonding layer recombinant analogues of diphtheria toxin cell receptor HB-EGF from sensitive and resistant to the toxin of the organisms were served. According to the results of ELISA the natural diphtheria toxin, in contrast to recombinant toxoids — CRM197, and B subunit, interacted with mouse HB-EGF with a very low affinity. While human HB-EGF with an equally high affinity connected as toxoids as native diphtheria toxin. Therefore, the analyzed recombinant analogs of toxin obtained in E. coli cells did not reproduce in full measure the receptor specificity of the natural toxin, which should be considered in the case of using these proteins as biotech products. |
| first_indexed | 2024-03-12T11:19:04Z |
| format | Article |
| id | doaj.art-bc151873da42483690c2ccbdb92df162 |
| institution | Directory Open Access Journal |
| issn | 2410-7751 2410-776X |
| language | English |
| last_indexed | 2024-03-12T11:19:04Z |
| publishDate | 2016-06-01 |
| publisher | National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry |
| record_format | Article |
| series | Biotechnologia Acta |
| spelling | doaj.art-bc151873da42483690c2ccbdb92df1622023-09-02T01:24:48ZengNational Academy of Sciences of Ukraine, Palladin Institute of BiochemistryBiotechnologia Acta2410-77512410-776X2016-06-01934451http://dx.doi.org/10.15407/biotech9.03.044:INTERACTION OF RECOMBINANT DIPHTHERIA TOXOIDS WITH CELLULAR RECEPTORS in vitroK. Yu. Manoilov0A. Ju. Labyntsev1 N. V. Korotkevych2D. V. Kolibo3S. V. Komisarenko4Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, KyivPalladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, KyivPalladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, KyivPalladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, KyivPalladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, KyivThe aim of the research was to compare in vitro characteristics of reception of the natural diphtheria toxin — DT and its nontoxic recombinant analogs — toxoids. For assessing ligand-receptor interaction the method of immunoenzyme analysis and ELISA was used, where the bonding layer recombinant analogues of diphtheria toxin cell receptor HB-EGF from sensitive and resistant to the toxin of the organisms were served. According to the results of ELISA the natural diphtheria toxin, in contrast to recombinant toxoids — CRM197, and B subunit, interacted with mouse HB-EGF with a very low affinity. While human HB-EGF with an equally high affinity connected as toxoids as native diphtheria toxin. Therefore, the analyzed recombinant analogs of toxin obtained in E. coli cells did not reproduce in full measure the receptor specificity of the natural toxin, which should be considered in the case of using these proteins as biotech products.http://biotechnology.kiev.ua/images/storage/3_2016/manoilov_3_2016.pdfdiphtheria toxinB subunit of diphtheria toxinCRM197HB-EGF |
| spellingShingle | K. Yu. Manoilov A. Ju. Labyntsev N. V. Korotkevych D. V. Kolibo S. V. Komisarenko INTERACTION OF RECOMBINANT DIPHTHERIA TOXOIDS WITH CELLULAR RECEPTORS in vitro Biotechnologia Acta diphtheria toxin B subunit of diphtheria toxin CRM197 HB-EGF |
| title | INTERACTION OF RECOMBINANT DIPHTHERIA TOXOIDS WITH CELLULAR RECEPTORS in vitro |
| title_full | INTERACTION OF RECOMBINANT DIPHTHERIA TOXOIDS WITH CELLULAR RECEPTORS in vitro |
| title_fullStr | INTERACTION OF RECOMBINANT DIPHTHERIA TOXOIDS WITH CELLULAR RECEPTORS in vitro |
| title_full_unstemmed | INTERACTION OF RECOMBINANT DIPHTHERIA TOXOIDS WITH CELLULAR RECEPTORS in vitro |
| title_short | INTERACTION OF RECOMBINANT DIPHTHERIA TOXOIDS WITH CELLULAR RECEPTORS in vitro |
| title_sort | interaction of recombinant diphtheria toxoids with cellular receptors in vitro |
| topic | diphtheria toxin B subunit of diphtheria toxin CRM197 HB-EGF |
| url | http://biotechnology.kiev.ua/images/storage/3_2016/manoilov_3_2016.pdf |
| work_keys_str_mv | AT kyumanoilov interactionofrecombinantdiphtheriatoxoidswithcellularreceptorsinvitro AT ajulabyntsev interactionofrecombinantdiphtheriatoxoidswithcellularreceptorsinvitro AT nvkorotkevych interactionofrecombinantdiphtheriatoxoidswithcellularreceptorsinvitro AT dvkolibo interactionofrecombinantdiphtheriatoxoidswithcellularreceptorsinvitro AT svkomisarenko interactionofrecombinantdiphtheriatoxoidswithcellularreceptorsinvitro |