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Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family
Birnaviridae is a family of viruses (birnaviruses) which consists of four genera, members of which cause diseases in fish, birds, mollusks, and insects. The genome of birnaviruses encodes the highly immunogenic VP2 capsid protein. In order to demonstrate that the VP2 protein can be exploited as a di...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7222154/ https://www.ncbi.nlm.nih.gov/pubmed/32088761 http://dx.doi.org/10.1007/s00253-020-10458-6 |
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author | Zafar, Maryam Shah, Majid Ali Shehzad, Aamir Tariq, Anam Habib, Mudasser Muddassar, Muhammad Shah, Muhammad Salahuddin Iqbal, Mazhar Hemmatzadeh, Farhid Rahman, Moazur |
author_facet | Zafar, Maryam Shah, Majid Ali Shehzad, Aamir Tariq, Anam Habib, Mudasser Muddassar, Muhammad Shah, Muhammad Salahuddin Iqbal, Mazhar Hemmatzadeh, Farhid Rahman, Moazur |
author_sort | Zafar, Maryam |
collection | PubMed |
description | Birnaviridae is a family of viruses (birnaviruses) which consists of four genera, members of which cause diseases in fish, birds, mollusks, and insects. The genome of birnaviruses encodes the highly immunogenic VP2 capsid protein. In order to demonstrate that the VP2 protein can be exploited as a diagnostic antigen for birnaviruses, we developed a lateral flow assay based on the surface-exposed VP2 protrusion domain of a representative birnavirus, infectious bursal disease virus (IBDV) of serotype 1 which causes the highly devastating infectious bursal disease in chickens. The biophysical characterization of the purified domain reveals that the domain predominantly consists of β-sheets, exists in a trimeric form, and remains folded at high temperatures, making it suitable for diagnostic purposes. Owing to its highly immunogenic nature and excellent biophysical properties, we employed the VP2 protrusion domain in a gold nanoparticle-based lateral flow assay for rapid detection of anti-IBDV antibodies in serum samples of infected chickens. Our results indicate that the domain binds anti-IBDV antibodies with high specificity during laboratory testing and on-site testing. The lateral flow assay reported here yields comparable results in a qualitative manner as obtained through a commercial enzyme-linked immunosorbent assay (ELISA). As VP2 is a common capsid protein of birnaviruses, the lateral flow assay can be generalized for other birnaviruses, and members of Tetraviridae and Nodaviridae families which contain homologous VP2 capsid proteins. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00253-020-10458-6) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-7222154 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-72221542020-05-14 Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family Zafar, Maryam Shah, Majid Ali Shehzad, Aamir Tariq, Anam Habib, Mudasser Muddassar, Muhammad Shah, Muhammad Salahuddin Iqbal, Mazhar Hemmatzadeh, Farhid Rahman, Moazur Appl Microbiol Biotechnol Biotechnologically Relevant Enzymes and Proteins Birnaviridae is a family of viruses (birnaviruses) which consists of four genera, members of which cause diseases in fish, birds, mollusks, and insects. The genome of birnaviruses encodes the highly immunogenic VP2 capsid protein. In order to demonstrate that the VP2 protein can be exploited as a diagnostic antigen for birnaviruses, we developed a lateral flow assay based on the surface-exposed VP2 protrusion domain of a representative birnavirus, infectious bursal disease virus (IBDV) of serotype 1 which causes the highly devastating infectious bursal disease in chickens. The biophysical characterization of the purified domain reveals that the domain predominantly consists of β-sheets, exists in a trimeric form, and remains folded at high temperatures, making it suitable for diagnostic purposes. Owing to its highly immunogenic nature and excellent biophysical properties, we employed the VP2 protrusion domain in a gold nanoparticle-based lateral flow assay for rapid detection of anti-IBDV antibodies in serum samples of infected chickens. Our results indicate that the domain binds anti-IBDV antibodies with high specificity during laboratory testing and on-site testing. The lateral flow assay reported here yields comparable results in a qualitative manner as obtained through a commercial enzyme-linked immunosorbent assay (ELISA). As VP2 is a common capsid protein of birnaviruses, the lateral flow assay can be generalized for other birnaviruses, and members of Tetraviridae and Nodaviridae families which contain homologous VP2 capsid proteins. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00253-020-10458-6) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2020-02-23 2020 /pmc/articles/PMC7222154/ /pubmed/32088761 http://dx.doi.org/10.1007/s00253-020-10458-6 Text en © Springer-Verlag GmbH Germany, part of Springer Nature 2020 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Biotechnologically Relevant Enzymes and Proteins Zafar, Maryam Shah, Majid Ali Shehzad, Aamir Tariq, Anam Habib, Mudasser Muddassar, Muhammad Shah, Muhammad Salahuddin Iqbal, Mazhar Hemmatzadeh, Farhid Rahman, Moazur Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family |
title | Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family |
title_full | Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family |
title_fullStr | Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family |
title_full_unstemmed | Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family |
title_short | Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family |
title_sort | characterization of the highly immunogenic vp2 protrusion domain as a diagnostic antigen for members of birnaviridae family |
topic | Biotechnologically Relevant Enzymes and Proteins |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7222154/ https://www.ncbi.nlm.nih.gov/pubmed/32088761 http://dx.doi.org/10.1007/s00253-020-10458-6 |
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