scholarly journals Gene therapy using the human telomerase catalytic subunit gene promoter enables targeting of the therapeutic effects of vesicular stomatitis virus matrix protein against human lung adenocarcinoma

2012 ◽  
Vol 4 (5) ◽  
pp. 859-864 ◽  
Author(s):  
PING ZHANG ◽  
JIAO TAN ◽  
DA-BING YANG ◽  
ZI-CHAO LUO ◽  
SHAN LUO ◽  
...  
Keyword(s):  
Gene Therapy ◽  
Lung Adenocarcinoma ◽  
Vesicular Stomatitis Virus ◽  
Matrix Protein ◽  
Human Lung ◽  
Gene Promoter ◽  
Therapeutic Effects ◽  
Subunit Gene ◽  
Vesicular Stomatitis ◽  
Human Telomerase

scholarly journals Delivery of modified mRNA encoding vesicular stomatitis virus matrix protein for colon cancer gene therapy

RSC Advances ◽  
2018 ◽  
Vol 8 (22) ◽  
pp. 12104-12115 ◽  
Author(s):  
Ke Men ◽  
Rui Zhang ◽  
Xueyan Zhang ◽  
Rong Huang ◽  
Guonian Zhu ◽  
...  
Keyword(s):  
Gene Therapy ◽  
Colon Cancer ◽  
Colon Carcinoma ◽  
Vesicular Stomatitis Virus ◽  
Matrix Protein ◽  
Cancer Gene Therapy ◽  
Viral Gene ◽  
Cancer Gene ◽  
Viral Gene Therapy ◽  
Vesicular Stomatitis

Liposome–protamine complex delivered VSVMP mRNA efficiently inhibits C26 colon carcinoma with safety, providing an alternative strategy for non-viral gene therapy.

A Novel Telomerase-Specific Gene Therapy: Gene Transfer of Caspase-8 Utilizing the Human Telomerase Catalytic Subunit Gene Promoter

2000 ◽  
Vol 11 (10) ◽  
pp. 1397-1406 ◽  
Author(s):  
Shoji Koga ◽  
Satoshi Hirohata ◽  
Yasuko Kondo ◽  
Tadashi Komata ◽  
Masahiro Takakura ◽  
...  
Keyword(s):  
Gene Therapy ◽  
Gene Transfer ◽  
Gene Promoter ◽  
Catalytic Subunit ◽  
Specific Gene ◽  
Caspase 8 ◽  
Subunit Gene ◽  
Human Telomerase

A promising cancer gene therapy agent based on the matrix protein of vesicular stomatitis virus

2008 ◽  
Vol 22 (12) ◽  
pp. 4272-4280 ◽  
Author(s):  
Ju‐mei Zhao ◽  
Yan‐jun Wen ◽  
Qiu Li ◽  
Yong‐sheng Wang ◽  
Hong‐bo Wu ◽  
...  
Keyword(s):  
Gene Therapy ◽  
Vesicular Stomatitis Virus ◽  
Matrix Protein ◽  
Cancer Gene Therapy ◽  
Cancer Gene ◽  
Agent Based ◽  
The Matrix ◽  
Vesicular Stomatitis

Role of matrix protein in cytopathogenesis of vesicular stomatitis virus.

1990 ◽  
Vol 64 (4) ◽  
pp. 1716-1725 ◽  
Author(s):  
D Blondel ◽  
G G Harmison ◽  
M Schubert
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Matrix Protein ◽  
Vesicular Stomatitis

scholarly journals Tracking the Fate of Genetically Distinct Vesicular Stomatitis Virus Matrix Proteins Highlights the Role for Late Domains in Assembly

2015 ◽  
Vol 89 (23) ◽  
pp. 11750-11760 ◽  
Author(s):  
Timothy K. Soh ◽  
Sean P. J. Whelan
Keyword(s):  
Plasma Membrane ◽  
Vesicular Stomatitis Virus ◽  
Matrix Protein ◽  
Fluorescent Proteins ◽  
Endosomal Sorting ◽  
Escrt Machinery ◽  
Viral Particles ◽  
The Matrix ◽  
Vesicular Stomatitis ◽  
Late Domains

