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Article ; Online: Mammalian antiviral RNAi is on the move.

Schierhorn, Kristina L / Sanchez-David, Raul Y / Maillard, Pierre V

2022 Volume 41, Issue 11, Page(s) e111210

Abstract: Recent work reported the existence of a mammalian cell-autonomous antiviral defence based on RNA interference (RNAi), which relies on the accumulation of virus-derived small interfering RNAs (vsiRNAs) to guide the degradation of complementary viral RNAs. ...

Abstract	Recent work reported the existence of a mammalian cell-autonomous antiviral defence based on RNA interference (RNAi), which relies on the accumulation of virus-derived small interfering RNAs (vsiRNAs) to guide the degradation of complementary viral RNAs. In a new study, Zhang et al (2022) find that, in infected mice, vsiRNAs can enter the bloodstream via their incorporation into extracellular vesicles (EVs) and confer sequence-specific antiviral activity to recipient cells, thus indicating that mammalian antiviral RNAi participates in both cell-autonomous and non-cell-autonomous host defence.
MeSH term(s)	Animals ; Antiviral Agents ; Mammals/genetics ; Mice ; RNA Interference ; RNA, Double-Stranded ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; RNA, Viral/genetics ; Viruses
Chemical Substances	Antiviral Agents ; RNA, Double-Stranded ; RNA, Small Interfering ; RNA, Viral
Language	English
Publishing date	2022-04-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2022111210
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Article ; Online: Unlocking the therapeutic potential of antiviral RNAi.

Sanchez-David, Raul Y / Maillard, Pierre V

Immunity

2021 Volume 54, Issue 10, Page(s) 2180–2182

Abstract: RNA interference (RNAi) provides antiviral defense in many organisms, including plants, insects, and nematodes. In this issue of Immunity, Fang et al. (2021) utilize designer peptides targeting viral suppressors of RNAi to provide evidence for the ... ...

Abstract	RNA interference (RNAi) provides antiviral defense in many organisms, including plants, insects, and nematodes. In this issue of Immunity, Fang et al. (2021) utilize designer peptides targeting viral suppressors of RNAi to provide evidence for the relevance of RNAi to antiviral immunity in mammals, also revealing the potential of this approach toward antiviral therapy.
MeSH term(s)	Animals ; Antiviral Agents/therapeutic use ; RNA Interference
Chemical Substances	Antiviral Agents
Language	English
Publishing date	2021-10-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	1217235-2
ISSN	1097-4180 ; 1074-7613
ISSN (online)	1097-4180
ISSN	1074-7613
DOI	10.1016/j.immuni.2021.09.013
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Article ; Online: Slicing and dicing viruses: antiviral RNA interference in mammals.

Maillard, Pierre V / van der Veen, Annemarthe G / Poirier, Enzo Z / Reis e Sousa, Caetano

The EMBO journal

2019 Volume 38, Issue 8

Abstract: To protect against the harmful consequences of viral infections, organisms are equipped with sophisticated antiviral mechanisms, including cell-intrinsic means to restrict viral replication and propagation. Plant and invertebrate cells utilise mostly RNA ...

Abstract	To protect against the harmful consequences of viral infections, organisms are equipped with sophisticated antiviral mechanisms, including cell-intrinsic means to restrict viral replication and propagation. Plant and invertebrate cells utilise mostly RNA interference (RNAi), an RNA-based mechanism, for cell-intrinsic immunity to viruses while vertebrates rely on the protein-based interferon (IFN)-driven innate immune system for the same purpose. The RNAi machinery is conserved in vertebrate cells, yet whether antiviral RNAi is still active in mammals and functionally relevant to mammalian antiviral defence is intensely debated. Here, we discuss cellular and viral factors that impact on antiviral RNAi and the contexts in which this system might be at play in mammalian resistance to viral infection.
MeSH term(s)	Animals ; Antiviral Agents/administration & dosage ; Host-Pathogen Interactions/genetics ; Host-Pathogen Interactions/immunology ; Mammals/genetics ; Mammals/immunology ; Mammals/virology ; RNA Interference ; RNA, Viral/genetics ; Virus Diseases/genetics ; Virus Diseases/immunology ; Virus Diseases/virology ; Virus Replication ; Viruses/immunology ; Viruses/isolation & purification
Chemical Substances	Antiviral Agents ; RNA, Viral
Keywords	covid19
Language	English
Publishing date	2019-03-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2018100941
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Article ; Online: Drosha cuts the tethers of myelopoiesis.

van der Veen, Annemarthe G / Maillard, Pierre V / Reis e Sousa, Caetano

Nature immunology

2015 Volume 16, Issue 11, Page(s) 1110–1112

MeSH term(s)	Animals ; Dendritic Cells/immunology ; Dendritic Cells/metabolism ; Myelopoiesis/immunology ; RNA, Messenger/metabolism ; Ribonuclease III/immunology
Chemical Substances	RNA, Messenger ; Ribonuclease III (EC 3.1.26.3)
Language	English
Publishing date	2015-10-21
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2016987-5
ISSN	1529-2916 ; 1529-2908
ISSN (online)	1529-2916
ISSN	1529-2908
DOI	10.1038/ni.3297
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Article ; Online: The HUSH complex is a gatekeeper of type I interferon through epigenetic regulation of LINE-1s.

