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Envelope proteins of avian infectious bronchitis virus: Purification and biological properties
Immunoadsorbents, made with monoclonal antibodies, were used to purify the spike and membrane proteins of infectious bronchitis virus (IBV). The purified proteins were inoculated into rabbits to produce antisera. The rabbit anti-spike sera neutralized the infectivity of the virus whereas the anti-me...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Published by Elsevier B.V.
1985
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7119818/ https://www.ncbi.nlm.nih.gov/pubmed/3009515 http://dx.doi.org/10.1016/0166-0934(85)90138-7 |
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author | Mockett, A.P.Adrian |
author_facet | Mockett, A.P.Adrian |
author_sort | Mockett, A.P.Adrian |
collection | PubMed |
description | Immunoadsorbents, made with monoclonal antibodies, were used to purify the spike and membrane proteins of infectious bronchitis virus (IBV). The purified proteins were inoculated into rabbits to produce antisera. The rabbit anti-spike sera neutralized the infectivity of the virus whereas the anti-membrane sera did not. IBV-infected chickens produced antibodies to both the spike and membrane proteins. Both these antibodies were at their highest concentration about 9–11 days after inoculation, whereas neutralizing antibodies were present only at very low concentrations at that time. Neutralizing antibodies were at their highest concentration 21 days after inoculation. A second inoculation of virus at 42 days induced an anamnestic antibody response to the spike and membrane proteins and also for the neutralizing antibodies. The neutralizing, anti-spike and anti-membrane antibodies all reached highest concentrations 7–11 days after this inoculation. The advantages of purifying viral proteins using affinity chromatography with monoclonal antibodies are discussed. |
format | Online Article Text |
id | pubmed-7119818 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1985 |
publisher | Published by Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71198182020-04-08 Envelope proteins of avian infectious bronchitis virus: Purification and biological properties Mockett, A.P.Adrian J Virol Methods Article Immunoadsorbents, made with monoclonal antibodies, were used to purify the spike and membrane proteins of infectious bronchitis virus (IBV). The purified proteins were inoculated into rabbits to produce antisera. The rabbit anti-spike sera neutralized the infectivity of the virus whereas the anti-membrane sera did not. IBV-infected chickens produced antibodies to both the spike and membrane proteins. Both these antibodies were at their highest concentration about 9–11 days after inoculation, whereas neutralizing antibodies were present only at very low concentrations at that time. Neutralizing antibodies were at their highest concentration 21 days after inoculation. A second inoculation of virus at 42 days induced an anamnestic antibody response to the spike and membrane proteins and also for the neutralizing antibodies. The neutralizing, anti-spike and anti-membrane antibodies all reached highest concentrations 7–11 days after this inoculation. The advantages of purifying viral proteins using affinity chromatography with monoclonal antibodies are discussed. Published by Elsevier B.V. 1985-12 2002-12-20 /pmc/articles/PMC7119818/ /pubmed/3009515 http://dx.doi.org/10.1016/0166-0934(85)90138-7 Text en Copyright © 1985 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 | Article Mockett, A.P.Adrian Envelope proteins of avian infectious bronchitis virus: Purification and biological properties |
title | Envelope proteins of avian infectious bronchitis virus: Purification and biological properties |
title_full | Envelope proteins of avian infectious bronchitis virus: Purification and biological properties |
title_fullStr | Envelope proteins of avian infectious bronchitis virus: Purification and biological properties |
title_full_unstemmed | Envelope proteins of avian infectious bronchitis virus: Purification and biological properties |
title_short | Envelope proteins of avian infectious bronchitis virus: Purification and biological properties |
title_sort | envelope proteins of avian infectious bronchitis virus: purification and biological properties |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7119818/ https://www.ncbi.nlm.nih.gov/pubmed/3009515 http://dx.doi.org/10.1016/0166-0934(85)90138-7 |
work_keys_str_mv | AT mockettapadrian envelopeproteinsofavianinfectiousbronchitisviruspurificationandbiologicalproperties |