Involvement of Gangliosides in Rabies Virus Infection

Superti, Fabiana; Hauttecoeur, Bernard; Morelec, M J; Goldoni, Paola; Bizzini, B; Tsiang, H

doi:10.1099/0022-1317-67-1-47

Cited by 90 publications

(43 citation statements)

References 40 publications

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“…In earlier reports we demonstrated that the lysosomal entry pathway is involved in the infection of non-neuronal cells as well as neurons Tsiang & Superti, 1984). Furthermore highly sialylated gangliosides may participate in these early steps of viral entry into the target cell (Superti et al, 1986;Conti et al, 1988). From our present results we infer that there are presumably two different mechanisms of viral entry into the cell.…”

Section: Retrograde and Anterograde Transport Of Rabies Virus In A Musupporting

confidence: 31%

“…Rabies virus infects a great variety of neuronal cell lines (Clark, 1978;Honda et al, 1984;Iwasaki & Clark, 1977;Tsiang et al, 1983a) as well as primary dissociated neuron cultures (Lycke & Tsiang, 1987;Tsiang et al, 1983aTsiang et al, , b, 1986. Whereas conventional neuronal cultures are less appropriate for the investigation of viral transport, neurons cultivated in a compartmentalized culture system as described by Campenot (1977) will demonstrate convincingly the transport of herpes simplex virus in vitro (Kristensson et al, 1986;Lycke et al, 1984;Ziegler & Herman, 1980) and the retrograde transport of both fixed and street rabies viruses in cultured rat sensory neurons (Lycke & Tsiang, 1987;Tsiang, 1988).…”

Section: Introductionmentioning

confidence: 99%

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The Anterograde Transport of Rabies Virus in Rat Sensory Dorsal Root Ganglia Neurons

Tsiang¹,

Lycke²,

Ceccaldi³

et al. 1989

Journal of General Virology

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SUMMARYWe have previously described the capacity of neurites extending from cultured rat sensory dorsal root ganglia (DRG) neurons to transport rabies virus through axoplasm in the retrograde direction. Here we report the infection of cultured neurons derived from the DRG and the subsequent anterograde transport of rabies virus from the infected cell somas through the extending neurites to its release into the culture supernatant. Viral transport was monitored by titration of the virus yield in the external compartment. Both early and late transport mechanisms of rabies virions were identified. The first one occurred a few hours post-infection and was undetectable 6 h later, before the initiation of viral replication. The velocity of this first wave of infective virions was in the range of 100 to 400 mm/day. The early viral transport was probably the result of a direct translocation of infective virions from the somatic site of entry to the neuritic extensions and subsequent release into the culture medium without replication in the cellular perikaryon. The second virus transport peak was detected 48 h post-infection. In this case, the virions detected in the neuritic compartment were presumably the progeny of the inoculated virus which had replicated in the perikaryon before the viral transport occurs. Using a four-compartment culture device we were able to demonstrate, simultaneously, retrograde and anterograde transport of the virus. The presence of antirabies serum in contact with the exposed neurites did not inhibit either the retrograde or the anterograde transport mechanisms. The viral release from the neuritic extensions after the fast anterograde transport was evaluated to be in the range of 150 to 300 infectious virions per bundle of neurites per day.

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Section: Retrograde and Anterograde Transport Of Rabies Virus In A Musupporting

confidence: 31%

Section: Introductionmentioning

confidence: 99%

The Anterograde Transport of Rabies Virus in Rat Sensory Dorsal Root Ganglia Neurons

Tsiang¹,

Lycke²,

Ceccaldi³

et al. 1989

Journal of General Virology

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“…Gangliosides, principally GD1b, GQ1b, and GT1b, have also been proposed to play a role in RV binding (48). While some of these gangliosides are prevalently found in subpopulations of DRG neurons, none have the specific expression pattern that is found in infected neurons (20).…”

Section: Discussionmentioning

confidence: 99%

The Rabies Virus Glycoprotein Receptor p75 ^NTR Is Not Essential for Rabies Virus Infection

