Erratum to: HIV-1 Vpu and HIV-2 Env counteract BST-2/tetherin by sequestration in a perinuclear compartment

Hauser, Heiko; Lopez, Lisa A.; Yang, Su Jung; Oldenburg, Jill; Exline, Colin M.; Cannon, Paula M.

doi:10.1186/1742-4690-8-85

Cited by 25 publications

(31 citation statements)

References 1 publication

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“…Even though degradation does not appear to be the primary system by which Vpu counteracts BST-2, sequestration and degradation might be parallel existing and not mutually exclusive mechanisms by which Vpu optimizes the chances to counteract the antiviral effect of tetherin. In agreement with the concept of multiple mechanisms, other viral proteins are able to counteract tetherin function, both by inducing its Ub-dependent endosomal degradation, as in the case of the KHSV K5 protein [82], or by sequestration in a perinuclear compartment, as in the case of the HIV-2 Env [155].…”

Section: Vpu and Tetherinsupporting

confidence: 63%

The Ubiquitin-Conjugating System: Multiple Roles in Viral Replication and Infection

Calistri

Munegato

Carli

et al. 2014

Cells

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Through the combined action of ubiquitinating and deubiquitinating enzymes, conjugation of ubiquitin to a target protein acts as a reversible post-translational modification functionally similar to phosphorylation. Indeed, ubiquitination is more and more recognized as a central process for the fine regulation of many cellular pathways. Due to their nature as obligate intracellular parasites, viruses rely on the most conserved host cell machineries for their own replication. Thus, it is not surprising that members from almost every viral family are challenged by ubiquitin mediated mechanisms in different steps of their life cycle and have evolved in order to by-pass or exploit the cellular ubiquitin conjugating system to maximize their chance to establish a successful infection. In this review we will present several examples of the complex interplay that links viruses and the ubiquitin conjugation machinery, with a special focus on the mechanisms evolved by the human immunodeficiency virus to escape from cellular restriction factors and to exit from infected cells.

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Section: Vpu and Tetherinsupporting

confidence: 63%

The Ubiquitin-Conjugating System: Multiple Roles in Viral Replication and Infection

Calistri

Munegato

Carli

et al. 2014

Cells

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“…SIV does not encode Vpu, but its Nef protein removes tetherin from the membrane [31]. HIV-2 and Ebola envelope glycoproteins also target tetherin [32,33]. Tetherin appears to block release of IAV budding particles [34], and this effect was partially antagonized by the neuraminidase surface protein of influenza virus [35].…”

Section: Reviewmentioning

confidence: 99%

Viral evasion mechanisms of early antiviral responses involving regulation of ubiquitin pathways

Rajsbaum

García‐Sastre

2013

Trends in Microbiology

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Early innate and cell-intrinsic responses are essential to protect host cells against pathogens. In turn, viruses have developed sophisticated mechanisms to establish productive infections, counteracting the host innate immune responses. Increasing evidence indicates that these antiviral factors may have a dual role by directly inhibiting viral replication, as well as by sensing and transmitting signals to induce antiviral cytokines. Recent studies have pointed at new, unappreciated mechanisms of viral evasion of host innate protective responses including manipulating the host ubiquitin system. Viral inhibition of antiviral factors by ubiquitin-dependent degradation is emerging as critical evasion mechanism of the antiviral response. In addition, recent studies have uncovered new mechanisms by which viral encoded proteins inhibit ubiquitin and ubiquitin-like modification of host proteins involved innate immune signaling pathways. Here we discuss recent findings and novel strategies that viruses have developed to counteract these early innate antiviral defenses.

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“…Tetherin also causes the retention of fully formed, mature virions on the surface of cells infected with Vpu-deficient HIV-1 (40). The HIV-1 Vpu protein antagonizes tetherin by causing its degradation and sequestration into a perinuclear compartment away from virus assembly sites (12,13,20,26,33). Moreover, the Nef and envelope proteins from some SIVs (24,29,51,54,73) and the HIV-2 envelope protein (26,31) function as antagonists of tetherin in a species-specific manner.…”

mentioning

confidence: 99%

Feline Tetherin Is Characterized by a Short N-Terminal Region and Is Counteracted by the Feline Immunodeficiency Virus Envelope Glycoprotein

Celestino

Calistri

Vecchio

et al. 2012

J Virol

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dTetherin (BST2) is the host cell factor that blocks the particle release of some enveloped viruses. Two putative feline tetherin proteins differing at the level of the N-terminal coding region have recently been described and tested for their antiviral activity. By cloning and comparing the two reported feline tetherins (called here cBST2 504 and cBST2*) and generating specific derivative mutants, this study provides evidence that feline tetherin has a shorter intracytoplasmic domain than those of other known homologues. The minimal tetherin promoter was identified and assayed for its ability to drive tetherin expression in an alpha interferon-inducible manner. We also demonstrated that cBST2 504 is able to dimerize, is localized at the cellular membrane, and impairs human immunodeficiency virus type 1 (HIV-1) particle release, regardless of the presence of the Vpu antagonist accessory protein. While cBST2 504 failed to restrict wild-type feline immunodeficiency virus (FIV) egress, FIV mutants, bearing a frameshift at the level of the envelope-encoding region, were potently blocked. The transient expression of the FIV envelope glycoprotein was able to rescue mutant particle release from feline tetherin-positive cells but did not antagonize human BST2 activity. Moreover, cBST2 504 was capable of specifically immunoprecipitating the FIV envelope glycoprotein. Finally, cBST2 504 also exerted its function on HIV-2 ROD10 and on the simian immunodeficiency virus SIVmac239. Taken together, these results show that feline tetherin does indeed have a short N-terminal region and that the FIV envelope glycoprotein is the predominant factor counteracting tetherin restriction.

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Erratum to: HIV-1 Vpu and HIV-2 Env counteract BST-2/tetherin by sequestration in a perinuclear compartment

Cited by 25 publications

References 1 publication

The Ubiquitin-Conjugating System: Multiple Roles in Viral Replication and Infection

The Ubiquitin-Conjugating System: Multiple Roles in Viral Replication and Infection

Viral evasion mechanisms of early antiviral responses involving regulation of ubiquitin pathways

Feline Tetherin Is Characterized by a Short N-Terminal Region and Is Counteracted by the Feline Immunodeficiency Virus Envelope Glycoprotein

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