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ZIKV Envelope Domain-Specific Antibodies: Production, Purification and Characterization
Infection with Zika virus (ZIKV) came first to public attention after it was found to be associated with congenital microcephaly during the outbreak in Brazil (2015–2016). Diagnosis of ZIKV suffers from extensive cross-reactivity with other Flaviviruses, which are circulating in many ZIKV epidemic a...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6723789/ https://www.ncbi.nlm.nih.gov/pubmed/31412626 http://dx.doi.org/10.3390/v11080748 |
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author | Akhras, Sami Herrlein, Marie-Luise Elgner, Fabian Holzhauser, Thomas Hildt, Eberhard |
author_facet | Akhras, Sami Herrlein, Marie-Luise Elgner, Fabian Holzhauser, Thomas Hildt, Eberhard |
author_sort | Akhras, Sami |
collection | PubMed |
description | Infection with Zika virus (ZIKV) came first to public attention after it was found to be associated with congenital microcephaly during the outbreak in Brazil (2015–2016). Diagnosis of ZIKV suffers from extensive cross-reactivity with other Flaviviruses, which are circulating in many ZIKV epidemic areas. Due to the fatal outcome of ZIKV infection during pregnancy, detailed knowledge about neutralizing and non-neutralizing epitopes is crucial for the development of robust detection systems of protective antibodies. Therefore, additional information about ZIKV immunogenicity and antibody response is required. In this project, we report the production, purification and characterization of six different polyclonal antibodies against ZIKV envelope (E) protein. The produced antibodies bind to isolated ZIKV E protein as well as to the surface of ZIKV particles, interestingly without being potently neutralizing. Surface plasmon resonance measurement showed that these antibodies bind with high affinity to ZIKV E protein. Epitope mapping revealed that the epitopes are distributed among the three ZIKV E domains with seven binding sites. These identified binding sites overlap only partially with the previously described epitopes recognized by neutralizing antibodies, which is in accordance with their lack of potent neutralizing activity. Additionally, these antibodies showed neither cross-reactivity nor potent neutralizing activity against West Nile virus, a related flavivirus. The gained set of data helps to extend our understanding about the distribution of neutralizing and non-/weak-neutralizing epitopes in ZIKV E protein, and provides a rationale for ZIKV vaccine design and development of robust detection assays for neutralizing antibodies. |
format | Online Article Text |
id | pubmed-6723789 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-67237892019-09-10 ZIKV Envelope Domain-Specific Antibodies: Production, Purification and Characterization Akhras, Sami Herrlein, Marie-Luise Elgner, Fabian Holzhauser, Thomas Hildt, Eberhard Viruses Article Infection with Zika virus (ZIKV) came first to public attention after it was found to be associated with congenital microcephaly during the outbreak in Brazil (2015–2016). Diagnosis of ZIKV suffers from extensive cross-reactivity with other Flaviviruses, which are circulating in many ZIKV epidemic areas. Due to the fatal outcome of ZIKV infection during pregnancy, detailed knowledge about neutralizing and non-neutralizing epitopes is crucial for the development of robust detection systems of protective antibodies. Therefore, additional information about ZIKV immunogenicity and antibody response is required. In this project, we report the production, purification and characterization of six different polyclonal antibodies against ZIKV envelope (E) protein. The produced antibodies bind to isolated ZIKV E protein as well as to the surface of ZIKV particles, interestingly without being potently neutralizing. Surface plasmon resonance measurement showed that these antibodies bind with high affinity to ZIKV E protein. Epitope mapping revealed that the epitopes are distributed among the three ZIKV E domains with seven binding sites. These identified binding sites overlap only partially with the previously described epitopes recognized by neutralizing antibodies, which is in accordance with their lack of potent neutralizing activity. Additionally, these antibodies showed neither cross-reactivity nor potent neutralizing activity against West Nile virus, a related flavivirus. The gained set of data helps to extend our understanding about the distribution of neutralizing and non-/weak-neutralizing epitopes in ZIKV E protein, and provides a rationale for ZIKV vaccine design and development of robust detection assays for neutralizing antibodies. MDPI 2019-08-13 /pmc/articles/PMC6723789/ /pubmed/31412626 http://dx.doi.org/10.3390/v11080748 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Akhras, Sami Herrlein, Marie-Luise Elgner, Fabian Holzhauser, Thomas Hildt, Eberhard ZIKV Envelope Domain-Specific Antibodies: Production, Purification and Characterization |
title | ZIKV Envelope Domain-Specific Antibodies: Production, Purification and Characterization |
title_full | ZIKV Envelope Domain-Specific Antibodies: Production, Purification and Characterization |
title_fullStr | ZIKV Envelope Domain-Specific Antibodies: Production, Purification and Characterization |
title_full_unstemmed | ZIKV Envelope Domain-Specific Antibodies: Production, Purification and Characterization |
title_short | ZIKV Envelope Domain-Specific Antibodies: Production, Purification and Characterization |
title_sort | zikv envelope domain-specific antibodies: production, purification and characterization |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6723789/ https://www.ncbi.nlm.nih.gov/pubmed/31412626 http://dx.doi.org/10.3390/v11080748 |
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