Vif of Feline Immunodeficiency Virus from Domestic Cats Protects against APOBEC3 Restriction Factors from Many Felids

Zielonka, Jörg; Marino, Daniela; Hofmann, Henning; Yuhki, Naoya; Löchelt, Martin; Münk, Carsten

doi:10.1128/jvi.00209-10

Cited by 48 publications

(122 citation statements)

References 58 publications

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“…The CBF-␤ gene sequence was submitted to GenBank under accession number KM250107. (49,52). To test if feline CBF-␤ interacts with FIV Vif, we first cloned the CBF-␤ gene from a Chinese domestic cat.…”

Section: Cbf-␤-kd 293t Cell Generationmentioning

confidence: 99%

Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation

Zhu

Wang

et al. 2014

J Virol

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Viral infectivity factor (Vif) is required for lentivirus fitness and pathogenicity, except in equine infectious anemia virus (EIAV).Vif enhances viral infectivity by a Cullin5-Elongin B/C E3 complex to inactivate the host restriction factor APOBEC3. Corebinding factor subunit beta (CBF-␤) is a cell factor that was recently shown to be important for the primate lentiviral Vif function. Non-primate lentiviral Vif also degrades APOBEC3 through the proteasome pathway. However, it is unclear whether CBF-␤ is required for the non-primate lentiviral Vif function. In this study, we demonstrated that the Vifs of non-primate lentiviruses, including feline immunodeficiency virus (FIV), bovine immunodeficiency virus (BIV), caprine arthritis encephalitis virus (CAEV), and maedi-visna virus (MVV), do not interact with CBF-␤. In addition, CBF-␤ did not promote the stability of FIV, BIV, CAEV, and MVV Vifs. Furthermore, CBF-␤ silencing or overexpression did not affect non-primate lentiviral Vif-mediated APOBEC3 degradation. Our results suggest that non-primate lentiviral Vif induces APOBEC3 degradation through a different mechanism than primate lentiviral Vif. IMPORTANCEThe APOBEC3 protein family members are host restriction factors that block retrovirus replication. Vif, an accessory protein of lentivirus, degrades APOBEC3 to rescue viral infectivity by forming Cullin5-Elongin B/C-based E3 complex. CBF-␤ was proved to be a novel regulator of primate lentiviral Vif function. In this study, we found that CBF-␤ knockdown or overexpression did not affect FIV Vif's function, which induced polyubiquitination and degradation of APOBEC3 by recruiting the E3 complex in a manner similar to that of HIV-1 Vif. We also showed that other non-primate lentiviral Vifs did not require CBF-␤ to degrade APOBEC3. CBF-␤ did not interact with non-primate lentiviral Vifs or promote their stability. These results suggest that a different mechanism exists for the Vif-APOBEC interaction and that non-primates are not suitable animal models for exploring pharmacological interventions that disrupt Vif-CBF-␤ interaction.

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Section: Cbf-␤-kd 293t Cell Generationmentioning

confidence: 99%

Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation

Zhu

Wang

et al. 2014

J Virol

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“…These restriction factors are incorporated into the progeny virions and enzymically convert viral cDNA cytosines to uracils during reverse transcription, which can debilitate viral function (Albin & Harris, 2010;Desimmie et al, 2014;Feng et al, 2014;Kitamura et al, 2011;Refsland & Harris, 2013). Although original studies focused on human APOBEC3G (Harris et al, 2003;Mariani et al, 2003;Sheehy et al, 2002;Zhang et al, 2003), subsequent work revealed that all placental mammals have APOBEC3 enzymes (Münk et al, 2012), albeit different numbers, and that these enzymes have the potential to attenuate the infectivity of a broad spectrum of viruses, including simian immunodeficiency virus (SIV) (Mariani et al, 2003), feline immunodeficiency virus (FIV) (Münk et al, 2008;Zielonka et al, 2010), bovine immunodeficiency virus (BIV) (LaRue et al, 2010) and small ruminant lentiviruses (SRLVs; e.g. Maedi-Visna virus and caprine arthritis encephalitis virus) (LaRue et al, 2010).…”

