Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein
The glycosylated membrane protein M of the severe acute respiratory syndrome associated coronavirus (SARS-CoV) is the main structural component of the virion and mediates assembly and budding of viral particles. The membrane topology of SARS-CoV M and the functional significance of its N-glycosylation are not completely understood as is its interaction with the surface glycoprotein S. Using biochemical and immunofluorescence analyses we found that M consists of a short glycosylated N-terminal ectodomain, three transmembrane segments and a long, immunogenic C-terminal endodomain. Although the N-glycosylation site of M seems to be highly conserved between group 1 and 3 coronaviruses, studies using a recombinant SARS-CoV expressing a glycosylation-deficient M revealed that N-glycosylation of M neither influence the shape of the virions nor their infectivity in cell culture. Further functional analysis of truncated M proteins showed that the N-terminal 134 amino acids comprising the three transmembrane domains are sufficient to mediate accumulation of M in the Golgi complex and to enforce recruitment of the viral spike protein S to the sites of virus assembly and budding in the ERGIC.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2009 |
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| Erschienen: |
2009 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:6 |
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| Enthalten in: |
Virology journal - 6(2009) vom: 18. Juni, Seite 79 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Voss, Daniel [VerfasserIn] |
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| Links: |
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| Themen: |
Coronavirus M Proteins |
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| Anmerkungen: |
Date Completed 03.08.2009 Date Revised 07.12.2022 published: Electronic Citation Status MEDLINE |
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| doi: |
10.1186/1743-422X-6-79 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM189364130 |
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| 100 | 1 | |a Voss, Daniel |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein |
| 264 | 1 | |c 2009 | |
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| 500 | |a Date Completed 03.08.2009 | ||
| 500 | |a Date Revised 07.12.2022 | ||
| 500 | |a published: Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a The glycosylated membrane protein M of the severe acute respiratory syndrome associated coronavirus (SARS-CoV) is the main structural component of the virion and mediates assembly and budding of viral particles. The membrane topology of SARS-CoV M and the functional significance of its N-glycosylation are not completely understood as is its interaction with the surface glycoprotein S. Using biochemical and immunofluorescence analyses we found that M consists of a short glycosylated N-terminal ectodomain, three transmembrane segments and a long, immunogenic C-terminal endodomain. Although the N-glycosylation site of M seems to be highly conserved between group 1 and 3 coronaviruses, studies using a recombinant SARS-CoV expressing a glycosylation-deficient M revealed that N-glycosylation of M neither influence the shape of the virions nor their infectivity in cell culture. Further functional analysis of truncated M proteins showed that the N-terminal 134 amino acids comprising the three transmembrane domains are sufficient to mediate accumulation of M in the Golgi complex and to enforce recruitment of the viral spike protein S to the sites of virus assembly and budding in the ERGIC | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a Coronavirus M Proteins |2 NLM | |
| 650 | 7 | |a M protein, SARS-CoV |2 NLM | |
| 650 | 7 | |a Membrane Glycoproteins |2 NLM | |
| 650 | 7 | |a Spike Glycoprotein, Coronavirus |2 NLM | |
| 650 | 7 | |a Viral Envelope Proteins |2 NLM | |
| 650 | 7 | |a Viral Matrix Proteins |2 NLM | |
| 700 | 1 | |a Pfefferle, Susanne |e verfasserin |4 aut | |
| 700 | 1 | |a Drosten, Christian |e verfasserin |4 aut | |
| 700 | 1 | |a Stevermann, Lea |e verfasserin |4 aut | |
| 700 | 1 | |a Traggiai, Elisabetta |e verfasserin |4 aut | |
| 700 | 1 | |a Lanzavecchia, Antonio |e verfasserin |4 aut | |
| 700 | 1 | |a Becker, Stephan |e verfasserin |4 aut | |
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