scholarly journals Recombinant Vesicular Stomatitis Virus Expressing Respiratory Syncytial Virus (RSV) Glycoproteins: RSV Fusion Protein Can Mediate Infection and Cell Fusion

Virology ◽  
1999 ◽  
Vol 254 (1) ◽  
pp. 81-91 ◽  
Author(s):  
Jeffrey S. Kahn ◽  
Matthias J. Schnell ◽  
Linda Buonocore ◽  
John K. Rose
Keyword(s):  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Cell Fusion ◽  
Vesicular Stomatitis Virus ◽  
Vesicular Stomatitis ◽  
Syncytial Virus

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

Proceedings ◽  
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.

scholarly journals Insertion of the Two Cleavage Sites of the Respiratory Syncytial Virus Fusion Protein in Sendai Virus Fusion Protein Leads to Enhanced Cell-Cell Fusion and a Decreased Dependency on the HN Attachment Protein for Activity

2008 ◽  
Vol 82 (12) ◽  
pp. 5986-5998 ◽  
Author(s):  
Joanna Rawling ◽  
Blanca García-Barreno ◽  
José A. Melero
Keyword(s):  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Membrane Fusion ◽  
Cell Fusion ◽  
Sendai Virus ◽  
Cleavage Sites ◽  
Attachment Protein ◽  
F Protein ◽  
Syncytial Virus ◽  
Cell Cell

ABSTRACT Cell entry by paramyxoviruses requires fusion of the viral envelope with the target cell membrane. Fusion is mediated by the viral fusion (F) glycoprotein and usually requires the aid of the attachment glycoprotein (G, H or HN, depending on the virus). Human respiratory syncytial virus F protein (FRSV) is able to mediate membrane fusion in the absence of the attachment G protein and is unique in possessing two multibasic furin cleavage sites, separated by a region of 27 amino acids (pep27). Cleavage at both sites is required for cell-cell fusion. We have investigated the significance of the two cleavage sites and pep27 in the context of Sendai virus F protein (FSeV), which possesses a single monobasic cleavage site and requires both coexpression of the HN attachment protein and trypsin in order to fuse cells. Inclusion of both FRSV cleavage sites in FSeV resulted in a dramatic increase in cell-cell fusion activity in the presence of HN. Furthermore, chimeric FSeV mutants containing both FRSV cleavage sites demonstrated cell-cell fusion in the absence of HN. The presence of two multibasic cleavage sites may therefore represent a strategy to regulate activation of a paramyxovirus F protein for cell-cell fusion in the absence of an attachment protein.

scholarly journals Agmatine-Containing Poly(amidoamine)s as a Novel Class of Antiviral Macromolecules: Structural Properties andIn VitroEvaluation of Infectivity Inhibition

2014 ◽  
Vol 58 (10) ◽  
pp. 6315-6319 ◽  
Author(s):  
Manuela Donalisio ◽  
Elisabetta Ranucci ◽  
Valeria Cagno ◽  
Andrea Civra ◽  
Amedea Manfredi ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Herpes Simplex ◽  
Antiviral Activity ◽  
Vesicular Stomatitis Virus ◽  
Human Papillomavirus 16 ◽  
Human Rotavirus ◽  
Vesicular Stomatitis ◽  
Syncytial Virus ◽  
Simplex Virus ◽  
Structural Versatility

ABSTRACTPoly(amidoamine)s (PAAs) are multifunctionaltert-amine polymers endowed with high structural versatility. Here we report on the screening of a minilibrary of PAAs against a panel of viruses. The PAA AGMA1 showed antiviral activity against herpes simplex virus, human cytomegalovirus, human papillomavirus 16, and respiratory syncytial virus but not against human rotavirus and vesicular stomatitis virus. The results suggest the contribution of both a polycationic nature and side guanidine groups in imparting antiviral activity.

Vaccination with prefusion-stabilized respiratory syncytial virus fusion protein induces genetically and antigenically diverse antibody responses

Immunity ◽  
2021 ◽  
Author(s):  
Maryam Mukhamedova ◽  
Daniel Wrapp ◽  
Chen-Hsiang Shen ◽  
Morgan S.A. Gilman ◽  
Tracy J. Ruckwardt ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Fusion Protein ◽  
Antibody Responses ◽  
Virus Fusion ◽  
Syncytial Virus
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