The role of acidification of the medium on the erythrocyte agglutinating and adsorbing properties of blood group-specific monoclonal antibodies
Background : Studies on the specificity of ABH antigen-antibody interactions at different pH values are rare. Therefore, the aim of this study was to estimate the effect of acidification of the reacting medium on the agglutinating ability of anti-A monoclonal antibodies (mABs) and their inhibition b...
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| Format: | Article |
| Language: | English |
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Korean Society for Transplantation
2023-09-01
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| Series: | Korean Journal of Transplantation |
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| Online Access: | http://www.ekjt.org/journal/view.html?doi=10.4285/kjt.23.0033 |
| _version_ | 1797327337176432640 |
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| author | Yuriy Pavlovich Delevsky Olexandr Anatoliyovich Zinchenko |
| author_facet | Yuriy Pavlovich Delevsky Olexandr Anatoliyovich Zinchenko |
| author_sort | Yuriy Pavlovich Delevsky |
| collection | DOAJ |
| description | Background : Studies on the specificity of ABH antigen-antibody interactions at different pH values are rare. Therefore, the aim of this study was to estimate the effect of acidification of the reacting medium on the agglutinating ability of anti-A monoclonal antibodies (mABs) and their inhibition by glycoconjugates of red blood cell membranes. Methods : Anti-A mABs were obtained from the Fourth International Workshop on Monoclonal Antibodies Against Human Red Blood Cell and Related Antigens (on July 19-20, 2002, in Paris, France). The glycoconjugates were isolated from erythrocytes' membranes. The inhibition of the lipid and protein isotypes of the blood group A antigen was assessed. Results : The acidic medium decreased the agglutinating ability of acid immunoglobulin M (IgM) anti-A mABs, in contrast to alkaline immunoglobulin G (IgG) mABs. Meanwhile, at pH 6.5, IgM antibodies exhibited a high adsorption capacity, while IgG antibodies demonstrated a strong adsorption capacity at an alkaline pH. mABs 2-19, 2-28, 2-22, and 2-8 were inhibited by the acidic lipid and protein glycotopes of erythrocyte membranes. However, mAB 2-8 was inhibited by both acidic and alkaline glycotope variants. Conclusions: The agglutinating and adsorbing abilities of mABs, which are revealed at opposing pH values, should be taken into account during studies of antigen-antibody interactions. |
| first_indexed | 2024-03-08T06:36:47Z |
| format | Article |
| id | doaj.art-db4f9401a715413e9cf4a92db546a9ab |
| institution | Directory Open Access Journal |
| issn | 2671-8790 |
| language | English |
| last_indexed | 2024-03-08T06:36:47Z |
| publishDate | 2023-09-01 |
| publisher | Korean Society for Transplantation |
| record_format | Article |
| series | Korean Journal of Transplantation |
| spelling | doaj.art-db4f9401a715413e9cf4a92db546a9ab2024-02-03T09:52:56ZengKorean Society for TransplantationKorean Journal of Transplantation2671-87902023-09-0137318919610.4285/kjt.23.0033kjt.23.0033The role of acidification of the medium on the erythrocyte agglutinating and adsorbing properties of blood group-specific monoclonal antibodiesYuriy Pavlovich Delevsky0Olexandr Anatoliyovich Zinchenko1Sytenko Institute of Spine and Joint Pathology, National Academy of Medical Sciences of Ukraine, Kharkiv, UkraineUkrainian Scientific Pharmacopeial Center for the Quality of Medicines, Kharkiv, UkraineBackground : Studies on the specificity of ABH antigen-antibody interactions at different pH values are rare. Therefore, the aim of this study was to estimate the effect of acidification of the reacting medium on the agglutinating ability of anti-A monoclonal antibodies (mABs) and their inhibition by glycoconjugates of red blood cell membranes. Methods : Anti-A mABs were obtained from the Fourth International Workshop on Monoclonal Antibodies Against Human Red Blood Cell and Related Antigens (on July 19-20, 2002, in Paris, France). The glycoconjugates were isolated from erythrocytes' membranes. The inhibition of the lipid and protein isotypes of the blood group A antigen was assessed. Results : The acidic medium decreased the agglutinating ability of acid immunoglobulin M (IgM) anti-A mABs, in contrast to alkaline immunoglobulin G (IgG) mABs. Meanwhile, at pH 6.5, IgM antibodies exhibited a high adsorption capacity, while IgG antibodies demonstrated a strong adsorption capacity at an alkaline pH. mABs 2-19, 2-28, 2-22, and 2-8 were inhibited by the acidic lipid and protein glycotopes of erythrocyte membranes. However, mAB 2-8 was inhibited by both acidic and alkaline glycotope variants. Conclusions: The agglutinating and adsorbing abilities of mABs, which are revealed at opposing pH values, should be taken into account during studies of antigen-antibody interactions.http://www.ekjt.org/journal/view.html?doi=10.4285/kjt.23.0033antibody; adsorption; erythrocyte; transferase; charge |
| spellingShingle | Yuriy Pavlovich Delevsky Olexandr Anatoliyovich Zinchenko The role of acidification of the medium on the erythrocyte agglutinating and adsorbing properties of blood group-specific monoclonal antibodies Korean Journal of Transplantation antibody; adsorption; erythrocyte; transferase; charge |
| title | The role of acidification of the medium on the erythrocyte agglutinating and adsorbing properties of blood group-specific monoclonal antibodies |
| title_full | The role of acidification of the medium on the erythrocyte agglutinating and adsorbing properties of blood group-specific monoclonal antibodies |
| title_fullStr | The role of acidification of the medium on the erythrocyte agglutinating and adsorbing properties of blood group-specific monoclonal antibodies |
| title_full_unstemmed | The role of acidification of the medium on the erythrocyte agglutinating and adsorbing properties of blood group-specific monoclonal antibodies |
| title_short | The role of acidification of the medium on the erythrocyte agglutinating and adsorbing properties of blood group-specific monoclonal antibodies |
| title_sort | role of acidification of the medium on the erythrocyte agglutinating and adsorbing properties of blood group specific monoclonal antibodies |
| topic | antibody; adsorption; erythrocyte; transferase; charge |
| url | http://www.ekjt.org/journal/view.html?doi=10.4285/kjt.23.0033 |
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