Studies on in vitro Interferon induction capacity and Interferon sensitivity of Simian Foamy viruses

Rhodes-Feuillette, A.; Saal, F; Lasneret, J; Santillana-Hayat, Maud; Périès, J.

doi:10.1007/bf01310735

Cited by 16 publications

(13 citation statements)

References 21 publications

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“…IFN partially abrogates reactivation of latent FV by PMA. The antiviral effects of interferons on FV replication in fully permissive cell types is well documented (27)(28)(29)(30) PMA (Fig. 5).…”

Section: Expression Of Pml-binding Domain Of Tas Does Not Induce Fv Rmentioning

confidence: 94%

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The Promyelocytic Leukemia Protein Does Not Mediate Foamy Virus Latency In Vitro

Meiering

Linial

2003

J Virol

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Section: Expression Of Pml-binding Domain Of Tas Does Not Induce Fv Rmentioning

confidence: 94%

“…The effects of overexpressed or IFN-induced PML on FV replication are evident (27). However, FVs have apparently evolved a replication strategy that does not induce IFN (14,29). Therefore, the role of PML in FV biology remains unclear.…”

Section: Discussionmentioning

confidence: 99%

The Promyelocytic Leukemia Protein Does Not Mediate Foamy Virus Latency In Vitro

Meiering

Linial

2003

J Virol

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“…Innate immune system sensing of FV infections is poorly characterized. A failure of FVs to induce type I interferon (IFN-I) was suggested by early studies using primate or human cell lines [73,74,75]. A very recent study by Rua and colleagues, however, demonstrates that FVs are efficiently sensed by primary human hematopoietic cells [76].…”

Section: Innate Sensing and Cellular Restriction Factors Of Fvsmentioning

confidence: 99%

Early Events in Foamy Virus—Host Interaction and Intracellular Trafficking

Berka

Hamann

Lindemann

2013

Viruses

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Here we review viral and cellular requirements for entry and intracellular trafficking of foamy viruses (FVs) resulting in integration of viral sequences into the host cell genome. The virus encoded glycoprotein harbors all essential viral determinants, which are involved in absorption to the host membrane and triggering the uptake of virus particles. However, only recently light was shed on some details of FV’s interaction with its host cell receptor(s). Latest studies indicate glycosaminoglycans of cellular proteoglycans, particularly heparan sulfate, to be of utmost importance. In a species-specific manner FVs encounter endogenous machineries of the target cell, which are in some cases exploited for fusion and further egress into the cytosol. Mostly triggered by pH-dependent endocytosis, viral and cellular membranes fuse and release naked FV capsids into the cytoplasm. Intact FV capsids are then shuttled along microtubules and are found to accumulate nearby the centrosome where they can remain in a latent state for extended time periods. Depending on the host cell cycle status, FV capsids finally disassemble and, by still poorly characterized mechanisms, the preintegration complex gets access to the host cell chromatin. Host cell mitosis finally allows for viral genome integration, ultimately starting a new round of viral replication.

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“…Specifically, it was reported that ␥-IFN delayed the cultivation of FVs and, furthermore, that the likelihood of isolating FV from naturally infected host cells was strongly enhanced by the addition of antibodies to ␥-IFN to the culture medium (15). These findings point to the vulnerability of FV replication to the IFN system although FVs are not regarded as superb IFN inducers (51).…”

Section: Analysis Of Pfv Revertants and Pseudo-revertants In Gagmentioning

confidence: 99%

“…Early reports on the IFN-dependence of FV replication (50,51) were the rationale behind this experiment. Specifically, it was reported that ␥-IFN delayed the cultivation of FVs and, furthermore, that the likelihood of isolating FV from naturally infected host cells was strongly enhanced by the addition of antibodies to ␥-IFN to the culture medium (15).…”

Section: Analysis Of Pfv Revertants and Pseudo-revertants In Gagmentioning

confidence: 99%

Basic Residues in the Foamy Virus Gag Protein

Matthes

Wiktorowicz

Zahn

et al. 2011

J Virol

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Two subfamilies comprise the family of exogenous retroviruses: the orthoretroviruses, made up of six genera (␣-to ε-retroviruses and lentiviruses), and the spumaretroviruses, comprised exclusively of the foamy virus (FV) genus (33). There are major differences in the replication strategies between both subfamilies which are responsible for this distinction (32, 48).On a structural level, this is reflected by very unusual FV Gag proteins, which are not cleaved by the viral protease (PR) into matrix (MA), capsid (CA), and nucleocapsid (NC) subunits (32, 48). Instead, the FV PR cleaves only a small peptide (p3 in case of the prototypic FV [PFV]) from the C terminus of FV Gag proteins (17,44). This C-terminal cleavage is essential for FV replication (13, 76). Complete proteolytic cleavage of the capsid occurs most likely in the process of uncoating after fusion with new cells and uses unconventional cleavage sites (19,28).The FV Env protein constitutes another peculiarity. In contrast to orthoretroviral Envs, which are-with surface (SU) and transmembrane (TM) subunits-bipartite in nature (22), the FV Env is a tripartite protein that bears, in addition to SU and TM, a membrane-spanning type II and particle-associated leader peptide (LP), which has a mass of 18 kDa in the case of PFV (30,31). The LP of the PFV Env protein is oligo-ubiquitinated and appears to perform functions in viral replication which are confined to Gag in orthoretroviruses (62).FV capsids do not bud spontaneously from the plasma membrane and do not naturally form virus-like particles (VLPs) (16). They require the presence of authentic Env for cellular export (45). Furthermore, pseudotyping of unmodified FV capsids with other (viral) glycoproteins appears to be impossible (45). On the other hand, pseudotyping of other viral capsids by FV Env and, in particular, by mutants in the ubiquitination sites of LP, is very efficient (72). In FVs, domains on the side of Env particularly located in LP are essential for a specific contact with Gag (31).With Gag, the situation is less clear. Deletion studies suggested that approximately the first 100 amino acids of the 648 residues of PFV Gag are essential to mediate the specific Env interaction (6).Some other domains in the PFV Gag protein have been characterized. A cytoplasmic targeting and retention signal (CTRS) is located in the N-terminal domain (amino acids [aa] 43 to 60) (12). A late (L) domain, specified by the motif PSAP (aa 284 to 287) interacts with the cellular export machinery (vacuolar protein sorting [VPS]) via TSG101 for complete release of virus particles from the plasma membrane (41, 61). However, ubiquitination of PFV Gag has not been found, while ubiquitination is a common feature of orthoretroviral capsids upon interaction with the VPS machinery (46,77).Four coiled-coil (CC) motifs (CC1 to CC4) are predicted to be present in PFV Gag. The CC1 motif is very N-terminally (aa 4 to 19) located, and mutations in this region indicated an interaction domain with Env (29). The CC2 (aa 133 to 146)...

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Studies on in vitro Interferon induction capacity and Interferon sensitivity of Simian Foamy viruses

Cited by 16 publications

References 21 publications

The Promyelocytic Leukemia Protein Does Not Mediate Foamy Virus Latency In Vitro

The Promyelocytic Leukemia Protein Does Not Mediate Foamy Virus Latency In Vitro

Early Events in Foamy Virus—Host Interaction and Intracellular Trafficking

Basic Residues in the Foamy Virus Gag Protein

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