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Post-translational processing of the glycoproteins of lymphocytic choriomeningitis virus
Intracellular events in the synthesis, glycosylation, and transport of the lymphocytic choriomeningitis virus (LCMV) glycoproteins have been examined. We have shown by N-glycanase digestion that LCMV strain Arm-4 bears five oligosaccharides on GP-1 and two on GP-2. By pulse-chase labeling experiment...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Elsevier Inc.
1990
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130728/ https://www.ncbi.nlm.nih.gov/pubmed/2141203 http://dx.doi.org/10.1016/0042-6822(90)90471-3 |
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author | Wright, K.E. Spiro, R.C. Burns, J.W. Buchmeier, M.J. |
author_facet | Wright, K.E. Spiro, R.C. Burns, J.W. Buchmeier, M.J. |
author_sort | Wright, K.E. |
collection | PubMed |
description | Intracellular events in the synthesis, glycosylation, and transport of the lymphocytic choriomeningitis virus (LCMV) glycoproteins have been examined. We have shown by N-glycanase digestion that LCMV strain Arm-4 bears five oligosaccharides on GP-1 and two on GP-2. By pulse-chase labeling experiments in the presence of drugs which inhibit N-linked oligosaccharide addition and processing we demonstrate that addition of high mannose precursor oligosaccharides is necessary for transport and cleavage of the viral GP-C glycoprotein. Moreover, in the presence of tunicamycin which inhibits en bloc addition of these mannose-rich side chains, virus budding was substantially decreased and infectious virions were reduced by more than 1000-fold in the supernatant medium. Incubation in the presence of castantospermine, which permits addition of oligomannosyl-rich chains but blocks further processing, restored transport and cleavage of GP-C and maturation of virions. Finally, by temperature block experiments we have determined that maturation of GP-C oligosaccharides to an endoglycosidase H resistant form precedes cleavage to GP-1 and GP-2. The latter process is most likely to occur in the Golgi or post-Golgi compartment. |
format | Online Article Text |
id | pubmed-7130728 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | Published by Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71307282020-04-08 Post-translational processing of the glycoproteins of lymphocytic choriomeningitis virus Wright, K.E. Spiro, R.C. Burns, J.W. Buchmeier, M.J. Virology Article Intracellular events in the synthesis, glycosylation, and transport of the lymphocytic choriomeningitis virus (LCMV) glycoproteins have been examined. We have shown by N-glycanase digestion that LCMV strain Arm-4 bears five oligosaccharides on GP-1 and two on GP-2. By pulse-chase labeling experiments in the presence of drugs which inhibit N-linked oligosaccharide addition and processing we demonstrate that addition of high mannose precursor oligosaccharides is necessary for transport and cleavage of the viral GP-C glycoprotein. Moreover, in the presence of tunicamycin which inhibits en bloc addition of these mannose-rich side chains, virus budding was substantially decreased and infectious virions were reduced by more than 1000-fold in the supernatant medium. Incubation in the presence of castantospermine, which permits addition of oligomannosyl-rich chains but blocks further processing, restored transport and cleavage of GP-C and maturation of virions. Finally, by temperature block experiments we have determined that maturation of GP-C oligosaccharides to an endoglycosidase H resistant form precedes cleavage to GP-1 and GP-2. The latter process is most likely to occur in the Golgi or post-Golgi compartment. Published by Elsevier Inc. 1990-07 2004-02-23 /pmc/articles/PMC7130728/ /pubmed/2141203 http://dx.doi.org/10.1016/0042-6822(90)90471-3 Text en Copyright © 1990 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 Wright, K.E. Spiro, R.C. Burns, J.W. Buchmeier, M.J. Post-translational processing of the glycoproteins of lymphocytic choriomeningitis virus |
title | Post-translational processing of the glycoproteins of lymphocytic choriomeningitis virus |
title_full | Post-translational processing of the glycoproteins of lymphocytic choriomeningitis virus |
title_fullStr | Post-translational processing of the glycoproteins of lymphocytic choriomeningitis virus |
title_full_unstemmed | Post-translational processing of the glycoproteins of lymphocytic choriomeningitis virus |
title_short | Post-translational processing of the glycoproteins of lymphocytic choriomeningitis virus |
title_sort | post-translational processing of the glycoproteins of lymphocytic choriomeningitis virus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130728/ https://www.ncbi.nlm.nih.gov/pubmed/2141203 http://dx.doi.org/10.1016/0042-6822(90)90471-3 |
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