Cargando…
Processing and intracellular transport of rubella virus structural proteins in COS cells
Plasmids encoding rubella virus (RV) structural proteins C-E2-Et, E2-Et, E2, and E1 have been constructed in the eukaryotic expression vector pCMV5. The processing and intracellular transport of these proteins have been examined by transient expression of the cDNAs in COS cells. Compared to alphavir...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Elsevier Inc.
1990
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7131528/ https://www.ncbi.nlm.nih.gov/pubmed/2117827 http://dx.doi.org/10.1016/0042-6822(90)90385-5 |
_version_ | 1783517259329699840 |
---|---|
author | Hobman, Tom C. Lundstrom, Marita L. Gillam, Shirley |
author_facet | Hobman, Tom C. Lundstrom, Marita L. Gillam, Shirley |
author_sort | Hobman, Tom C. |
collection | PubMed |
description | Plasmids encoding rubella virus (RV) structural proteins C-E2-Et, E2-Et, E2, and E1 have been constructed in the eukaryotic expression vector pCMV5. The processing and intracellular transport of these proteins have been examined by transient expression of the cDNAs in COS cells. Compared to alphaviruses, processing of RV glycoprotein moieties occurred relatively slowly and the transport of glycoproteins E2 and El to the plasma membrane was inefficient. Indirect immunofluoresence revealed that the majority of RV antigen in transfected and infected COS cells was localized to the Golgi region, including the capsid protein. Accumulation of capsid protein in the juxtanuclear region was determined to be RV glycoprotein dependent. Unlike alphaviruses, RV El did not require E2 for targeting to the Golgi where it was retained. E2 was however necessary for cell surface expression of Et. This study revealed that the processing and transport of RV structural proteins is quite different from alphaviruses and that the accumulation of antigens in the Golgi region may be significant in light of previous reports which suggest that RV buds from the internal membranes in some cell types. |
format | Online Article Text |
id | pubmed-7131528 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | Published by Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71315282020-04-08 Processing and intracellular transport of rubella virus structural proteins in COS cells Hobman, Tom C. Lundstrom, Marita L. Gillam, Shirley Virology Article Plasmids encoding rubella virus (RV) structural proteins C-E2-Et, E2-Et, E2, and E1 have been constructed in the eukaryotic expression vector pCMV5. The processing and intracellular transport of these proteins have been examined by transient expression of the cDNAs in COS cells. Compared to alphaviruses, processing of RV glycoprotein moieties occurred relatively slowly and the transport of glycoproteins E2 and El to the plasma membrane was inefficient. Indirect immunofluoresence revealed that the majority of RV antigen in transfected and infected COS cells was localized to the Golgi region, including the capsid protein. Accumulation of capsid protein in the juxtanuclear region was determined to be RV glycoprotein dependent. Unlike alphaviruses, RV El did not require E2 for targeting to the Golgi where it was retained. E2 was however necessary for cell surface expression of Et. This study revealed that the processing and transport of RV structural proteins is quite different from alphaviruses and that the accumulation of antigens in the Golgi region may be significant in light of previous reports which suggest that RV buds from the internal membranes in some cell types. Published by Elsevier Inc. 1990-09 2004-06-17 /pmc/articles/PMC7131528/ /pubmed/2117827 http://dx.doi.org/10.1016/0042-6822(90)90385-5 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 Hobman, Tom C. Lundstrom, Marita L. Gillam, Shirley Processing and intracellular transport of rubella virus structural proteins in COS cells |
title | Processing and intracellular transport of rubella virus structural proteins in COS cells |
title_full | Processing and intracellular transport of rubella virus structural proteins in COS cells |
title_fullStr | Processing and intracellular transport of rubella virus structural proteins in COS cells |
title_full_unstemmed | Processing and intracellular transport of rubella virus structural proteins in COS cells |
title_short | Processing and intracellular transport of rubella virus structural proteins in COS cells |
title_sort | processing and intracellular transport of rubella virus structural proteins in cos cells |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7131528/ https://www.ncbi.nlm.nih.gov/pubmed/2117827 http://dx.doi.org/10.1016/0042-6822(90)90385-5 |
work_keys_str_mv | AT hobmantomc processingandintracellulartransportofrubellavirusstructuralproteinsincoscells AT lundstrommarital processingandintracellulartransportofrubellavirusstructuralproteinsincoscells AT gillamshirley processingandintracellulartransportofrubellavirusstructuralproteinsincoscells |