Laboratory for Molecular Diagnostics
Center for Nephrology and Metabolic Disorders

Enzyme APOBEC-3G

The APOBEC3G gene encodes a protein of the APOBEC family. Enzymes of this family are responsible for mRNA editing. They introduce base exchanges before the protein is translated, which plays an important role in defense of viral infections and lipid metabolism.

Genetests:

Clinic Method Carrier testing
Turnaround 5
Specimen type genomic DNA
Research Method Genomic sequencing of the entire coding region
Turnaround 25
Specimen type genomic DNA
Clinic Method Massive parallel sequencing
Turnaround 25
Specimen type genomic DNA

Related Diseases:

Disorders of mRNA editing
APOBEC1
APOBEC2
APOBEC3A
APOBEC3B
APOBEC3C
APOBEC3D
APOBEC3F
APOBEC3G
APOBEC3H
APOBEC4

References:

1.

Harris RS et. al. (2002) RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators.

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2.

Jarmuz A et. al. (2002) An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22.

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3.

Sheehy AM et. al. (2002) Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein.

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4.

Zhang H et. al. (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.

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5.

Mangeat B et. al. (2003) Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.

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6.

Harris RS et. al. (2003) DNA deamination mediates innate immunity to retroviral infection.

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7.

Sheehy AM et. al. (2003) The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif.

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8.

Marin M et. al. (2003) HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation.

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9.

Yu X et. al. (2003) Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.

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10.

Schröfelbauer B et. al. (2004) A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif).

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11.

Bogerd HP et. al. (2004) A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor.

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12.

Turelli P et. al. (2004) Inhibition of hepatitis B virus replication by APOBEC3G.

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13.

Xu H et. al. (2004) A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion.

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14.

Zhang J et. al. (2004) Rapid evolution of primate antiviral enzyme APOBEC3G.

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15.

Rösler C et. al. (2004) Comment on "Inhibition of hepatitis B virus replication by APOBEC3G".

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16.

Esnault C et. al. (2005) APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses.

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17.

Chiu YL et. al. (2005) Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells.

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18.

Okeoma CM et. al. (2007) APOBEC3 inhibits mouse mammary tumour virus replication in vivo.

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19.

Wang T et. al. (2007) 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G.

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20.

Chen KM et. al. (2008) Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G.

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21.

Kinoshita SM et. al. (2008) NF-IL6 (C/EBPbeta) induces HIV-1 replication by inhibiting cytidine deaminase APOBEC3G.

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22.

Kamata M et. al. (2009) Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells.

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23.

Santoni de Sio FR et. al. (2009) APOBEC3G-depleted resting CD4+ T cells remain refractory to HIV1 infection.

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24.

Okeoma CM et. al. (2010) APOBEC3 proteins expressed in mammary epithelial cells are packaged into retroviruses and can restrict transmission of milk-borne virions.

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Update: Sept. 26, 2018