mentioning

confidence: 99%

“…It is known that domestic cat (F. catus) expresses five kinds of APOBEC3 proteins, APOBEC3Z2a, APOBEC3Z2b, APOBEC3Z2c, APOBEC3Z3 and APOBEC3Z2Z3 (LaRue et al, 2010;Münk et al, 2008;Stern et al, 2010;Zielonka et al, 2010), and that feline APOBECZ3 and APOBEC3Z2Z3 have the ability to restrict FIV infectivity (Zielonka & Münk, 2011). To determine whether CBF-b was required for FIV Vif as a co-factor to degrade feline APOBEC3s, we constructed a FLAG-tagged FIV Vif expression plasmid as follows: the codon-optimized ORF of FIV strain Petaluma with a FLAG-tag at the C terminus (the sequence is available upon request) was obtained from GeneArt Gene Synthesis service (Life Technologies).…”

mentioning

confidence: 99%

Vif determines the requirement for CBF-β in APOBEC3 degradation

Yoshikawa

Takeuchi

Yamada

et al. 2015

Journal of General Virology

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APOBEC3 (apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3) proteins are cellular DNA deaminases that restrict a broad spectrum of lentiviruses. This process is counteracted by Vif (viral infectivity factor) of lentiviruses, which binds APOBEC3s and promotes their degradation. CBF-b (core binding factor subunit b) is an essential co-factor for the function of human immunodeficiency virus type 1 Vif to degrade human APOBEC3s. However, the requirement for CBF-b in Vif-mediated degradation of other mammalian APOBEC3 proteins is less clear. Here, we determined the sequence of feline CBFB and performed phylogenetic analyses. These analyses revealed that mammalian CBFB is under purifying selection. Moreover, we demonstrated that CBF-b is dispensable for feline immunodeficiency virus Vif-mediated degradation of APOBEC3s of its host. These findings suggested that primate lentiviruses have adapted to use CBF-b, an evolutionary stable protein, to counteract APOBEC3 proteins of their hosts after diverging from other lentiviruses.

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“…It is currently unknown whether genetic adaptation to the new host occurs, for instance, in genes that are at the forefront of hostpathogen interactions (10,11). Here, host-encoded antiviral restriction factors like APOBEC3 cytidine deaminases and the viral proteins counteracting this restriction, like the lentiviral Vif and the FV Bet proteins, are prominent examples for rapid coevolution and cospeciation (12,13,14,15).…”

mentioning

confidence: 99%

Similar Patterns of Infection with Bovine Foamy Virus in Experimentally Inoculated Calves and Sheep

Materniak

Hechler

Löchelt

et al. 2013

J Virol

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bFoamy viruses (FVs) are the least known retroviruses commonly found in primates, cats, horses, and cattle. Although FVs are considered apathogenic, simian and feline FVs have been shown to be associated with some transient health abnormalities in animal models. Currently, data regarding the course of infection with bovine FV (BFV) are not available. In this study, we conducted experimental infections of natural (cattle) and heterologous (sheep) hosts with the BFV 100 isolate and monitored infection patterns in both hosts during the early phase postinoculation as well as after long-term infection. Four calves and six sheep inoculated with BFV 100 showed no signs of pathology but developed persistent infection, as confirmed by virus rescue, consistent detection of BFV-specific antibodies, and presence of viral DNA. In both hosts, antibodies against BFV Gag and Bet appeared early after infection and persisted at high and stable levels while seroreactivity toward Env was consistently detectable only in BFV-infected sheep. Interestingly, the BFV proviral DNA load was highest in lung, spleen, and liver and moderate in leukocytes, while salivary glands contained either low or undetectable DNA loads in calves or sheep, respectively. Additionally, comparison of partial BFV sequences from inoculum and infected animals demonstrated very limited changes after long-term infection in the heterologous host, clearly less than those found in BFV field isolates. The persistence of BFV infection in both hosts suggests full replication competence of the BFV 100 isolate with no requirement of genetic adaptation for productive replication in the authentic and even in a heterologous host.

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Vif of Feline Immunodeficiency Virus from Domestic Cats Protects against APOBEC3 Restriction Factors from Many Felids

Cited by 48 publications

References 58 publications

Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation

Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation

Vif determines the requirement for CBF-β in APOBEC3 degradation

Similar Patterns of Infection with Bovine Foamy Virus in Experimentally Inoculated Calves and Sheep

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