ABSTRACTVesicular stomatitis virus (VSV) assembly requires condensation of the viral ribonucleoprotein (RNP) core with the matrix protein (M) during budding from the plasma membrane. The RNP core comprises the negative-sense genomic RNA completely coated by the nucleocapsid protein (N) and associated by a phosphoprotein (P) with the large polymerase protein (L). To study the assembly of single viral particles, we tagged M and P with fluorescent proteins. We selected from a library of viruses with insertions in the M gene a replication-competent virus containing a fluorescent M and combined that with our previously described virus containing fluorescent P. Virus particles containing those fusions maintained the same bullet shape appearance as wild-type VSV but had a modest increase in particle length, reflecting the increased genome size. Imaging of the released particles revealed a variation in the amount of M and P assembled into the virions, consistent with a flexible packaging mechanism. We used the recombinants to further study the importance of the late domains in M, which serve to recruit the endosomal sorting complex required for transport (ESCRT) machinery during budding. Mutations in late domains resulted in the accumulation of virions that failed to pinch off from the plasma membrane. Imaging of single virions released from cells that were coinfected with M tagged with enhanced green fluorescent protein and M tagged with mCherry variants in which the late domains of one virus were inactivated by mutation showed a strong bias against the incorporation of the late-domain mutant into the released virions. In contrast, the intracellular expression and membrane association of the two variants were unaltered. These studies provide new tools for imaging particle assembly and enhance our resolution of existing models for assembly of VSV.IMPORTANCEAssembly of vesicular stomatitis virus (VSV) particles requires the separate trafficking of the viral replication machinery, a matrix protein (M) and a glycoprotein, to the plasma membrane. The matrix protein contains a motif termed a “late domain” that engages the host endosomal sorting complex required for transport (ESCRT) machinery to facilitate the release of viral particles. Inactivation of the late domains through mutation results in the accumulation of virions arrested at the point of release. In the study described here, we developed new tools to study VSV assembly by fusing fluorescent proteins to M and to a constituent of the replication machinery, the phosphoprotein (P). We used those tools to show that the late domains of M are required for efficient incorporation into viral particles and that the particles contain a variable quantity of M and P.

scholarly journals Matrix Protein Mutations Contribute to Inefficient Induction of Apoptosis Leading to Persistent Infection of Human Neural Cells by Vesicular Stomatitis Virus

Virology ◽  
2002 ◽  
Vol 295 (1) ◽  
pp. 63-73 ◽  
Author(s):  
Marc Desforges ◽  
Geneviève Despars ◽  
Stéphane Bérard ◽  
Myriam Gosselin ◽  
Margie O. McKenzie ◽  
...  
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Persistent Infection ◽  
Matrix Protein ◽  
Neural Cells ◽  
Vesicular Stomatitis ◽  
Human Neural Cells ◽  
Induction Of Apoptosis ◽  
Protein Mutations

scholarly journals Phenotypes of vesicular stomatitis virus mutants with mutations in the PSAP motif of the matrix protein

2012 ◽  
Vol 93 (4) ◽  
pp. 857-865 ◽  
Author(s):  
Linda Obiang ◽  
Hélène Raux ◽  
Malika Ouldali ◽  
Danielle Blondel ◽  
Yves Gaudin
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Matrix Protein ◽  
Virus Assembly ◽  
Susceptibility Gene ◽  
Point Mutations ◽  
Binding Motif ◽  
Single Mutation ◽  
Amino Terminal ◽  
Vesicular Stomatitis ◽  
Late Domains

Vesicular stomatitis virus (VSV) matrix protein (M) has a flexible amino-terminal part that recruits cellular partners. It contains a dynamin-binding site that is required for efficient virus assembly, and two motifs, 24PPPY27 and 37PSAP40, that constitute potential late domains. Late domains are present in proteins of several enveloped viruses and are involved in the ultimate step of the budding process (i.e. fission between viral and cellular membranes). In baby hamster kidney (BHK)-21 cells, it has been demonstrated that the 24PPPY27 motif binds the Nedd4 (neuronal precursor cell-expressed developmentally downregulated 4) E3 ubiquitin ligase for efficient virus budding and that the 37PSAP40 motif, although conserved among M proteins of vesiculoviruses, does not possess late-domain activity. In this study, we have re-examined the contribution of the PSAP motif to VSV budding. First, we demonstrate that VSV M indeed binds TSG101 [tumour susceptibility gene 101; a component of the ESCRT1 (endosomal sorting complex required for transport 1)] through its PSAP motif. Second, we analysed the phenotype of several recombinant mutants. We show that a double mutant with point mutations in both the PSAP and the PPPY motifs is impaired compared with a single mutant in the PPPY motif, indicating that the PSAP motif partially compensates for the lack of the PPPY motif. Mutants’ phenotypes depend on cell lines: in CERA (chicken embryo-related, Alger clone) cells, a recombinant virus with a single mutation in the PSAP motif was impaired compared with the wild type, and a mutant with a single mutation in the dynamin-binding motif was much less impaired in Vero cells than in BSR (clones of BHK-21) cells. These results have implications for the VSV budding pathway that will be discussed.

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