Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells

The fatty acid acylation of the cell-associated virus-specific proteins of mouse hepatitis virus (A 59-strain) was studied.(3)H-palmitate label was associated with E 2, one of the two virion glycoproteins and its intracellular precursor gp 150. A 110 K protein, the unglycosylated apoprotein of gp 15...

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Autores principales: van Berlo, M. F., van den Brink, W. J., Horzinek, M. C., van der Zeijst, B. A. M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer-Verlag 1987
Materias:
Brief Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7086565/
https://www.ncbi.nlm.nih.gov/pubmed/3036041
http://dx.doi.org/10.1007/BF01311339
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author van Berlo, M. F.
van den Brink, W. J.
Horzinek, M. C.
van der Zeijst, B. A. M.
author_facet van Berlo, M. F.
van den Brink, W. J.
Horzinek, M. C.
van der Zeijst, B. A. M.
author_sort van Berlo, M. F.
collection PubMed
description The fatty acid acylation of the cell-associated virus-specific proteins of mouse hepatitis virus (A 59-strain) was studied.(3)H-palmitate label was associated with E 2, one of the two virion glycoproteins and its intracellular precursor gp 150. A 110 K protein, the unglycosylated apoprotein of gp 150, accumulated by tunicamycin treatment, also incorporated radiolabeled palmitic acid. The addition of fatty acid to the MHV-A 59 E 2 protein is therefore not dependent on glycosylation.
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spelling pubmed-70865652020-03-23 Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells van Berlo, M. F. van den Brink, W. J. Horzinek, M. C. van der Zeijst, B. A. M. Arch Virol Brief Report The fatty acid acylation of the cell-associated virus-specific proteins of mouse hepatitis virus (A 59-strain) was studied.(3)H-palmitate label was associated with E 2, one of the two virion glycoproteins and its intracellular precursor gp 150. A 110 K protein, the unglycosylated apoprotein of gp 150, accumulated by tunicamycin treatment, also incorporated radiolabeled palmitic acid. The addition of fatty acid to the MHV-A 59 E 2 protein is therefore not dependent on glycosylation. Springer-Verlag 1987 /pmc/articles/PMC7086565/ /pubmed/3036041 http://dx.doi.org/10.1007/BF01311339 Text en © Springer-Verlag 1987 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Brief Report
van Berlo, M. F.
van den Brink, W. J.
Horzinek, M. C.
van der Zeijst, B. A. M.
Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells
title Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells
title_full Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells
title_fullStr Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells
title_full_unstemmed Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells
title_short Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells
title_sort fatty acid acylation of viral proteins in murine hepatitis virus-infected cells
topic Brief Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7086565/
https://www.ncbi.nlm.nih.gov/pubmed/3036041
http://dx.doi.org/10.1007/BF01311339
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