Fish Rhabdovirus Cell Entry Is Mediated by Fibronectin

Béarzotti, M.; Delmas, Bernard; Lamoureux, Annie; Loustau, Anne-Marie; Chilmonczyk, Stéfan; Brémont, Michel

doi:10.1128/jvi.73.9.7703-7709.1999

Cited by 83 publications

(43 citation statements)

References 42 publications

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“…However, it seems unlikely that fibronectin is one of the receptors shared with IPNV. Bearzotti, Delmas, Lamoureux, Loustau, Chilmonczyk & Bremont (1999) developed three monoclonal antibodies (Mabs) directed against a viral cell receptor that prevents VHSV infection, and a large panel of other antigenically unrelated fish rhabdoviruses, such as IHNV, but these Mabs did not block IPNV. The data suggests that fibronectin is the main receptor for fish rhabdoviruses, although other co-receptors cannot be ruled out.…”

Section: Discussionsupporting

confidence: 82%

Salmonid fish viruses and cell interactions at early steps of the infective cycle

Heras

Saint-Jean

Pérez-Prieto

2008

Journal of Fish Diseases

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A flow cytometric virus-binding assay that directly visualizes the binding and entry of infectious pancreatic necrosis virus (IPNV), infectious haematopoietic necrosis virus (IHNV) and virus haemorrhagic septicaemia virus (VHSV) to several cell lines was established. The highest efficiency of binding was shown by the BF-2 cell line and this was used to study, at the attachment level, the interactions of these cells with salmonid fish viruses in coinfections, and to further determine if the earliest stage of the viral growth cycle could explain the previously described loss of infectivity of IHNV when IPNV is present. Our results demonstrated that IPNV binds to around 88% of cells either in single or dual infections, whereas IHNV attachment always decreased in the presence of any of the other viruses. VHSV binding was not affected by IPNV, but coinfection with IHNV reduced the percentage of virus-binding cells, which suggests competition for viral receptors or co-receptors. Internalization of the adsorbed IHNV was not decreased by coinfection with IPNV, so the hypothetical competence could be restricted to the binding step. Treatment of the cells with antiviral agents, such as amantadine or chloroquine, did not affect the binding of IPNV and VHSV, but reduced IHNV binding by more than 30%. Tributylamine affected viral binding of the three viruses to different degrees and inhibited IPNV or IHNV entry in a large percentage of cells treated for 30 min. Tributylamine also inhibited IHNV cytopathic effects in a dose-dependent manner, decreasing the virus yield by 4 log of the 50% endpoint titre, at 10 mm concentration. IPNV was also inhibited, but at a lower level. The results of this study support the hypothesis that IHNV, in contrast to VHSV or IPNV, is less efficient at completing its growth cycle in cells with a simultaneous infection with IPNV. It can be affected at several stages of viral infection and is more sensitive to the action of antiviral compounds.

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Section: Discussionsupporting

confidence: 82%

Salmonid fish viruses and cell interactions at early steps of the infective cycle

Heras

Saint-Jean

Pérez-Prieto

2008

Journal of Fish Diseases

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“…In the case of VHSV G protein, a proteinaceous receptor is also likely to be involved in virus entry. Despite its strong binding to PS, studies with inhibitory monoclonal antibodies have identified fibronectin as a VHSV receptor on fish cells [27].…”

Section: Receptor Utilization By Glycoprotein Gmentioning

confidence: 99%

Internalization and Fusion Mechanism of Vesicular Stomatitis Virus and Related Rhabdoviruses

et al. 2009

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Members of the Rhabdoviridae infect a wide variety of animals and plants, and are the causative agents of many important diseases. Rhabdoviruses enter host cells following internalization into endosomes, with the glycoprotein (G protein) mediating both receptor binding to host cells and fusion with the cellular membrane. The recently solved crystal structure of vesicular stomatitis virus G has allowed considerable insight into the mechanism of rhabdovirus entry, in particular the low pH-dependent conformational changes that lead to fusion activation. Rhabdovirus entry shows several distinct features compared with other enveloped viruses; first, the entry process appears to consist of two distinct fusion events, initial fusion into vesicles within endosomes followed by back-fusion into the cytosol; second, the conformational changes in the G protein that lead to fusion activation are reversible; and third, the G protein is structurally distinct from other viral fusion proteins and is not proteolytically cleaved. The internalization and fusion mechanisms of rhabdoviruses are discussed in this article, with a focus on viral systems where the G protein has been studied extensively: vesicular stomatitis virus and rabies virus, as well as viral hemorrhagic septicemia virus.

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“…Although the VSV receptor remains undetermined, proteinaceous receptors for other Rhabdoviruses such as RABV and VHSV have been identified. 2,3 The current model of RABV entry proposes that virions are concentrated at neuromuscular junctions by binding to nicotinic acetylcholine receptor (nAChR). [30][31][32][33][34] This increases the chance of the virion binding to the neural cell adhesion molecule (NCAM) at the presynaptic membranewhich likely acts to facilitate internalization.…”

Section: Host Cell Receptorsmentioning

confidence: 99%

“…34,35 In the case of VHSV, antibodies directed towards fibronectin protected fish cells from infection, and fibronectin was shown to bind VHSV virions, strongly suggesting a role for this protein in viral entry. 2 Although a truly definitive understanding of host cell receptors has not yet been demonstrated for any Rhabdovirus, it is clear that proteinaceous receptors are utilized, that receptors vary between strains, and that attachment and internalization may involve a sequential series of events.…”

Section: Host Cell Receptorsmentioning

confidence: 99%

Entry of Rhabdoviruses Into Animal Cells

Regan

Whittaker

2006

Viral Entry Into Host Cells

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Entry is the first step in the infectious life cycle of a virus. In the case of rhabdoviruses, entry is facilitated exclusively by the envelope glycoprotein G and its interactions with the host cell. For vesicular stomatitis virus (VSV), attachment to the cell surface was thought to be facilitated by interactions with the lipid phosphatidylserine, however recent work suggests that it is in fact initiated by recognition of proteinaeous receptors. Clathrin-mediated endocytosis delivers the virions into endosomes where they have been proposed to traffic to multi-vesicular bodies. There, the viral envelope fuses with internal vesicles in a process mediated by glycoprotein G in a pH- and phosphatidylserine-dependent manner. A clear mechanistic understanding of glycoprotein G mediated fusion has yet to be obtained, however current data suggests that it is likely facilitated by events distinct from Class I or Class II fusion proteins of other viruses. Rhabdoviruses are also notable in that their fusion protein exists in a reversible pH-dependent equilibrium, which prevents irreversible preactivation during assembly, and may prove to be relevant in the mediation of cell-to-cell fusion - an alternate form of viral spread.

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Fish Rhabdovirus Cell Entry Is Mediated by Fibronectin

Cited by 83 publications

References 42 publications

Salmonid fish viruses and cell interactions at early steps of the infective cycle

Salmonid fish viruses and cell interactions at early steps of the infective cycle

Internalization and Fusion Mechanism of Vesicular Stomatitis Virus and Related Rhabdoviruses

Entry of Rhabdoviruses Into Animal Cells

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