pyridostatin and Common-Cold

pyridostatin has been researched along with Common-Cold* in 1 studies

Other Studies

1 other study(ies) available for pyridostatin and Common-Cold

Article	Year
Catching Common Cold Virus with a Net: Pyridostatin Forms Filaments in Tris Buffer That Trap Viruses-A Novel Antiviral Strategy? Viruses, 2020, 07-04, Volume: 12, Issue:7 The neutrophil extracellular trap (ET) is a eukaryotic host defense machinery that operates by capturing and concentrating pathogens in a filamentous network manufactured by neutrophils and made of DNA, histones, and many other components. Respiratory virus-induced ETs are involved in tissue damage and impairment of the alveolar-capillary barrier, but they also aid in fending off infection. We found that the small organic compound pyridostatin (PDS) forms somewhat similar fibrillary structures in Tris buffer in a concentration-dependent manner. Common cold viruses promote this process and become entrapped in the network, decreasing their infectivity by about 70% in tissue culture. We propose studying this novel mechanism of virus inhibition for its utility in preventing viral infection. Topics: Aminoquinolines; Antiviral Agents; Cells, Cultured; Common Cold; Extracellular Traps; HeLa Cells; Humans; Microscopy, Electron, Transmission; Neutrophils; Picolinic Acids; Rhinovirus; Tromethamine	2020

Article

Year

Catching Common Cold Virus with a Net: Pyridostatin Forms Filaments in Tris Buffer That Trap Viruses-A Novel Antiviral Strategy?

Viruses, 2020, 07-04, Volume: 12, Issue:7

The neutrophil extracellular trap (ET) is a eukaryotic host defense machinery that operates by capturing and concentrating pathogens in a filamentous network manufactured by neutrophils and made of DNA, histones, and many other components. Respiratory virus-induced ETs are involved in tissue damage and impairment of the alveolar-capillary barrier, but they also aid in fending off infection. We found that the small organic compound pyridostatin (PDS) forms somewhat similar fibrillary structures in Tris buffer in a concentration-dependent manner. Common cold viruses promote this process and become entrapped in the network, decreasing their infectivity by about 70% in tissue culture. We propose studying this novel mechanism of virus inhibition for its utility in preventing viral infection.

Topics: Aminoquinolines; Antiviral Agents; Cells, Cultured; Common Cold; Extracellular Traps; HeLa Cells; Humans; Microscopy, Electron, Transmission; Neutrophils; Picolinic Acids; Rhinovirus; Tromethamine

2020