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Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus

A recombinant glutathione-S-transferase fusion protein expressing amino acids 55–98 of equine arteritis virus (EAV) G(L) (rG(L)55–98) was tested in an ELISA for its ability to detect serum antibodies to EAV. Host antibodies induced following EAV infection bound the recombinant antigen by ELISA. The...

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Autores principales: Chirnside, E.D., Francis, P.M., De Vries, A.A.F., Sinclaira, R., Mumford, J.A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier B.V. 1995
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7119792/
https://www.ncbi.nlm.nih.gov/pubmed/7559853
http://dx.doi.org/10.1016/0166-0934(95)00020-U
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author Chirnside, E.D.
Francis, P.M.
De Vries, A.A.F.
Sinclaira, R.
Mumford, J.A.
author_facet Chirnside, E.D.
Francis, P.M.
De Vries, A.A.F.
Sinclaira, R.
Mumford, J.A.
author_sort Chirnside, E.D.
collection PubMed
description A recombinant glutathione-S-transferase fusion protein expressing amino acids 55–98 of equine arteritis virus (EAV) G(L) (rG(L)55–98) was tested in an ELISA for its ability to detect serum antibodies to EAV. Host antibodies induced following EAV infection bound the recombinant antigen by ELISA. The ELISA specificity and sensitivity were determined with a panel of equine sera including postinfection and postvaccination samples. A good correlation existed between EAV neutralizing antibody titers and ELISA absorbance values (r = 0.827). The sensitivity and specificity of the ELISA were 99.6 and 90.1%, respectively, compared with the EAV neutralization test and the recombinant antigen did not crossreact in ELISA with equine sera directed against other common equine respiratory viruses. Three post-EAV infection equine sera raised against different EAV isolates reacted strongly in the ELISA, as did two equine sera raised against EAV vaccines, indicating that the viral epitope was conserved between the viruses tested. Following vaccination with an inactivated whole virus vaccine, antibody detected with the recombinant antigen ELISA preceded the development of a virus-neutralizing response. The study demonstrates the potential application of rG(L)55–98 as a diagnostic antigen.
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spelling pubmed-71197922020-04-08 Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus Chirnside, E.D. Francis, P.M. De Vries, A.A.F. Sinclaira, R. Mumford, J.A. J Virol Methods Research Paper A recombinant glutathione-S-transferase fusion protein expressing amino acids 55–98 of equine arteritis virus (EAV) G(L) (rG(L)55–98) was tested in an ELISA for its ability to detect serum antibodies to EAV. Host antibodies induced following EAV infection bound the recombinant antigen by ELISA. The ELISA specificity and sensitivity were determined with a panel of equine sera including postinfection and postvaccination samples. A good correlation existed between EAV neutralizing antibody titers and ELISA absorbance values (r = 0.827). The sensitivity and specificity of the ELISA were 99.6 and 90.1%, respectively, compared with the EAV neutralization test and the recombinant antigen did not crossreact in ELISA with equine sera directed against other common equine respiratory viruses. Three post-EAV infection equine sera raised against different EAV isolates reacted strongly in the ELISA, as did two equine sera raised against EAV vaccines, indicating that the viral epitope was conserved between the viruses tested. Following vaccination with an inactivated whole virus vaccine, antibody detected with the recombinant antigen ELISA preceded the development of a virus-neutralizing response. The study demonstrates the potential application of rG(L)55–98 as a diagnostic antigen. Published by Elsevier B.V. 1995-07 2000-04-04 /pmc/articles/PMC7119792/ /pubmed/7559853 http://dx.doi.org/10.1016/0166-0934(95)00020-U Text en Copyright © 1995 Published by Elsevier B.V. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Research Paper
Chirnside, E.D.
Francis, P.M.
De Vries, A.A.F.
Sinclaira, R.
Mumford, J.A.
Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus
title Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus
title_full Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus
title_fullStr Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus
title_full_unstemmed Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus
title_short Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus
title_sort development and evaluation of an elisa using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7119792/
https://www.ncbi.nlm.nih.gov/pubmed/7559853
http://dx.doi.org/10.1016/0166-0934(95)00020-U
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