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Characterizing Cellular Responses During Oncolytic Maraba Virus Infection.
Int J Mol Sci
January 2019
Molecular Biomedicine Program, Children's Hospital of Eastern Ontario Research Institute, Ottawa, ON K1H 8L1, Canada.
The rising demand for powerful oncolytic virotherapy agents has led to the identification of Maraba virus, one of the most potent oncolytic viruses from Rhabdoviridae family which displays high selectivity for killing malignant cells and low cytotoxicity in normal cells. Although the virus is readied to be used for clinical trials, the interactions between the virus and the host cells is still unclear. Using a newly developed interferon-sensitive mutant Maraba virus (MG1), we have identified two key regulators of global translation (4E-BP1 and eIF2α) as being involved in the regulation of protein synthesis in the infected cells.
View Article and Find Full Text PDFReovirus FAST Protein Enhances Vesicular Stomatitis Virus Oncolytic Virotherapy in Primary and Metastatic Tumor Models.
Mol Ther Oncolytics
September 2017
Department of Microbiology and Immunology, Dalhousie University, Halifax, NS B3H4R2, Canada.
The reovirus fusion-associated small transmembrane (FAST) proteins are the smallest known viral fusogens (∼100-150 amino acids) and efficiently induce cell-cell fusion and syncytium formation in multiple cell types. Syncytium formation enhances cell-cell virus transmission and may also induce immunogenic cell death, a form of apoptosis that stimulates immune recognition of tumor cells. These properties suggest that FAST proteins might serve to enhance oncolytic virotherapy.
View Article and Find Full Text PDFNormal human cell proteins that interact with the adenovirus type 5 E1B 55kDa protein.
Virology
April 2017
Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA. Electronic address:
Several of the functions of the human adenovirus type 5 E1B 55kDa protein are fulfilled via the virus-specific E3 ubiquitin ligase it forms with the viral E4 Orf6 protein and several cellular proteins. Important substrates of this enzyme have not been identified, and other functions, including repression of transcription of interferon-sensitive genes, do not require the ligase. We therefore used immunoaffinity purification and liquid chromatography-mass spectrometry of lysates of normal human cells infected in parallel with HAdV-C5 and E1B 55kDa protein-null mutant viruses to identify specifically E1B 55kDa-associated proteins.
View Article and Find Full Text PDFHuman pegivirus (GB virus C) NS3 protease activity inhibits induction of the type I interferon response and is not inhibited by HCV NS3 protease inhibitors.
Virology
May 2014
Saint Louis University School of Medicine, Department of Molecular Microbiology and Immunology, St. Louis, MO, USA; Saint Louis University School of Medicine, Department of Internal Medicine, Division of Infectious Diseases, Allergy & Immunology, St. Louis, MO, USA; Saint Louis Veterans Administration Medical Center, St. Louis, MO, USA. Electronic address:
Article Synopsis
- HPgV NS3 protease has been found to inhibit HIV replication in CD4+ T cells while also being similar to the HCV NS3 protease.
- Researchers investigated whether HPgV protease affects type I interferon responses or is impacted by HCV protease inhibitors and found that major HCV inhibitors do not affect HPgV activity.
- The study revealed that HPgV NS3 protease can cleave MAVS and inhibit interferon responses, potentially promoting HPgV persistence, which may provide clinical benefits for HIV-infected patients.
The human adenovirus type 5 E1B 55 kDa protein obstructs inhibition of viral replication by type I interferon in normal human cells.
PLoS Pathog
December 2012
Princeton University, Department of Molecular Biology, Lewis Thomas Laboratory, Princeton, New Jersey, United States of America.
Vectors derived from human adenovirus type 5, which typically lack the E1A and E1B genes, induce robust innate immune responses that limit their therapeutic efficacy. We reported previously that the E1B 55 kDa protein inhibits expression of a set of cellular genes that is highly enriched for those associated with anti-viral defense and immune responses, and includes many interferon-sensitive genes. The sensitivity of replication of E1B 55 kDa null-mutants to exogenous interferon (IFN) was therefore examined in normal human fibroblasts and respiratory epithelial cells.
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