Regulation of Antiviral Innate Immunity Through APOBEC Ribonucleoprotein Complexes

Salter, Jason D.; Polevoda, Bogdan; Bennett, Ryan P.; Smith, Harold C.

doi:10.1007/978-3-030-28151-9_6

Cited by 11 publications

(10 citation statements)

References 114 publications

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“…The G4 substrates also induced cooperative AID oligomerization, possibly to enhance deamination efficiency [32]. This binding mode may be unique among the APOBEC family since AID is the only identified member known to bind specific structured DNA [33].…”

Section: Apobec Protein Structuresmentioning

confidence: 90%

“…For example, A3F binds non-substrate ssDNA within a positively charged oligomerization in adjacent L3 loops also has been observed in the A3G structure [57] and at the A3A dimerization interface [58]. The L7 loop forms multiple hydrogen bonds with the Watson-Crick (WC) face of the base at the -1 position of the targeted cytidine [33]. A3G also forms additional watermediated hydrogen bonds with the WC face of the -2 position, which explains the preference for deoxycytidine by A3G at the -2 position [59].…”

Section: Apobec Protein Structuresmentioning

confidence: 94%

“…Although we still lack the complete mechanistic basis for requiring full-length A3G for deamination, the CD1 domain likely provides structural support for the catalytically active domain. CD1 also may participate in nucleic acid binding and dimerization/oligomerization [12,33].…”

Section: Apobec Protein Structuresmentioning

confidence: 99%

“…Many subsequent studies have confirmed the ability of APOBEC proteins to restrict both RNA-and DNA-containing viruses. In this section, we will discuss APOBEC inhibition of virus replication through deaminase-dependent and deaminase-independent mechanisms [1,33,50].…”

Section: Viral Restriction By Apobec Enzymesmentioning

confidence: 99%

See 3 more Smart Citations

The Role of APOBECs in Viral Replication

Xu¹,

Byun²,

Dudley³

2020

Preprint

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Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like (APOBEC) proteins are a diverse and evolutionarily conserved family of cytidine deaminases that provide a variety of functions from tissue-specific gene expression and immunoglobulin diversity to control of viruses and retrotransposons. APOBEC family expansion has been documented among mammalian species, suggesting a powerful selection for their activity. Enzymes with a duplicated zinc-binding domain often have catalytically active and inactive domains, yet both have antiviral function. Although APOBEC antiviral function was discovered through hypermutation of HIV-1 genomes lacking an active Vif protein, much evidence indicates that APOBECs also inhibit virus replication through mechanisms other than mutagenesis. Multiple steps of the viral replication cycle may be affected, although nucleic acid replication is a primary target. Packaging of APOBECs into virions was first noted with HIV-1, yet is not a prerequisite for viral inhibition. APOBEC antagonism may occur in viral producer and recipient cells. Signatures of APOBEC activity include G-to-A and C-to-T mutations in a particular sequence context. The importance of APOBEC activity for viral inhibition is reflected in the identification of numerous viral factors, including Vif, which are dedicated to antagonism of these deaminases. Such viral antagonists often are only partially successful, leading to selection for viral variants.

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Section: Apobec Protein Structuresmentioning

confidence: 90%

Section: Apobec Protein Structuresmentioning

confidence: 94%

Section: Apobec Protein Structuresmentioning

confidence: 99%

Section: Viral Restriction By Apobec Enzymesmentioning

confidence: 99%

See 2 more Smart Citations

The Role of APOBECs in Viral Replication

Xu¹,

Byun²,

Dudley³

2020

Preprint

View full text Add to dashboard Cite

show abstract

“…A3A, A3C et A3H ne contiennent qu'un seul CD, contre deux pour A3B, A3D, A3F et A3G ( figure 2A). Dans le cas des A3 à double domaine, le domaine N-terminal (NTD) est catalytiquement inactif et est responsable de la liaison aux acides nucléiques, tandis que le domaine C-terminal (CTD) porte l'activité désaminase [23][24][25]. Lors de la désamination, une molécule d'eau coordinée dans le site actif par un ion Zn 2+ est déprotonée en ion hydroxyde qui va réagir avec le carbone C4 de la cytosine.…”

Section: Structure Et Activité Enzymatique Des Apobec3unclassified

APOBEC3s: history of an antiviral and mutagenic protein family

Verriez¹,

Marquet²,

Paillart³

et al. 2020

Virologie

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La réponse immunitaire innée est une réponse non spécifique qui constitue la première ligne de défense en cas d'infection, notamment en permettant l'élimination des pathogènes par phagocytose ou apoptose. Au sein des cellules immunitaires, cette réponse innée se caractérise entre autres par la synthèse de protéines nommées facteurs de restriction dont le rôle est d'inhiber la réplication virale. Parmi ces facteurs, les protéines de la famille APOBEC3 (Apolipoprotein B mRNA-editing Enzyme Catalytic polypeptide-like 3 ou A3) constituent des facteurs antiviraux majeurs qui ciblent de nombreux types de virus. L'une des cibles des A3 est le virus de l'immunodéficience humaine de type 1 (VIH-1) : l'activité désaminase de certaines A3 convertit une fraction des cytidines du génome viral en uridines et perturbe son expression. Néanmoins, le VIH-1 contrecarre les A3 en exprimant la protéine Vif qui les inhibe en détournant divers mécanismes cellulaires. Par ailleurs, les APOBEC3 participent au maintien de l'intégrité génétique par l'inhibition des rétroéléments mais contribuent également à la cancérogenèse, à l'image d'A3A et A3B, deux facteurs majeurs dans ce processus. L'éventail de leurs activités, combiné aux récentes études montrant leur implication dans la régulation de virus émergents (Zika, SARS-CoV-2), permettent d'envisager les A3 ainsi que leurs partenaires viraux comme axes thérapeutiques.

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The Role of Ribonucleases in RNA Damage, Inactivation and Degradation

Hia

Takeuchi

2021

RNA Damage and Repair

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Regulation of Antiviral Innate Immunity Through APOBEC Ribonucleoprotein Complexes

Cited by 11 publications

References 114 publications

The Role of APOBECs in Viral Replication

The Role of APOBECs in Viral Replication

APOBEC3s: history of an antiviral and mutagenic protein family

The Role of Ribonucleases in RNA Damage, Inactivation and Degradation

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