Tunbak, Hale / Enriquez-Gasca, Rocio / Tie, Christopher H C / Gould, Poppy A / Mlcochova, Petra / Gupta, Ravindra K / Fernandes, Liane / Holt, James / van der Veen, Annemarthe G / Giampazolias, Evangelos / Burns, Kathleen H / Maillard, Pierre V / Rowe, Helen M

Nature communications

2020 Volume 11, Issue 1, Page(s) 5387

Abstract: The Human Silencing Hub (HUSH) complex is necessary for epigenetic repression of LINE-1 elements. We show that HUSH-depletion in human cell lines and primary fibroblasts leads to induction of interferon-stimulated genes (ISGs) through JAK/STAT signaling. ...

Abstract	The Human Silencing Hub (HUSH) complex is necessary for epigenetic repression of LINE-1 elements. We show that HUSH-depletion in human cell lines and primary fibroblasts leads to induction of interferon-stimulated genes (ISGs) through JAK/STAT signaling. This effect is mainly attributed to MDA5 and RIG-I sensing of double-stranded RNAs (dsRNAs). This coincides with upregulation of primate-conserved LINE-1s, as well as increased expression of full-length hominid-specific LINE-1s that produce bidirectional RNAs, which may form dsRNA. Notably, LTRs nearby ISGs are derepressed likely rendering these genes more responsive to interferon. LINE-1 shRNAs can abrogate the HUSH-dependent response, while overexpression of an engineered LINE-1 construct activates interferon signaling. Finally, we show that the HUSH component, MPP8 is frequently downregulated in diverse cancers and that its depletion leads to DNA damage. These results suggest that LINE-1s may drive physiological or autoinflammatory responses through dsRNA sensing and gene-regulatory roles and are controlled by the HUSH complex.
MeSH term(s)	DEAD Box Protein 58/genetics ; DEAD Box Protein 58/metabolism ; DNA Damage ; Down-Regulation ; Epigenesis, Genetic/physiology ; Gene Expression Regulation, Neoplastic ; Gene Knockout Techniques ; Gene Silencing/physiology ; HEK293 Cells ; HeLa Cells ; Humans ; Inflammation ; Interferon Type I/metabolism ; Interferon-Induced Helicase, IFIH1/metabolism ; Long Interspersed Nucleotide Elements/genetics ; Long Interspersed Nucleotide Elements/physiology ; Phosphoproteins/metabolism ; RNA, Double-Stranded ; Receptors, Immunologic ; Sequence Analysis, RNA ; Signal Transduction
Chemical Substances	Interferon Type I ; MPHOSPH8 protein, human ; Phosphoproteins ; RNA, Double-Stranded ; Receptors, Immunologic ; RIGI protein, human (EC 3.6.1.-) ; IFIH1 protein, human (EC 3.6.1.-) ; DEAD Box Protein 58 (EC 3.6.4.13) ; Interferon-Induced Helicase, IFIH1 (EC 3.6.4.13)
Language	English
Publishing date	2020-11-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-020-19170-5
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Article ; Online: Inactivation of the type I interferon pathway reveals long double-stranded RNA-mediated RNA interference in mammalian cells.

Maillard, Pierre V / Van der Veen, Annemarthe G / Deddouche-Grass, Safia / Rogers, Neil C / Merits, Andres / Reis e Sousa, Caetano

The EMBO journal

2016 Volume 35, Issue 23, Page(s) 2505–2518

Abstract: RNA interference (RNAi) elicited by long double-stranded (ds) or base-paired viral RNA constitutes the major mechanism of antiviral defence in plants and invertebrates. In contrast, it is controversial whether it acts in chordates. Rather, in vertebrates, ...

