Iron-Utilization System in Vibrio vulnificus M2799
| Autor: | Katsushiro Miyamoto, Hiroaki Kawano, Naoko Okai, Takeshi Hiromoto, Nao Miyano, Koji Tomoo, Takahiro Tsuchiya, Jun Komano, Tomotaka Tanabe, Tatsuya Funahashi, Hiroshi Tsujibo |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: | |
| Zdroj: | Marine Drugs, Vol 19, Iss 12, p 710 (2021) |
| Druh dokumentu: | article |
| ISSN: | 19120710 1660-3397 |
| DOI: | 10.3390/md19120710 |
| Popis: | Vibrio vulnificus is a Gram-negative pathogenic bacterium that causes serious infections in humans and requires iron for growth. A clinical isolate, V. vulnificus M2799, secretes a catecholate siderophore, vulnibactin, that captures ferric ions from the environment. In the ferric-utilization system in V. vulnificus M2799, an isochorismate synthase (ICS) and an outer membrane receptor, VuuA, are required under low-iron conditions, but alternative proteins FatB and VuuB can function as a periplasmic-binding protein and a ferric-chelate reductase, respectively. The vulnibactin-export system is assembled from TolCV1 and several RND proteins, including VV1_1681. In heme acquisition, HupA and HvtA serve as specific outer membrane receptors and HupB is a sole periplasmic-binding protein, unlike FatB in the ferric-vulnibactin utilization system. We propose that ferric-siderophore periplasmic-binding proteins and ferric-chelate reductases are potential targets for drug discovery in infectious diseases. |
| Databáze: | Directory of Open Access Journals |
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