Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli

Rice tungro disease (RTD) is a recurring disease affecting rice farming especially in the South and Southeast Asia. The disease is commonly diagnosed by visual observation of the symptoms on diseased plants in paddy fields and by polymerase chain reaction (PCR). However, visual observation is unreli...

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Main Authors: Yee, Siewfung, Chu, Chiahuay, Poili, Evenni, Magdline Sia, Henry Sum
Format: Article
Language:English
Published: Elsevier B.V. 2017
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Online Access:http://ir.unimas.my/id/eprint/14953/7/fung.pdf
http://ir.unimas.my/id/eprint/14953/
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85002397997&doi=10.1016%2fj.jviromet.2016.12.001&partnerID=40&md5=8603e22ff3ff4aa94345b19869aebaca
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spelling my.unimas.ir.149532021-05-21T12:20:07Z http://ir.unimas.my/id/eprint/14953/ Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli Yee, Siewfung Chu, Chiahuay Poili, Evenni Magdline Sia, Henry Sum QR355 Virology Rice tungro disease (RTD) is a recurring disease affecting rice farming especially in the South and Southeast Asia. The disease is commonly diagnosed by visual observation of the symptoms on diseased plants in paddy fields and by polymerase chain reaction (PCR). However, visual observation is unreliable and PCR can be costly. High-throughput as well as relatively cheap detection methods are important for RTD management for screening large number of samples. Due to this, detection by serological assays such as immunoblotting assays and enzyme-linked immunosorbent assay are preferred. However, these serological assays are limited by lack of continuous supply of antibodies as reagents due to the difficulty in preparing sufficient purified virions as antigens. This study aimed to generate and evaluate the reactivity of the recombinant coat proteins of Rice tungro bacilliform virus (RTBV) and Rice tungro spherical virus (RTSV) as alternative antigens to generate antibodies. The genes encoding the coat proteins of both viruses, RTBV (CP), and RTSV (CP1, CP2 and CP3) were cloned and expressed as recombinant fusion proteins in Escherichia coli. All of the recombinant fusion proteins, with the exception of the recombinant fusion protein of the CP2 of RTSV, were reactive against our in-house anti-tungro rabbit serum. In conclusion, our study showed the potential use of the recombinant fusion coat proteins of the tungro viruses as alternative antigens for production of antibodies for diagnostic purposes. Elsevier B.V. 2017-02-01 Article PeerReviewed text en http://ir.unimas.my/id/eprint/14953/7/fung.pdf Yee, Siewfung and Chu, Chiahuay and Poili, Evenni and Magdline Sia, Henry Sum (2017) Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli. Journal of Virological Methods, 240. pp. 69-72. ISSN 01660934 https://www.scopus.com/inward/record.uri?eid=2-s2.0-85002397997&doi=10.1016%2fj.jviromet.2016.12.001&partnerID=40&md5=8603e22ff3ff4aa94345b19869aebaca DOI: 10.1016/j.jviromet.2016.12.001
institution Universiti Malaysia Sarawak
building Centre for Academic Information Services (CAIS)
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaysia Sarawak
content_source UNIMAS Institutional Repository
url_provider http://ir.unimas.my/
language English
topic QR355 Virology
spellingShingle QR355 Virology
Yee, Siewfung
Chu, Chiahuay
Poili, Evenni
Magdline Sia, Henry Sum
Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli
description Rice tungro disease (RTD) is a recurring disease affecting rice farming especially in the South and Southeast Asia. The disease is commonly diagnosed by visual observation of the symptoms on diseased plants in paddy fields and by polymerase chain reaction (PCR). However, visual observation is unreliable and PCR can be costly. High-throughput as well as relatively cheap detection methods are important for RTD management for screening large number of samples. Due to this, detection by serological assays such as immunoblotting assays and enzyme-linked immunosorbent assay are preferred. However, these serological assays are limited by lack of continuous supply of antibodies as reagents due to the difficulty in preparing sufficient purified virions as antigens. This study aimed to generate and evaluate the reactivity of the recombinant coat proteins of Rice tungro bacilliform virus (RTBV) and Rice tungro spherical virus (RTSV) as alternative antigens to generate antibodies. The genes encoding the coat proteins of both viruses, RTBV (CP), and RTSV (CP1, CP2 and CP3) were cloned and expressed as recombinant fusion proteins in Escherichia coli. All of the recombinant fusion proteins, with the exception of the recombinant fusion protein of the CP2 of RTSV, were reactive against our in-house anti-tungro rabbit serum. In conclusion, our study showed the potential use of the recombinant fusion coat proteins of the tungro viruses as alternative antigens for production of antibodies for diagnostic purposes.
format Article
author Yee, Siewfung
Chu, Chiahuay
Poili, Evenni
Magdline Sia, Henry Sum
author_facet Yee, Siewfung
Chu, Chiahuay
Poili, Evenni
Magdline Sia, Henry Sum
author_sort Yee, Siewfung
title Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli
title_short Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli
title_full Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli
title_fullStr Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli
title_full_unstemmed Expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in Escherichia coli
title_sort expression and the antigenicity of recombinant coat proteins of tungro viruses expressed in escherichia coli
publisher Elsevier B.V.
publishDate 2017
url http://ir.unimas.my/id/eprint/14953/7/fung.pdf
http://ir.unimas.my/id/eprint/14953/
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85002397997&doi=10.1016%2fj.jviromet.2016.12.001&partnerID=40&md5=8603e22ff3ff4aa94345b19869aebaca
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