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Regulation of Antiviral Innate Immunity Through APOBEC Ribonucleoprotein Complexes

  • Jason D. Salter
  • Bogdan Polevoda
  • Ryan P. Bennett
  • Harold C. SmithEmail author
Chapter
Part of the Subcellular Biochemistry book series (SCBI, volume 93)

Abstract

The DNA mutagenic enzyme known as APOBEC3G (A3G) plays a critical role in innate immunity to Human Immunodeficiency Virus-1 (HIV-1 ). A3G is a zinc-dependent enzyme that mutates select deoxycytidines (dC) to deoxyuridine (dU) through deamination within nascent single stranded DNA (ssDNA) during HIV reverse transcription. This activity requires that the enzyme be delivered to viral replication complexes by redistributing from the cytoplasm of infected cells to budding virions through what appears to be an RNA-dependent process. Once inside infected cells, A3G must bind to nascent ssDNA reverse transcripts for dC to dU base modification gene editing. In this chapter we will discuss data indicating that ssDNA deaminase activity of A3G is regulated by RNA binding to A3G and ribonucleoprotein complex formation along with evidence suggesting that RNA-selective interactions with A3G are temporally and mechanistically important in this process.

Keywords

A3G AID Antiviral APOBEC Crosslinking Crystal structure Cure Cytidine deaminase DNA Gene editing HIV Hypermutation Innate immunity Mass spectrometry Noncoding RNA Protein RNA interactions Ribonucleoprotein particles RNA RNA binding domains 

Abbreviations

A3

Collectively all APOBEC3 proteins, A3A, A3B, A3C, A3D, A3F, A3G, A3H

AID

Activation induced deaminase

APOBEC

Apolipoprotein B editing catalytic unit

CD1

N-terminal domain of dual domain APOBEC proteins

CD2

C-terminal domain of dual domain APOBEC proteins

CLIP-Seq

Crosslinking immunoprecipitation and sequencing of RNA bound to proteins

gRNA

HIV genomic RNA

HIV

Human immunodeficiency virus

hY

Human Y ncRNA

NC

Nucleocapsid portion of HIV Gag

ncRNA

Noncoding RNA

RNP

Ribonucleoprotein particle

RT

Reverse transcriptase

RNA-Seq

RNA sequencing

ssDNA

Single stranded DNA

ZBD

Zinc binding domain

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Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  • Jason D. Salter
    • 1
  • Bogdan Polevoda
    • 2
  • Ryan P. Bennett
    • 1
  • Harold C. Smith
    • 1
    • 2
    Email author
  1. 1.OyaGen, IncRochesterUSA
  2. 2.Department of Biochemistry and Biophysics, School of Medicine and DentistryUniversity of RochesterRochesterUSA

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