Tuffereau

Schmidt

Langevin

et al. 2007

J Virol

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Rabies virus glycoprotein (RVG) is known to be the only factor that mediates rabies infection. The neurotrophin receptor (p75 NTR ), through its cysteine-rich domain 1, is a specific receptor for RVG and neutralizes virus infectivity, but its role in virus infection has remained obscure. We used adult mouse dorsal root ganglion (DRG) neurons as a model to study the role of p75 NTR in RV infection of primary neurons. We show that RV infects around 20% of DRG neurons, of which more than 80% are p75 NTR positive, have large diameters, and are capsaicin insensitive. Surprisingly, RV binding and infection are absent in about half of the p75 NTRexpressing DRG neurons which have small diameters and are often capsaicin sensitive. This indicates that p75 NTR is not sufficient to mediate RV interaction in sensory neurons. The rate and specificity of neural infection are unchanged in RV-infected p75 NTRExonIV؊/؊ mice that lack all extracellular receptor domains and in wild-type mice infected with two independent RV mutants that lack p75 NTR binding. Accordingly, the mortality rate is unchanged in the absence of RV-p75 NTR interaction. We conclude that although p75 NTR is a receptor for soluble RVG in transfected cells of heterologous expression systems, an RVG-p75 NTR interaction is not necessary for RV infection of primary neurons. This means that other receptors are required to mediate RV infection in vivo and in vitro.Rabies causes severe progressive encephalitis, myelitis, and paralysis and affects more than 50,000 people worldwide each year (59). After onset of symptoms, the infection progresses relentlessly, and there is only one documented case of a nonvaccinated human patient who survived the disease (56). Rabies virus (RV) belongs to the genus Lyssavirus in the family Rhabdoviridae and is a simple, enveloped, nonsegmented, negative-strand RNA virus that encodes only five proteins (44). The glycoprotein (G) is known to be the only protein component of the viral envelope that mediates viral entry into host cells (44).RV is highly neurotropic, and after inoculation it is retrogradely transported by peripheral neurons before being passed on to second and higher-order neurons without being taken up by glia. It is this unique property of the virus that makes it a useful transsynaptic neuronal tracer over many synapses (28,52), which is dependent on RVG (17).Although several receptors have been suggested to be responsible for RV infection, none has been conclusively identified. In previous studies we adopted an expression cloning strategy using a soluble form of RVG as a ligand. That work identified the neurotrophin receptor p75 NTR as a unique interacting receptor (50). We have also shown that the glycoprotein from another lyssavirus genotype (EBL2) is also able to interact with p75 NTR (51). p75 NTR belongs to the tumor necrosis factor receptor family (11,14) and is the common receptor for all known mature neurotrophins as well immature proneurotrophins (35). In addition, several other ligands implicated in the patholo...

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“…In the case of VSV, although phosphatidylserine has been considered to be the viral receptor for a long time [17], recent results indicated that it is not [18]. In the case of RV, many molecules, including gangliosides [19], phospholipids [20], the nicotinic acetylcholine receptor [21,22], neuronal cellular adhesion molecules [23] and the low-affinity nerve growth factor receptor [24], have been proposed to be viral receptors. After binding, the virions enter the cell by the endocytic pathway.…”

Section: Rhabdovirus Glycoprotein Gmentioning

confidence: 99%

Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited

Roche

Albertini

Lepault

et al. 2008

Cell. Mol. Life Sci.

124

138

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Abstract. Glycoprotein G of the vesicular stomatitis virus (VSV) is involved in receptor recognition at the host cell surface and then, after endocytosis of the virion, triggers membrane fusion via a low pHinduced structural rearrangement. G is an atypical fusion protein, as there is a pH-dependent equilibrium between its pre-and post-fusion conformations. The atomic structures of these two conformations reveal that it is homologous to glycoprotein gB of herpesviruses and that it combines features of the previously characterized class I and class II fusion proteins.Comparison of the structures of G pre-and postfusion states shows a dramatic reorganization of the molecule that is reminiscent of that of paramyxovirus fusion protein F. It also allows identification of conserved key residues that constitute pH-sensitive molecular switches. Besides the similarities with other viral fusion machineries, the fusion properties and structures of G also reveal some striking particularities that invite us to reconsider a few dogmas concerning fusion proteins.

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Involvement of Gangliosides in Rabies Virus Infection

Cited by 90 publications

References 40 publications

The Anterograde Transport of Rabies Virus in Rat Sensory Dorsal Root Ganglia Neurons

The Anterograde Transport of Rabies Virus in Rat Sensory Dorsal Root Ganglia Neurons

The Rabies Virus Glycoprotein Receptor p75 ^NTR Is Not Essential for Rabies Virus Infection

Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited

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Involvement of Gangliosides in Rabies Virus Infection

Cited by 90 publications

References 40 publications

The Anterograde Transport of Rabies Virus in Rat Sensory Dorsal Root Ganglia Neurons

The Anterograde Transport of Rabies Virus in Rat Sensory Dorsal Root Ganglia Neurons

The Rabies Virus Glycoprotein Receptor p75 NTR Is Not Essential for Rabies Virus Infection

Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited

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The Rabies Virus Glycoprotein Receptor p75 ^NTR Is Not Essential for Rabies Virus Infection