Abstract	RNA interference (RNAi) elicited by long double-stranded (ds) or base-paired viral RNA constitutes the major mechanism of antiviral defence in plants and invertebrates. In contrast, it is controversial whether it acts in chordates. Rather, in vertebrates, viral RNAs induce a distinct defence system known as the interferon (IFN) response. Here, we tested the possibility that the IFN response masks or inhibits antiviral RNAi in mammalian cells. Consistent with that notion, we find that sequence-specific gene silencing can be triggered by long dsRNAs in differentiated mouse cells rendered deficient in components of the IFN pathway. This unveiled response is dependent on the canonical RNAi machinery and is lost upon treatment of IFN-responsive cells with type I IFN Notably, transfection with long dsRNA specifically vaccinates IFN-deficient cells against infection with viruses bearing a homologous sequence. Thus, our data reveal that RNAi constitutes an ancient antiviral strategy conserved from plants to mammals that precedes but has not been superseded by vertebrate evolution of the IFN system.
MeSH term(s)	Animals ; Cells, Cultured ; Gene Expression Regulation ; Immunity, Innate ; Interferon Type I/antagonists & inhibitors ; Mice ; RNA Interference ; RNA Viruses/immunology ; RNA, Double-Stranded/metabolism ; RNA, Viral/metabolism
Chemical Substances	Interferon Type I ; RNA, Double-Stranded ; RNA, Viral
Language	English
Publishing date	2016-11-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.201695086
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Article ; Online: The specificity of TRIM5 alpha-mediated restriction is influenced by its coiled-coil domain.

Maillard, Pierre V / Ecco, Gabriela / Ortiz, Millán / Trono, Didier

Journal of virology

2010 Volume 84, Issue 11, Page(s) 5790–5801

Abstract: Retroviruses are both powerful evolutionary forces and dangerous threats to genome integrity. As such, they have imposed strong selective pressure on their hosts, notably triggering the emergence of restriction factors, such as TRIM5 alpha, that act as ... ...

Abstract	Retroviruses are both powerful evolutionary forces and dangerous threats to genome integrity. As such, they have imposed strong selective pressure on their hosts, notably triggering the emergence of restriction factors, such as TRIM5 alpha, that act as potent barriers to their cross-species transmission. TRIM5 alpha orthologues from different primates have distinct retroviral restriction patterns, largely dictated by the sequence of their C-terminal PRYSPRY domain, which binds the capsid protein of incoming virions. Here, by combining genetic and functional analyses of human and squirrel monkey TRIM5 alpha, we demonstrate that the coiled-coil domain of this protein, thus far essentially known for mediating oligomerization, also conditions the spectrum of antiretroviral activity. Furthermore, we identify three coiled-coil residues responsible for this effect, one of which has been under positive selection during primate evolution, notably in New World monkeys. These results indicate that the PRYSPRY and coiled-coil domains cooperate to determine the specificity of TRIM5 alpha-mediated capture of retroviral capsids, shedding new light on this complex event.
MeSH term(s)	Animals ; Base Sequence ; Binding Sites ; Capsid Proteins/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Host-Pathogen Interactions ; Humans ; Macaca ; Protein Structure, Tertiary ; Proteins/chemistry ; Proteins/metabolism ; Retroviridae ; Saimiri ; Species Specificity ; Ubiquitin-Protein Ligases
Chemical Substances	Capsid Proteins ; Carrier Proteins ; Proteins ; TRIM5 protein, human (EC 2.3.2.27) ; TRIM5(alpha) protein, rhesus monkey (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2010-03-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.02413-09
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Article ; Online: Homology-based identification of capsid determinants that protect HIV1 from human TRIM5α restriction.

Maillard, Pierre V / Zoete, Vincent / Michielin, Olivier / Trono, Didier

The Journal of biological chemistry

2010 Volume 286, Issue 10, Page(s) 8128–8140

Abstract: The tropism of retroviruses relies on their ability to exploit cellular factors for their replication as well as to avoid host-encoded inhibitory activities such as TRIM5α. N-tropic murine leukemia virus is sensitive to human TRIM5α (huTRIM5α) ... ...

Abstract	The tropism of retroviruses relies on their ability to exploit cellular factors for their replication as well as to avoid host-encoded inhibitory activities such as TRIM5α. N-tropic murine leukemia virus is sensitive to human TRIM5α (huTRIM5α) restriction, whereas human immunodeficiency virus type 1 (HIV1) escapes this antiviral factor. We previously revealed that mutation of four critical amino acid residues within the capsid can render murine leukemia virus resistant to huTRIM5α. Here, we exploit the high degree of conservation in the tertiary structure of retroviral capsids to map the corresponding positions on the HIV1 capsid. We then demonstrated that, when changes were introduced at some of these positions, HIV1 becomes sensitive to huTRIM5α restriction, a phenomenon reinforced by additionally mutating the nearby cyclophilin A binding loop of the viral protein. These results indicate that retroviruses have evolved similar mechanisms to escape TRIM5α restriction via the interference of structurally homologous determinants in the viral capsid.
MeSH term(s)	Animals ; Capsid Proteins/genetics ; Capsid Proteins/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cells, Cultured ; Evolution, Molecular ; HIV-1/physiology ; Humans ; Leukemia Virus, Murine/physiology ; Murinae ; Mutation ; Protein Structure, Secondary ; Sequence Homology, Amino Acid ; Tripartite Motif Proteins ; Ubiquitin-Protein Ligases ; Virus Replication/physiology
Chemical Substances	Capsid Proteins ; Carrier Proteins ; Tripartite Motif Proteins ; TRIM5 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2010-12-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M110.187609
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Article: Homology-based Identification of Capsid Determinants That Protect HIV1 from Human TRIM5α Restriction

