Thermodynamic instability of viral proteins is a pathogen-associated molecular pattern targeted by human defensins.

ABSTRACT: Human defensins are innate immune defense peptides with a remarkably broad repertoire of anti-pathogen activities. In addition to modulating immune response, inflammation, and angiogenesis, disintegrating bacterial membranes, and inactivating bacterial toxins, defensins are known to intercept various viruses at different stages of their life cycles, while remaining relatively benign towards human cells and proteins. Recently we have found that human defensins inactivate proteinaceous bacterial toxins by taking advantage of their low thermodynamic stability and acting as natural "anti-chaperones", i.e. destabilizing the native conformation of the toxins. In the present study we tested various proteins produced by several viruses (HIV-1, PFV, and TEV) and found them to be susceptible to dest

SUBMITTER: Kudryashova E 

PROVIDER: S-EPMC5007486 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature