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A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV)
Pulse labeling with tritiated mannose was used to follow the time course of Autographa californica nuclear polyhedrosis virus (AcNPV) glycoprotein synthesis in Spodoptera frugiperda IPLB-21 cells. Nine viral-induced intracellular glycoproteins were first detected from as early as 2 hr postinoculatio...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Elsevier Inc.
1983
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7131021/ https://www.ncbi.nlm.nih.gov/pubmed/18639173 http://dx.doi.org/10.1016/0042-6822(83)90548-2 |
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author | Stiles, Brad Wood, H.A. |
author_facet | Stiles, Brad Wood, H.A. |
author_sort | Stiles, Brad |
collection | PubMed |
description | Pulse labeling with tritiated mannose was used to follow the time course of Autographa californica nuclear polyhedrosis virus (AcNPV) glycoprotein synthesis in Spodoptera frugiperda IPLB-21 cells. Nine viral-induced intracellular glycoproteins were first detected from as early as 2 hr postinoculation (67K, early phase) to as late as 14 hr (36K and 19K glycoproteins, intermediate phase). Glycosylation of these proteins was observed to continue to the end of the experiment (28 hr postinoculation). Seven of these intracellular glycoproteins could also be detected in infected Trichoplusia ni TN-368 cells 24 hr postinoculation. When the glycosylation inhibitor tunicamycin was present (from 0 hr postinoculation) there was no detectable glycosylation of any of these viral-induced glycoproteins. Metabolic labeling of the nonoccluded virus budded from IPLB-21 and TN-368 with tritiated mannose or N-acetylglucosamine identified 11 structural glycoproteins, 8 of which were identical in both virus preparations. All of these structural glycoproteins were sensitive to the inhibitory action of tunicamycin. A single 42K structural glycoprotein was detected (with acetylglucosamine only) in the occluded form of AcNPV. Glycosylation of this structural protein appeared to be insensitive to tunicamycin. Lactoperoxidase-catalyzed radioiodination was used to determine which of the virus structural glycoproteins are exposed on the virion surface. |
format | Online Article Text |
id | pubmed-7131021 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1983 |
publisher | Published by Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71310212020-04-08 A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV) Stiles, Brad Wood, H.A. Virology Article Pulse labeling with tritiated mannose was used to follow the time course of Autographa californica nuclear polyhedrosis virus (AcNPV) glycoprotein synthesis in Spodoptera frugiperda IPLB-21 cells. Nine viral-induced intracellular glycoproteins were first detected from as early as 2 hr postinoculation (67K, early phase) to as late as 14 hr (36K and 19K glycoproteins, intermediate phase). Glycosylation of these proteins was observed to continue to the end of the experiment (28 hr postinoculation). Seven of these intracellular glycoproteins could also be detected in infected Trichoplusia ni TN-368 cells 24 hr postinoculation. When the glycosylation inhibitor tunicamycin was present (from 0 hr postinoculation) there was no detectable glycosylation of any of these viral-induced glycoproteins. Metabolic labeling of the nonoccluded virus budded from IPLB-21 and TN-368 with tritiated mannose or N-acetylglucosamine identified 11 structural glycoproteins, 8 of which were identical in both virus preparations. All of these structural glycoproteins were sensitive to the inhibitory action of tunicamycin. A single 42K structural glycoprotein was detected (with acetylglucosamine only) in the occluded form of AcNPV. Glycosylation of this structural protein appeared to be insensitive to tunicamycin. Lactoperoxidase-catalyzed radioiodination was used to determine which of the virus structural glycoproteins are exposed on the virion surface. Published by Elsevier Inc. 1983-11 2004-06-09 /pmc/articles/PMC7131021/ /pubmed/18639173 http://dx.doi.org/10.1016/0042-6822(83)90548-2 Text en Copyright © 1983 Published by Elsevier Inc. 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 Stiles, Brad Wood, H.A. A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV) |
title | A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV) |
title_full | A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV) |
title_fullStr | A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV) |
title_full_unstemmed | A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV) |
title_short | A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV) |
title_sort | study of the glycoproteins of autographa californica nuclear polyhedrosis virus (acnpv) |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7131021/ https://www.ncbi.nlm.nih.gov/pubmed/18639173 http://dx.doi.org/10.1016/0042-6822(83)90548-2 |
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