Lipid rafts play an important role in the vesicular stomatitis virus life cycle

Chandipura virus, a member of the rhabdoviridae family and vesiculovirus genera, has recently emerged as human pathogen that is associated with a number of outbreaks in different parts of India. Although, the virus closely resembles with the prototype vesiculovirus, Vesicular Stomatitis Virus, it could be readily distinguished by its ability to infect humans. Studies on Chandipura virus while shed light into distinct stages of viral infection; it may also allow us to identify potential drug targets for antiviral therapy. In this review, we have summarized our current understanding of Chandipura virus life cycle at the molecular detail with particular interest in viral RNA metabolisms, namely transcription, replication and packaging of viral RNA into nucleocapsid structure. Contemporary research on otherwise extensively studied family member Vesicular Stomatitis Virus has also been addressed to present a more comprehensive picture of vesiculovirus life cycle. Finally, we reveal examples of protein economy in Chandipura virus life-cycle whereby each viral protein has evolved complexity to perform multiple tasks.

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Pseudotypes of Vesicular Stomatitis Virus with CD4 Formed by Clustering of Membrane Microdomains during Budding

Journal of Virology ◽

10.1128/jvi.79.11.7077-7086.2005 ◽

2005 ◽

Vol 79 (11) ◽

pp. 7077-7086 ◽

Cited By ~ 10

Author(s):

Erica L. Brown ◽

Douglas S. Lyles

Keyword(s):

Plasma Membrane ◽

G Protein ◽

Lipid Rafts ◽

Immunoelectron Microscopy ◽

Vesicular Stomatitis Virus ◽

Plasma Membranes ◽

Membrane Microdomains ◽

Virus Budding ◽

Vesicular Stomatitis ◽

Membrane Components

ABSTRACT Many plasma membrane components are organized into detergent-resistant membrane microdomains referred to as lipid rafts. However, there is much less information about the organization of membrane components into microdomains outside of lipid rafts. Furthermore, there are few approaches to determine whether different membrane components are colocalized in microdomains as small as lipid rafts. We have previously described a new method of determining the extent of organization of proteins into membrane microdomains by analyzing the distribution of pairwise distances between immunogold particles in immunoelectron micrographs. We used this method to analyze the microdomains involved in the incorporation of the T-cell antigen CD4 into the envelope of vesicular stomatitis virus (VSV). In cells infected with a recombinant virus that expresses CD4 from the viral genome, both CD4 and the VSV envelope glycoprotein (G protein) were found in detergent-soluble (nonraft) membrane fractions. However, analysis of the distribution of CD4 and G protein in plasma membranes by immunoelectron microscopy showed that both were organized into membrane microdomains of similar sizes, approximately 100 to 150 nm. In regions of plasma membrane outside of virus budding sites, CD4 and G protein were present in separate membrane microdomains, as shown by double-label immunoelectron microscopy data. However, virus budding occurred from membrane microdomains that contained both G protein and CD4, and extended to approximately 300 nm, indicating that VSV pseudotype formation with CD4 occurs by clustering of G protein- and CD4-containing microdomains.

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Valosin-Containing Protein (VCP/p97) Is a Potential Antiviral Target against Mononegavirales

Proceedings ◽

10.3390/proceedings2020050108 ◽

2020 ◽

Vol 50 (1) ◽

pp. 108

Author(s):

Victor Latorre ◽

Ron Geller

Keyword(s):

Life Cycle ◽

Respiratory Syncytial Virus ◽

Vesicular Stomatitis Virus ◽

Molecular Chaperones ◽

Cellular Machinery ◽

Vesicular Stomatitis ◽

Medical Importance ◽

Syncytial Virus ◽

Chaperone Network

The viral order Mononegavirales consist of eight virus families. Members of these families include some of the most infectious (Measles, lethal (Ebola and Rabies), and most common viruses (Respiratory syncytial virus, RSV). Despite their medical importance, few vaccines and no antiviral treatments are available for treating infections with these viruses. Being obligate cellular parasites, viruses must rely on the cellular machinery for their replication. One example of this is the widespread use of molecular chaperones, which assist the correct folding of newly synthesized proteins, refold misfolded or aggregated proteins, and play key roles in maintaining proteostasis in cells. Targeting chaperones required for viral replication may, therefore, provide an antiviral approach. In this work, we set out to identify all the members of the cytoplasmic chaperone network that are involved in the replication of RSV using an RNA interference screen. Among our hits is valosin-containing protein (VCP; also known as p97), a chaperone involved in ubiquitin-mediated protein degradation, which has been shown to play a role in the life cycle of several viruses. We investigated the role of VCP during RSV and vesicular stomatitis virus (VSV) infections using specific VCP inhibitors. Our results suggest that VCP activity is necessary for RSV and VSV replication and may constitute a promising antiviral approach for the Mononegavirales.

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Role of non-raft cholesterol in lymphocytic choriomeningitis virus infection via α-dystroglycan

Journal of General Virology ◽

10.1099/vir.0.81444-0 ◽

2006 ◽

Vol 87 (3) ◽

pp. 673-678 ◽

Cited By ~ 28

Author(s):

Waris A. Shah ◽

Huashan Peng ◽

Salvatore Carbonetto

Keyword(s):

Extracellular Matrix ◽

Lipid Rafts ◽

Vesicular Stomatitis Virus ◽

Lymphocytic Choriomeningitis ◽

Lymphocytic Choriomeningitis Virus ◽

Ganglioside Gm1 ◽

The Family ◽

Lymphocytic Choriomeningitis Virus Infection ◽

Vesicular Stomatitis

Dystroglycan (DG) is an extracellular matrix receptor necessary for the development of metazoans from flies to humans and is also an entry route for various pathogens. Lymphocytic choriomeningitis virus (LCMV), a member of the family Arenaviridae, infects by binding to α-DG. Here, the role of cholesterol lipid rafts in infection by LCMV via α-DG was investigated. The cholesterol-sequestering drugs methyl-β-cyclodextrin (MβCD), filipin and nystatin inhibited the infectivity of LCMV selectively, but did not affect infection by vesicular stomatitis virus. Cholesterol loading after depletion with MβCD restored infectivity to control levels. DG was not found in lipid rafts identified with the raft marker ganglioside GM1. Treatment with MβCD, however, enhanced the solubility of DG. This may reflect the association of DG with cholesterol outside lipid rafts and suggests that association of DG with non-raft cholesterol is critical for infection by LCMV through α-DG.

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