Antiviral Activity of Proteasome Inhibitors/Cytomegalovirus

Kaspari, Marion; Bogner, Elke

doi:10.1007/978-90-481-2348-3_4

Cited by 2 publications

(2 citation statements)

References 39 publications

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“…Several synthetic and a few natural proteasome inhibitors (e.g. lactacystin from Streptomyces lactacystinaeus) are known and have been reported to obstruct replication of several viruses, including influenza virus, herpes simplex virus type 1, paramyxovirus and rhabdoviruses, as well as cytomegalovirus (Kaspari and Bogner 2009). The serine proteases NS3 and NS2 of flaviviruses are targets for antiviral drug development against hepatitis C virus and dengue virus, with the former blood-transmitted virus causing various liver diseases (including cirrhosis and liver cancer) and the latter being a mosquitotransmitted disease causing dengue hemorrhagic fever.…”

Section: Viral Diseasesmentioning

confidence: 99%

Microbial and fungal protease inhibitors—current and potential applications

Sabotič

Kos

2012

Appl Microbiol Biotechnol

147

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Proteolytic enzymes play essential metabolic and regulatory functions in many biological processes and also offer a wide range of biotechnological applications. Because of their essential roles, their proteolytic activity needs to be tightly regulated. Therefore, small molecules and proteins that inhibit proteases can be versatile tools in the fields of medicine, agriculture and biotechnology. In medicine, protease inhibitors can be used as diagnostic or therapeutic agents for viral, bacterial, fungal and parasitic diseases as well as for treating cancer and immunological, neurodegenerative and cardiovascular diseases. They can be involved in crop protection against plant pathogens and herbivorous pests as well as against abiotic stress such as drought. Furthermore, protease inhibitors are indispensable in protein purification procedures to prevent undesired proteolysis during heterologous expression or protein extraction. They are also valuable tools for simple and effective purification of proteases, using affinity chromatography. Because there are such a large number and diversity of proteases in prokaryotes, yeasts, filamentous fungi and mushrooms, we can expect them to be a rich source of protease inhibitors as well.

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Section: Viral Diseasesmentioning

confidence: 99%

Microbial and fungal protease inhibitors—current and potential applications

Sabotič

Kos

2012

Appl Microbiol Biotechnol

147

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“…Once thought to be simple degradation engines, proteases are increasingly seen as pathway control agents for key processes ranging from blood clotting [4] to cell death [5]. Indeed, proteases have been shown or are postulated to be associated with a wide variety of disease conditions, including heart disease, cancer, Alzheimer's disease, arthritis, HIV/AIDS, Hepatitis C, inflammation, and diabetes mellitus [6][7][8][9][10][11][12][13][14][15][16][17]. Protease inhibitors are already being used to combat a variety of diseases, e.g., PAXLOVID for COVID-19 [18] and multiple treatments for HIV [19].…”

Section: Introductionmentioning

confidence: 99%

Realtime, continuous assessment of complex-mixture protease and protease inhibitor activity

Leonard,

Kenis,

Perkins

2022

4open

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Recently the treatment PAXLOVID™ (nirmatrelvir co-packaged with ritonavir) was authorized for use as a treatment for COVID-19. The presumed mechanism of action of the treatment, an inhibitor of a Sars-Cov-2 “3CL” protease, continues decades-long interest in viral protease inhibition in the fight against pathogenic viruses (e.g., HIV protease inhibitors). Proteolysis assay methods vary widely, roughly bounded by interrogation of basic biochemistry and high-throughput, early-stage drug screening. Reported here are methods that provide unique and biologically relevant characterization of proteolysis and protease inhibition. A companion report provides evidence that these methods show promise for drug and basic biological discovery, especially for early detection of potential side effects. Electron spin resonance spectroscopy and spin labeling (ESRSL) of whole proteins are leveraged to monitor reactants and products of whole-protein digestion through differentiation of angular mobility of those products and reactants. These proof-of-concept data demonstrate consistency with prior art for all possible combinations of four proteases, two whole-protein substrates and three inhibitors. Thus, ESRSL is shown to uniquely and widely interrogate proteolysis of natural, whole-protein, substrates insuring the biological relevance of results.

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Antiviral Activity of Proteasome Inhibitors/Cytomegalovirus

Cited by 2 publications

References 39 publications

Microbial and fungal protease inhibitors—current and potential applications

Microbial and fungal protease inhibitors—current and potential applications

Realtime, continuous assessment of complex-mixture protease and protease inhibitor activity

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