An Endoplasmic Reticulum Retrieval Signal Partitions Human Foamy Virus Maturation to Intracytoplasmic Membranes

Goepfert, Paul; Shaw, Kit L.; Wang, George; Edwards, Bradley H.; Mulligan, Mark J.

doi:10.1128/jvi.73.9.7210-7217.1999

Cited by 38 publications

(14 citation statements)

References 50 publications

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“…This localization directs budding of these spumaviruses to intracellular membranes (Shaw et al, 2003). Although the dilysine motif of spumaviruses imposes a partial restriction on the site of viral maturation, it is not necessary for virion formation (Goepfert et al, 1999).…”

Section: Subcellular Localization Signals In Envelope Glycoproteinsmentioning

confidence: 99%

Interactions Between Virus Proteins and Host Cell Membranes During the Viral Life Cycle

Villanueva

Rouillé

Dubuisson

2005

International Review of Cytology

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The structure and function of cells are critically dependent on membranes, which not only separate the interior of the cell from its environment but also define the internal compartments. It is therefore not surprising that the major steps of the life cycle of viruses of animals and plants also depend on cellular membranes. Indeed, interactions of viral proteins with host cell membranes are important for viruses to enter into host cells, replicate their genome, and produce progeny particles. To replicate its genome, a virus first needs to cross the plasma membrane. Some viruses can also modify intracellular membranes of host cells to create a compartment in which genome replication will take place. Finally, some viruses acquire an envelope, which is derived either from the plasma membrane or an internal membrane of the host cell. This paper reviews recent findings on the interactions of viral proteins with host cell membranes during the viral life cycle.

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Section: Subcellular Localization Signals In Envelope Glycoproteinsmentioning

confidence: 99%

Interactions Between Virus Proteins and Host Cell Membranes During the Viral Life Cycle

Villanueva

Rouillé

Dubuisson

2005

International Review of Cytology

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“…In contrast, we have found that PFV Env is absent from the pericentriolar assembly site, suggesting a separate subcellular compartment required for Gag–Env interaction. Previous work described an endoplasmic reticulum retention signal (ERRS) in the FV Env protein (19–21), a motif also found in the glycoprotein of HBV. It was therefore surprising to find that co‐localization of Gag and Env of PFV was not detected in ER or in late endosomes/MVB, but in the trans ‐Golgi network (TGN), suggesting a possible location for envelopment and/or budding of FV capsids.…”

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confidence: 99%

Foamy Virus Capsid Assembly Occurs at a Pericentriolar Region Through a Cytoplasmic Targeting/Retention Signal in Gag

Eastman

Linial

2006

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Foamy viruses (FV) are unusual retroviruses that differ in many aspects of their life cycle from the orthoretroviruses such as human immunodeficiency virus. Similar to Mason-Pfizer monkey virus (MPMV), FV assemble into capsids intracellularly. The capsids are then transported to a cellular membrane for acquisition of envelope (Env) glycoproteins and budding. However, unlike MPMV, budding of FV is dependent upon the presence of Env. Previous work suggested that FV Env proteins are localized to the endoplasmic reticulum (ER) where budding takes place. However, very little was known about the details of FV assembly. We have used immunofluorescence and electron microscopy to visualize the intracellular location of FV assembly and budding. We have found that, as in the case of MPMV, FV capsids assemble at a pericentriolar site in the cytoplasm. Surprisingly, FV Env is mostly absent from this site and, contrary to expectations, FV capsid structural protein (Gag) is absent from the ER. Gag and Env only co-localize at the transGolgi network, suggesting that Env-Gag interactions that are required for viral egress from the cell, occurs at this site. Finally, inhibitor studies suggest an important role of microtubule networks for foamy viral assembly and budding.

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“…The envelope glycoprotein from the retrovirus human foamy virus also contains a dilysine signal (15,16). This dilysine signal directs budding of this virus into intracellular compartments (14). Other types of targeting signals have been identified in envelope proteins of viruses that assemble at the ERGIC or Golgi, although the mechanism by which they work is not understood (reviewed in reference 21).…”

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confidence: 99%

Intracellular Targeting Signals Contribute to Localization of Coronavirus Spike Proteins near the Virus Assembly Site

Lontok

Corse

Machamer

2004

J Virol

151

196

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Coronavirus budding at the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) requiresaccumulation of the viral envelope proteins at this point in the secretory pathway. Here we demonstrate that the spike (S) protein from the group 3 coronavirus infectious bronchitis virus (IBV) contains a canonical dilysine endoplasmic reticulum retrieval signal (-KKXX-COOH) in its cytoplasmic tail. This signal can retain a chimeric reporter protein in the ERGIC and when mutated allows transport of the full-length S protein as well as the chimera to the plasma membrane. Interestingly, the IBV S protein also contains a tyrosine-based endocytosis signal in its cytoplasmic tail, suggesting that any S protein that escapes the ERGIC will be rapidly endocytosed when it reaches the plasma membrane. We also identified a novel dibasic motif (-KXHXX-COOH) in the cytoplasmic tails of S proteins from group 1 coronaviruses and from the newly identified coronavirus implicated in severe acute respiratory syndrome. This dibasic motif also retained a reporter protein in the ERGIC, similar to the dilysine motif in IBV S. The cytoplasmic tails of S proteins from group 2 coronaviruses lack an intracellular localization signal. The inherent differences in S-protein trafficking could point to interesting variations in pathogenesis of coronaviruses, since increased levels of surface S protein could promote syncytium formation and direct cell-to-cell spread of the infection.

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An Endoplasmic Reticulum Retrieval Signal Partitions Human Foamy Virus Maturation to Intracytoplasmic Membranes

Cited by 38 publications

References 50 publications

Interactions Between Virus Proteins and Host Cell Membranes During the Viral Life Cycle

Interactions Between Virus Proteins and Host Cell Membranes During the Viral Life Cycle

Foamy Virus Capsid Assembly Occurs at a Pericentriolar Region Through a Cytoplasmic Targeting/Retention Signal in Gag

Intracellular Targeting Signals Contribute to Localization of Coronavirus Spike Proteins near the Virus Assembly Site

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