mce11lia

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?:abstract	The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a beta-coronavirus, is the causative agent of the COVID-19 pandemic Like for other coronaviruses, its particles are composed of four structural proteins: Spike (S), Envelope (E), Membrane (M) and Nucleoprotein (N) proteins The involvement of each of these proteins and their interactions are critical for assembly and production of beta-coronavirus particles Here, we sought to characterize the interplay of SARS-CoV-2 structural proteins during the viral assembly process By combining biochemical and imaging assays in infected vs transfected cells, we show that E and M regulate intracellular trafficking of S as well as its intracellular processing Indeed, the imaging data reveal that S is re-localized at endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) or Golgi compartments upon co-expression of E or M, as observed in SARS-CoV-2-infected cells, which prevents syncytia formation We show that a C-terminal retrieval motif in the cytoplasmic tail of S is required for its M-mediated retention in the ERGIC, whereas E induces S retention by modulating the cell secretory pathway We also highlight that E and M induce a specific maturation of N-glycosylation of S, independently of the regulation of its localization, with a profile that is observed both in infected cells and in purified viral particles Finally, we show that E, M and N are required for optimal production of virus- like-particles Altogether, these results highlight how E and M proteins may influence the properties of S proteins and promote the assembly of SARS-CoV-2 viral particles The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a ß-coronavirus, is the causative agent of the COVID-19 pandemic. Like for other coronaviruses, its particles are composed of four structural proteins: Spike (S), Envelope (E), Membrane (M) and Nucleoprotein (N) proteins. The involvement of each of these proteins and their interactions are critical for assembly and production of ß-coronavirus particles. Here, we sought to characterize the interplay of SARS-CoV-2 structural proteins during the viral assembly process. By combining biochemical and imaging assays in infected vs. transfected cells, we show that E and M regulate intracellular trafficking of S as well as its intracellular processing. Indeed, the imaging data reveal that S is re-localized at endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) or Golgi compartments upon co-expression of E or M, as observed in SARS-CoV-2-infected cells, which prevents syncytia formation. We show that a C-terminal retrieval motif in the cytoplasmic tail of S is required for its M-mediated retention in the ERGIC, whereas E induces S retention by modulating the cell secretory pathway. We also highlight that E and M induce a specific maturation of N-glycosylation of S, independently of the regulation of its localization, with a profile that is observed both in infected cells and in purified viral particles. Finally, we show that E, M and N are required for optimal production of virus- like-particles. Altogether, these results highlight how E and M proteins may influence the properties of S proteins and promote the assembly of SARS-CoV-2 viral particles.
is ?:annotates of	<https://research.tib.eu/covid-19/entity/mce11lia_hasAnnotation_C5203676>
?:creator	<https://research.tib.eu/covid-19/entity/Boson%2C_B.%3B_Legros%2C_V.%3B_Zhou%2C_B.%3B_Siret%2C_E.%3B_Mathieu%2C_C.%3B_Cosset%2C_F._L.%3B_Lavillette%2C_D.%3B_Denolly%2C_S.> <https://research.tib.eu/covid-19/entity/Boson%2C_Bertrand%3B_Legros%2C_Vincent%3B_Zhou%2C_Bingjie%3B_Siret%2C_Eglantine%3B_Mathieu%2C_Cyrille%3B_Cosset%2C_Fran%C3%A7ois-Lo%C3%AFc%3B_Lavillette%2C_Dimitri%3B_Denolly%2C_Sol%C3%A8ne>
?:journal	Journal_of_Biological_Chemistry
?:license	unk
?:publication_isRelatedTo_Disease	<https://research.tib.eu/covid-19/entity/COVID-19>
?:source	WHO
?:title	The SARS-CoV-2 Envelope and Membrane proteins modulate maturation and retention of the Spike protein, allowing assembly of virus-like particles
?:type	<https://research.tib.eu/covid-19/vocab/Publication>
?:who_covidence_id	#1066049 #940855
?:year	2020

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?:abstract

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a beta-coronavirus, is the causative agent of the COVID-19 pandemic Like for other coronaviruses, its particles are composed of four structural proteins: Spike (S), Envelope (E), Membrane (M) and Nucleoprotein (N) proteins The involvement of each of these proteins and their interactions are critical for assembly and production of beta-coronavirus particles Here, we sought to characterize the interplay of SARS-CoV-2 structural proteins during the viral assembly process By combining biochemical and imaging assays in infected vs transfected cells, we show that E and M regulate intracellular trafficking of S as well as its intracellular processing Indeed, the imaging data reveal that S is re-localized at endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) or Golgi compartments upon co-expression of E or M, as observed in SARS-CoV-2-infected cells, which prevents syncytia formation We show that a C-terminal retrieval motif in the cytoplasmic tail of S is required for its M-mediated retention in the ERGIC, whereas E induces S retention by modulating the cell secretory pathway We also highlight that E and M induce a specific maturation of N-glycosylation of S, independently of the regulation of its localization, with a profile that is observed both in infected cells and in purified viral particles Finally, we show that E, M and N are required for optimal production of virus- like-particles Altogether, these results highlight how E and M proteins may influence the properties of S proteins and promote the assembly of SARS-CoV-2 viral particles
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a ß-coronavirus, is the causative agent of the COVID-19 pandemic. Like for other coronaviruses, its particles are composed of four structural proteins: Spike (S), Envelope (E), Membrane (M) and Nucleoprotein (N) proteins. The involvement of each of these proteins and their interactions are critical for assembly and production of ß-coronavirus particles. Here, we sought to characterize the interplay of SARS-CoV-2 structural proteins during the viral assembly process. By combining biochemical and imaging assays in infected vs. transfected cells, we show that E and M regulate intracellular trafficking of S as well as its intracellular processing. Indeed, the imaging data reveal that S is re-localized at endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) or Golgi compartments upon co-expression of E or M, as observed in SARS-CoV-2-infected cells, which prevents syncytia formation. We show that a C-terminal retrieval motif in the cytoplasmic tail of S is required for its M-mediated retention in the ERGIC, whereas E induces S retention by modulating the cell secretory pathway. We also highlight that E and M induce a specific maturation of N-glycosylation of S, independently of the regulation of its localization, with a profile that is observed both in infected cells and in purified viral particles. Finally, we show that E, M and N are required for optimal production of virus- like-particles. Altogether, these results highlight how E and M proteins may influence the properties of S proteins and promote the assembly of SARS-CoV-2 viral particles.

is ?:annotates of