Glycosylation and oligomerization of the spike protein of marburg virus

The oligosaccharide side chains of the glycoprotein of Marburg virus (MW 170,000) have been analyzed by determining their sensitivity to enzymatic degradation and their reactivity with lectins. It was found that they consist of N- and O-glycans. Studies employing chemical cross-linking showed that t...

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Autores principales: Feldmann, H., Will, C., Schikore, M., Slenczka, W., Klenk, H.-D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier Inc. 1991
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7172319/
https://www.ncbi.nlm.nih.gov/pubmed/2024471
http://dx.doi.org/10.1016/0042-6822(91)90680-A
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author Feldmann, H.
Will, C.
Schikore, M.
Slenczka, W.
Klenk, H.-D.
author_facet Feldmann, H.
Will, C.
Schikore, M.
Slenczka, W.
Klenk, H.-D.
author_sort Feldmann, H.
collection PubMed
description The oligosaccharide side chains of the glycoprotein of Marburg virus (MW 170,000) have been analyzed by determining their sensitivity to enzymatic degradation and their reactivity with lectins. It was found that they consist of N- and O-glycans. Studies employing chemical cross-linking showed that the glycoprotein is present as a homotrimer in the viral envelope.
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spelling pubmed-71723192020-04-22 Glycosylation and oligomerization of the spike protein of marburg virus Feldmann, H. Will, C. Schikore, M. Slenczka, W. Klenk, H.-D. Virology Article The oligosaccharide side chains of the glycoprotein of Marburg virus (MW 170,000) have been analyzed by determining their sensitivity to enzymatic degradation and their reactivity with lectins. It was found that they consist of N- and O-glycans. Studies employing chemical cross-linking showed that the glycoprotein is present as a homotrimer in the viral envelope. Published by Elsevier Inc. 1991-05 2004-02-10 /pmc/articles/PMC7172319/ /pubmed/2024471 http://dx.doi.org/10.1016/0042-6822(91)90680-A 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
Feldmann, H.
Will, C.
Schikore, M.
Slenczka, W.
Klenk, H.-D.
Glycosylation and oligomerization of the spike protein of marburg virus
title Glycosylation and oligomerization of the spike protein of marburg virus
title_full Glycosylation and oligomerization of the spike protein of marburg virus
title_fullStr Glycosylation and oligomerization of the spike protein of marburg virus
title_full_unstemmed Glycosylation and oligomerization of the spike protein of marburg virus
title_short Glycosylation and oligomerization of the spike protein of marburg virus
title_sort glycosylation and oligomerization of the spike protein of marburg virus
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7172319/
https://www.ncbi.nlm.nih.gov/pubmed/2024471
http://dx.doi.org/10.1016/0042-6822(91)90680-A
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AT slenczkaw glycosylationandoligomerizationofthespikeproteinofmarburgvirus
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