Intracellular localisation of Fv1

Yap, Melvyn W.; Stoye, Jonathan P.

doi:10.1016/s0042-6822(02)00053-3

Cited by 19 publications

(19 citation statements)

References 49 publications

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“…This suggests that restriction factor is limiting and can be saturated, or "abrogated," by restricted virus. Consistent with this proposition, natural levels of Fv1 expression appear very low (40). Abrogation therefore provides the basis of a method for studying the interaction between CA and restriction factors.…”

supporting

confidence: 54%

“…However, even with the highest concentration of added VLPs, an appreciable difference in titers of N-MLV and B-MLV was still apparent. We attribute this to the relatively high levels of Fv1 n present in NIH 3T3 cells (40). With BALB/3T3 cells, almost complete abrogation of Fv1 b restriction was seen by N-tropic VLP (Fig.…”

Section: Resultsmentioning

confidence: 81%

“…Alternatively, it seems possible that the intracellular localization of CA during viral egress and ingress plays a critical role. Active Fv1 is found in association with tubules of the trans-Golgi network (40), and it may be that Gag polyprotein never meets Fv1 during its outgoing transit through the cell. In this report we describe experiments designed to address these possibilities, focusing on establishing the relationship between Gag processing and abrogation.…”

mentioning

confidence: 99%

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Capsid Processing Requirements for Abrogation of Fv1 and Ref1 Restriction

Dodding

Bock²,

Yap³

et al. 2005

J Virol

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Murine leukemia virus is restricted in mouse cells lines by a host factor known as Fv1 and in human cell lines by Ref1. Genetic evidence indicates that these restriction factors target the virus capsid (CA) protein. Restriction can be overcome by adding virus at a high multiplicity of infection, indicating that the restriction factors can be saturated. Cells preexposed to restricted virus will allow infection by a second virus which would normally be restricted. This phenomenon is known as abrogation; it provides us with a tool with which to study the interaction of virus with restriction factors. We tested the abilities of several Gag processing mutants to abrogate restriction. Our results show that CA must be cleaved from both p12 and nucleocapsid in order for the incoming virion to interact with the restriction factor. Endogenous expression of properly processed CA, however, failed to abrogate restriction. These results suggest that as well as being processed, CA must also be properly assembled in the form of a condensed viral core in order to interact with Fv1 and Ref1. This polymeric structure may contain restriction factor binding sites not present in monomeric CA.

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supporting

confidence: 54%

Section: Resultsmentioning

confidence: 81%

mentioning

confidence: 99%

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Capsid Processing Requirements for Abrogation of Fv1 and Ref1 Restriction

Dodding

Bock²,

Yap³

et al. 2005

J Virol

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“…Certainly, concentration does not affect the phenotype of Fv1-or Trim5-mediated restriction, since cells transduced with factor and expressing at least 10-fold more protein than seen in nontransduced cells block virus replication at the same stage as cells expressing normal levels of factor (19,38,43; M. Dodding, unpublished data). The three blocks that have been identified represent three different modes of restriction.…”

Section: Discussionmentioning

confidence: 99%

Trim-Cyclophilin A Fusion Proteins Can Restrict Human Immunodeficiency Virus Type 1 Infection at Two Distinct Phases in the Viral Life Cycle

Yap¹,

Dodding²,

Stoye³

2006

J Virol

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“…MTs and dynein facilitate the antiretroviral activity of tripartite motif-containing proteins (TRIMs), a family of proteins that protect cells against retroviral infection, as the efficacy of TRIMs is reduced by MT depolymerization (116,117). Only low levels of another antiviral, called Fv1 (Friend virus susceptibility gene 1), are required for protection of mice against murine leukemia virus (MLV), but localization to MT-associated TGN tubules is critical for its activity (118). The guanine nucleotide exchange factor GEF-H1 is regulated by MT binding and couples MT and Rho-GTPase activity.…”

Section: Modulation Of Host Behavior and Antiviral Responsesmentioning

confidence: 99%

Microtubule Regulation and Function during Virus Infection

Naghavi

Walsh

2017

J Virol

102

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Microtubules (MTs) form a rapidly adaptable network of filaments that radiate throughout the cell. These dynamic arrays facilitate a wide range of cellular processes, including the capture, transport, and spatial organization of cargos and organelles, as well as changes in cell shape, polarity, and motility. Nucleating from MT-organizing centers, including but by no means limited to the centrosome, MTs undergo rapid transitions through phases of growth, pause, and catastrophe, continuously exploring and adapting to the intracellular environment. Subsets of MTs can become stabilized in response to environmental cues, acquiring distinguishing posttranslational modifications and performing discrete functions as specialized tracks for cargo trafficking. The dynamic behavior and organization of the MT array is regulated by MT-associated proteins (MAPs), which include a subset of highly specialized plus-end-tracking proteins (ϩTIPs) that respond to signaling cues to alter MT behavior. As pathogenic cargos, viruses require MTs to transport to and from their intracellular sites of replication. While interactions with and functions for MT motor proteins are well characterized and extensively reviewed for many viruses, this review focuses on MT filaments themselves. Changes in the spatial organization and dynamics of the MT array, mediated by virus-or host-induced changes to MT regulatory proteins, not only play a central role in the intracellular transport of virus particles but also regulate a wider range of processes critical to the outcome of infection.KEYWORDS virus, cytoskeleton, microtubules, nucleation, microtubule-associated proteins, plus-end-tracking proteins T he dense cytosolic environment poses a major barrier to the free movement of macromolecules, making microtubule (MT)-based transport a critical aspect of virus replication. Indeed, almost as soon as these filaments were identified and characterized, virus particles were observed proximal to "microtubuli," with evidence that MTassociated proteins (MAPs) might mediate this association. Chemicals that disrupt MT networks, still commonly used today, were reported to suppress virus infection. Moreover, either infection or expression of viral proteins was observed to alter the organization of these networks, suggesting that MTs not only facilitated infection but were also likely to be actively manipulated by viruses. In subsequent decades an enormous body of work helped unravel how virus particles exploit MT motors to traffic within infected cells, and we direct readers to a recent review of this subject (1). Here, we discuss recent advances in our understanding of how MTs themselves are regulated and function during infection, limiting this minireview to some illustrative examples in each case. TWO ENDS TO THE STORY: THE BASICS OF MT POLARITY AND ORGANIZATIONMTs form through the polymerization of ␣/␤-tubulin heterodimers into polarized filaments that have minus and plus ends (Fig. 1A and B). MTs nucleate through minus-end seeding at MT-organizing cen...

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Intracellular localisation of Fv1

Cited by 19 publications

References 49 publications

Capsid Processing Requirements for Abrogation of Fv1 and Ref1 Restriction

Capsid Processing Requirements for Abrogation of Fv1 and Ref1 Restriction

Trim-Cyclophilin A Fusion Proteins Can Restrict Human Immunodeficiency Virus Type 1 Infection at Two Distinct Phases in the Viral Life Cycle

Microtubule Regulation and Function during Virus Infection

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