Inactivation of Vibrio vulnificus Hemolysin by Oligomerization but Not Proteolysis
| Autor: | Joon Haeng Rhee, Choon Mee Kim, Young Ran Kim, Mi-Hwa Choi, Ra Young Park, Young Hoon Bai, Soo Young Kim, Sung-Heui Shin, Shee Eun Lee, Hui-Yu Sun |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Pharmacology
Functional assay Protease biology medicine.diagnostic_test Reverse Transcriptase Polymerase Chain Reaction Extracellular protease Hydrolysis Proteolysis medicine.medical_treatment Blotting Western Mutant Pharmaceutical Science Hemolysin General Medicine Vibrio vulnificus biology.organism_classification Microbiology Hemolysin Proteins Biopolymers Western blot medicine Electrophoresis Polyacrylamide Gel Peptide Hydrolases |
| Zdroj: | Biological and Pharmaceutical Bulletin. 28:1294-1297 |
| ISSN: | 1347-5215 0918-6158 |
| DOI: | 10.1248/bpb.28.1294 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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