Maillard, Pierre V / Zoete, Vincent / Michielin, Olivier / Trono, Didier

Journal of biological chemistry. 2011 Mar. 11, v. 286, no. 10

2011

Abstract	The tropism of retroviruses relies on their ability to exploit cellular factors for their replication as well as to avoid host-encoded inhibitory activities such as TRIM5α. N-tropic murine leukemia virus is sensitive to human TRIM5α (huTRIM5α) restriction, whereas human immunodeficiency virus type 1 (HIV1) escapes this antiviral factor. We previously revealed that mutation of four critical amino acid residues within the capsid can render murine leukemia virus resistant to huTRIM5α. Here, we exploit the high degree of conservation in the tertiary structure of retroviral capsids to map the corresponding positions on the HIV1 capsid. We then demonstrated that, when changes were introduced at some of these positions, HIV1 becomes sensitive to huTRIM5α restriction, a phenomenon reinforced by additionally mutating the nearby cyclophilin A binding loop of the viral protein. These results indicate that retroviruses have evolved similar mechanisms to escape TRIM5α restriction via the interference of structurally homologous determinants in the viral capsid.
Language	English
Dates of publication	2011-0311
Size	p. 8128-8140.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article ; Online: The RIG-I-like receptor LGP2 inhibits Dicer-dependent processing of long double-stranded RNA and blocks RNA interference in mammalian cells.

van der Veen, Annemarthe G / Maillard, Pierre V / Schmidt, Jan Marten / Lee, Sonia A / Deddouche-Grass, Safia / Borg, Annabel / Kjær, Svend / Snijders, Ambrosius P / Reis e Sousa, Caetano

The EMBO journal

2018 Volume 37, Issue 4

Abstract: In vertebrates, the presence of viral RNA in the cytosol is sensed by members of the RIG-I-like receptor (RLR) family, which signal to induce production of type I interferons (IFN). These key antiviral cytokines act in a paracrine and autocrine manner to ...

Abstract	In vertebrates, the presence of viral RNA in the cytosol is sensed by members of the RIG-I-like receptor (RLR) family, which signal to induce production of type I interferons (IFN). These key antiviral cytokines act in a paracrine and autocrine manner to induce hundreds of interferon-stimulated genes (ISGs), whose protein products restrict viral entry, replication and budding. ISGs include the RLRs themselves: RIG-I, MDA5 and, the least-studied family member, LGP2. In contrast, the IFN system is absent in plants and invertebrates, which defend themselves from viral intruders using RNA interference (RNAi). In RNAi, the endoribonuclease Dicer cleaves virus-derived double-stranded RNA (dsRNA) into small interfering RNAs (siRNAs) that target complementary viral RNA for cleavage. Interestingly, the RNAi machinery is conserved in mammals, and we have recently demonstrated that it is able to participate in mammalian antiviral defence in conditions in which the IFN system is suppressed. In contrast, when the IFN system is active, one or more ISGs act to mask or suppress antiviral RNAi. Here, we demonstrate that LGP2 constitutes one of the ISGs that can inhibit antiviral RNAi in mammals. We show that LGP2 associates with Dicer and inhibits cleavage of dsRNA into siRNAs both
MeSH term(s)	DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; Gene Expression Regulation ; HeLa Cells ; Humans ; Interferon Type I/metabolism ; RNA Helicases/genetics ; RNA Helicases/metabolism ; RNA Interference ; RNA Viruses/physiology ; RNA, Double-Stranded/genetics ; RNA, Double-Stranded/metabolism ; RNA, Small Interfering/genetics ; RNA, Viral/genetics ; Ribonuclease III/genetics ; Ribonuclease III/metabolism ; Signal Transduction
Chemical Substances	Interferon Type I ; RNA, Double-Stranded ; RNA, Small Interfering ; RNA, Viral ; DHX58 protein, human (EC 2.7.7.-) ; DICER1 protein, human (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3) ; DEAD-box RNA Helicases (EC 3.6.4.13) ; RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2018-01-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.201797479
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