Cargando…

Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein

The glycoproteins of bunyaviruses accumulate in membranes of the Golgi complex, where virus maturation occurs by budding. In this study we have constructed a series of full length or truncated mutants of the G2 glycoprotein of Punta Toro virus (PTV), a member of the Phlebovirus genus of the Bunyavir...

Descripción completa

Detalles Bibliográficos
Autores principales: Chen, Si-Yi, Matsuoka, Yumiko, Compans, Richard W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier Inc. 1991
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130718/
https://www.ncbi.nlm.nih.gov/pubmed/1905078
http://dx.doi.org/10.1016/0042-6822(91)90148-5
_version_ 1783517074118672384
author Chen, Si-Yi
Matsuoka, Yumiko
Compans, Richard W.
author_facet Chen, Si-Yi
Matsuoka, Yumiko
Compans, Richard W.
author_sort Chen, Si-Yi
collection PubMed
description The glycoproteins of bunyaviruses accumulate in membranes of the Golgi complex, where virus maturation occurs by budding. In this study we have constructed a series of full length or truncated mutants of the G2 glycoprotein of Punta Toro virus (PTV), a member of the Phlebovirus genus of the Bunyaviridae, and investigated their transport properties. The results indicate that the hydrophobic domain preceding the G2 glycoprotein can function as a translocational signal peptide, and that the hydrophobic domain near the C-terminus serves as a membrane anchor. A G2 glycoprotein construct with an extra hydrophobic sequence derived from the N-terminal NS(M) region was stably retained in the ER, and was unable to be transported to the Golgi complex. The full-length G2 glycoprotein, when expressed on its own, was transported out of the ER and expressed on the cell surface, whereas the G1 and G2 proteins when expressed together are retained in the Golgi complex. A truncated anchor-minus form of the G2 glycoprotein was found to be secreted into the culture medium, but was retained in the Golgi complex when coexpressed with the G1 glycoprotein. These results indicate that the G2 membrane glycoprotein is a class I membrane protein which does not contain a signal sufficient for Golgi retention, and suggest that its Golgi localization is a result of association with the G1 glycoprotein.
format Online
Article
Text
id pubmed-7130718
institution National Center for Biotechnology Information
language English
publishDate 1991
publisher Published by Elsevier Inc.
record_format MEDLINE/PubMed
spelling pubmed-71307182020-04-08 Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein Chen, Si-Yi Matsuoka, Yumiko Compans, Richard W. Virology Article The glycoproteins of bunyaviruses accumulate in membranes of the Golgi complex, where virus maturation occurs by budding. In this study we have constructed a series of full length or truncated mutants of the G2 glycoprotein of Punta Toro virus (PTV), a member of the Phlebovirus genus of the Bunyaviridae, and investigated their transport properties. The results indicate that the hydrophobic domain preceding the G2 glycoprotein can function as a translocational signal peptide, and that the hydrophobic domain near the C-terminus serves as a membrane anchor. A G2 glycoprotein construct with an extra hydrophobic sequence derived from the N-terminal NS(M) region was stably retained in the ER, and was unable to be transported to the Golgi complex. The full-length G2 glycoprotein, when expressed on its own, was transported out of the ER and expressed on the cell surface, whereas the G1 and G2 proteins when expressed together are retained in the Golgi complex. A truncated anchor-minus form of the G2 glycoprotein was found to be secreted into the culture medium, but was retained in the Golgi complex when coexpressed with the G1 glycoprotein. These results indicate that the G2 membrane glycoprotein is a class I membrane protein which does not contain a signal sufficient for Golgi retention, and suggest that its Golgi localization is a result of association with the G1 glycoprotein. Published by Elsevier Inc. 1991-07 2004-07-22 /pmc/articles/PMC7130718/ /pubmed/1905078 http://dx.doi.org/10.1016/0042-6822(91)90148-5 Text en Copyright © 1991 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
Chen, Si-Yi
Matsuoka, Yumiko
Compans, Richard W.
Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein
title Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein
title_full Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein
title_fullStr Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein
title_full_unstemmed Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein
title_short Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein
title_sort golgi complex localization of the punta toro virus g2 protein requires its association with the g1 protein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130718/
https://www.ncbi.nlm.nih.gov/pubmed/1905078
http://dx.doi.org/10.1016/0042-6822(91)90148-5
work_keys_str_mv AT chensiyi golgicomplexlocalizationofthepuntatorovirusg2proteinrequiresitsassociationwiththeg1protein
AT matsuokayumiko golgicomplexlocalizationofthepuntatorovirusg2proteinrequiresitsassociationwiththeg1protein
AT compansrichardw golgicomplexlocalizationofthepuntatorovirusg2proteinrequiresitsassociationwiththeg1protein