Deletion of 82–85 N-Terminal Residues in SARS-CoV-2 Nsp1 Restricts Virus Replication.
| Title: | Deletion of 82–85 N-Terminal Residues in SARS-CoV-2 Nsp1 Restricts Virus Replication. |
|---|---|
| Authors: | Gori Savellini, Gianni1 (AUTHOR) gabriele.anichini2@unisi.it, Anichini, Gabriele1 (AUTHOR), Manetti, Fabrizio2 (AUTHOR) claudia.trivisani2@unisi.it, Trivisani, Claudia Immacolata2 (AUTHOR), Cusi, Maria Grazia1 (AUTHOR) gianni.gori@unisi.it |
| Source: | Viruses (1999-4915). May2024, Vol. 16 Issue 5, p689. 18p. |
| Subject Terms: | *N-terminal residues, *SARS-CoV-2, *VIRAL replication, *VIRAL proteins, *GENE expression, *DRUG development, *MESSENGER RNA |
| Abstract: | Non-structural protein 1 (Nsp1) represents one of the most crucial SARS-CoV-2 virulence factors by inhibiting the translation of host mRNAs and promoting their degradation. We selected naturally occurring virus lineages with specific Nsp1 deletions located at both the N- and C-terminus of the protein. Our data provide new insights into how Nsp1 coordinates these functions on host and viral mRNA recognition. Residues 82–85 in the N-terminal part of Nsp1 likely play a role in docking the 40S mRNA entry channel, preserving the inhibition of host gene expression without affecting cellular mRNA decay. Furthermore, this domain prevents viral mRNAs containing the 5′-leader sequence to escape translational repression. These findings support the presence of distinct domains within the Nsp1 protein that differentially modulate mRNA recognition, translation and turnover. These insights have implications for the development of drugs targeting viral proteins and provides new evidences of how specific mutations in SARS-CoV-2 Nsp1 could attenuate the virus. [ABSTRACT FROM AUTHOR] |
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| Items | – Name: Title Label: Title Group: Ti Data: Deletion of 82–85 N-Terminal Residues in SARS-CoV-2 Nsp1 Restricts Virus Replication. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Gori+Savellini%2C+Gianni%22">Gori Savellini, Gianni</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> gabriele.anichini2@unisi.it</i><br /><searchLink fieldCode="AR" term="%22Anichini%2C+Gabriele%22">Anichini, Gabriele</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Manetti%2C+Fabrizio%22">Manetti, Fabrizio</searchLink><relatesTo>2</relatesTo> (AUTHOR)<i> claudia.trivisani2@unisi.it</i><br /><searchLink fieldCode="AR" term="%22Trivisani%2C+Claudia+Immacolata%22">Trivisani, Claudia Immacolata</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Cusi%2C+Maria+Grazia%22">Cusi, Maria Grazia</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> gianni.gori@unisi.it</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Viruses+%281999-4915%29%22">Viruses (1999-4915)</searchLink>. May2024, Vol. 16 Issue 5, p689. 18p. – Name: Subject Label: Subject Terms Group: Su Data: *<searchLink fieldCode="DE" term="%22N-terminal+residues%22">N-terminal residues</searchLink><br />*<searchLink fieldCode="DE" term="%22SARS-CoV-2%22">SARS-CoV-2</searchLink><br />*<searchLink fieldCode="DE" term="%22VIRAL+replication%22">VIRAL replication</searchLink><br />*<searchLink fieldCode="DE" term="%22VIRAL+proteins%22">VIRAL proteins</searchLink><br />*<searchLink fieldCode="DE" term="%22GENE+expression%22">GENE expression</searchLink><br />*<searchLink fieldCode="DE" term="%22DRUG+development%22">DRUG development</searchLink><br />*<searchLink fieldCode="DE" term="%22MESSENGER+RNA%22">MESSENGER RNA</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Non-structural protein 1 (Nsp1) represents one of the most crucial SARS-CoV-2 virulence factors by inhibiting the translation of host mRNAs and promoting their degradation. We selected naturally occurring virus lineages with specific Nsp1 deletions located at both the N- and C-terminus of the protein. Our data provide new insights into how Nsp1 coordinates these functions on host and viral mRNA recognition. Residues 82–85 in the N-terminal part of Nsp1 likely play a role in docking the 40S mRNA entry channel, preserving the inhibition of host gene expression without affecting cellular mRNA decay. Furthermore, this domain prevents viral mRNAs containing the 5′-leader sequence to escape translational repression. These findings support the presence of distinct domains within the Nsp1 protein that differentially modulate mRNA recognition, translation and turnover. These insights have implications for the development of drugs targeting viral proteins and provides new evidences of how specific mutations in SARS-CoV-2 Nsp1 could attenuate the virus. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Viruses (1999-4915) is the property of MDPI and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.3390/v16050689 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 18 StartPage: 689 Subjects: – SubjectFull: N-terminal residues Type: general – SubjectFull: SARS-CoV-2 Type: general – SubjectFull: VIRAL replication Type: general – SubjectFull: VIRAL proteins Type: general – SubjectFull: GENE expression Type: general – SubjectFull: DRUG development Type: general – SubjectFull: MESSENGER RNA Type: general Titles: – TitleFull: Deletion of 82–85 N-Terminal Residues in SARS-CoV-2 Nsp1 Restricts Virus Replication. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Gori Savellini, Gianni – PersonEntity: Name: NameFull: Anichini, Gabriele – PersonEntity: Name: NameFull: Manetti, Fabrizio – PersonEntity: Name: NameFull: Trivisani, Claudia Immacolata – PersonEntity: Name: NameFull: Cusi, Maria Grazia IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 05 Text: May2024 Type: published Y: 2024 Identifiers: – Type: issn-print Value: 19994915 Numbering: – Type: volume Value: 16 – Type: issue Value: 5 Titles: – TitleFull: Viruses (1999-4915) Type: main |
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