Related Experiment Video
Updated: Aug 17, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
Published on: January 2, 2026
Inactivation of Vibrio vulnificus hemolysin by oligomerization but not proteolysis
Sung-Heui Shin1, Hui-Yu Sun, Mi-Hwa Choi
1Research Center for Resistant Cells, Chosun University Medical School, Gwangju, South Korea. shsin@chosun.ac.kr
Abstract:
Vibrio vulnificus extracellular protease (VvpE) is believed to destroy its hemolysin (VvhA) in the late growth phase, without obvious experimental evidence. So, we attempted to elucidate the mechanism. The hemolytic activity steeply increased with the expression of the VvhA in the early growth phase, and then abruptly declined with the expression of VvpE in the late growth phase. However, the VvhA activity also abruptly declined in a VvpE-deficient mutant. In Western blot, the degradation of VvhA was not observed; instead, the oligomerization of VvhA increased with the concomitant loss of hemolytic activity. These results evidently indicate that the inactivation of VvhA is due to the novel oligomerization of VvhA by unknown mechanism, but not to the destruction of VvhA by VvpE, so that the routine functional assay measuring hemolytic activity cannot reflect the actual production of VvhA.
Related Concept Videos
Regulation of Bacterial Virulence
Protein Denaturation
Radical Formation: Homolysis
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
Viral Replication: Lysogenic Cycle
Inhibitors of Virion Maturation and Assembly

