Mapping Immunodominant Antibody Epitopes of Abrin
Abrin, a toxin isolated from the seeds of <i>Abrus precatorius</i> (jequirity pea) is considered a biological threat agent by the Center for Disease Control and Prevention. To date, there is no effective postexposure treatment for abrin poisoning, and efforts are being made to develop an...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-04-01
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| Series: | Antibodies |
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| Online Access: | https://www.mdpi.com/2073-4468/9/2/11 |
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| author | Ron Alcalay Reut Falach Yoav Gal Anita Sapoznikov Tamar Sabo Chanoch Kronman Ohad Mazor |
| author_facet | Ron Alcalay Reut Falach Yoav Gal Anita Sapoznikov Tamar Sabo Chanoch Kronman Ohad Mazor |
| author_sort | Ron Alcalay |
| collection | DOAJ |
| description | Abrin, a toxin isolated from the seeds of <i>Abrus precatorius</i> (jequirity pea) is considered a biological threat agent by the Center for Disease Control and Prevention. To date, there is no effective postexposure treatment for abrin poisoning, and efforts are being made to develop an efficient vaccine and measures for postexposure therapy. Epitope mapping is widely applied as an efficient tool for discovering the antigenic moieties of toxins, thus providing invaluable information needed for the development of vaccines and therapies. Aiming to identify the immunodominant epitopes of abrin, several neutralizing antiabrin polyclonal antibodies were screened using a set of 15-mer peptides spanning the amino acid sequence of either the A or B subunits of abrin. Analysis of the antibody-binding pattern revealed 11 linear epitopes for the A subunit and 14 epitopes for the B subunit that are located on the surface of the toxin and thus accessible for antibody interactions. Moreover, the spatial location of several of these epitopes suggests they may block the galactose-binding pockets or the catalytic domain, thus neutralizing the toxin. These findings provide useful information and suggest a possible strategy for the development and design of an improved abrin-based vaccine and therapeutic antibodies. |
| first_indexed | 2024-03-10T20:11:39Z |
| format | Article |
| id | doaj.art-a1f31c86cffa4374b4b8a2dedc30ca96 |
| institution | Directory Open Access Journal |
| issn | 2073-4468 |
| language | English |
| last_indexed | 2024-03-10T20:11:39Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibodies |
| spelling | doaj.art-a1f31c86cffa4374b4b8a2dedc30ca962023-11-19T22:52:49ZengMDPI AGAntibodies2073-44682020-04-01921110.3390/antib9020011Mapping Immunodominant Antibody Epitopes of AbrinRon Alcalay0Reut Falach1Yoav Gal2Anita Sapoznikov3Tamar Sabo4Chanoch Kronman5Ohad Mazor6Department of Biochemistry and Molecular Genetics, Israel Institute for Biological Research, Ness-Ziona 76100, IsraelDepartment of Biochemistry and Molecular Genetics, Israel Institute for Biological Research, Ness-Ziona 76100, IsraelDepartment of Biochemistry and Molecular Genetics, Israel Institute for Biological Research, Ness-Ziona 76100, IsraelDepartment of Biochemistry and Molecular Genetics, Israel Institute for Biological Research, Ness-Ziona 76100, IsraelDepartment of Biochemistry and Molecular Genetics, Israel Institute for Biological Research, Ness-Ziona 76100, IsraelDepartment of Biochemistry and Molecular Genetics, Israel Institute for Biological Research, Ness-Ziona 76100, IsraelDepartment of Infectious Diseases, Israel Institute for Biological Research, Ness-Ziona 76100, IsraelAbrin, a toxin isolated from the seeds of <i>Abrus precatorius</i> (jequirity pea) is considered a biological threat agent by the Center for Disease Control and Prevention. To date, there is no effective postexposure treatment for abrin poisoning, and efforts are being made to develop an efficient vaccine and measures for postexposure therapy. Epitope mapping is widely applied as an efficient tool for discovering the antigenic moieties of toxins, thus providing invaluable information needed for the development of vaccines and therapies. Aiming to identify the immunodominant epitopes of abrin, several neutralizing antiabrin polyclonal antibodies were screened using a set of 15-mer peptides spanning the amino acid sequence of either the A or B subunits of abrin. Analysis of the antibody-binding pattern revealed 11 linear epitopes for the A subunit and 14 epitopes for the B subunit that are located on the surface of the toxin and thus accessible for antibody interactions. Moreover, the spatial location of several of these epitopes suggests they may block the galactose-binding pockets or the catalytic domain, thus neutralizing the toxin. These findings provide useful information and suggest a possible strategy for the development and design of an improved abrin-based vaccine and therapeutic antibodies.https://www.mdpi.com/2073-4468/9/2/11abrintoxinpolyclonal antibodiesepitope mapping |
| spellingShingle | Ron Alcalay Reut Falach Yoav Gal Anita Sapoznikov Tamar Sabo Chanoch Kronman Ohad Mazor Mapping Immunodominant Antibody Epitopes of Abrin Antibodies abrin toxin polyclonal antibodies epitope mapping |
| title | Mapping Immunodominant Antibody Epitopes of Abrin |
| title_full | Mapping Immunodominant Antibody Epitopes of Abrin |
| title_fullStr | Mapping Immunodominant Antibody Epitopes of Abrin |
| title_full_unstemmed | Mapping Immunodominant Antibody Epitopes of Abrin |
| title_short | Mapping Immunodominant Antibody Epitopes of Abrin |
| title_sort | mapping immunodominant antibody epitopes of abrin |
| topic | abrin toxin polyclonal antibodies epitope mapping |
| url | https://www.mdpi.com/2073-4468/9/2/11 |
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