A putative siderophore receptor of Gallibacterium anatis 12656-12 under Fur control also binds hemoglobin
| Autor: | Alberto Chantes-Guerra, Samantha Maldonado-Puga, Norma Rojas-Ruiz, Ismael Rea-Hernandez, Fernando J. Montes-Garcia, Hector Trujillo-Ruiz, Ivan E. Yañez-Aguilar, Candelario Vazquez-Cruz, Patricia Sanchez-Alonso, Erasmo Negrete-Abascal |
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| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Frontiers in Microbiology, Vol 13 (2022) |
| Druh dokumentu: | article |
| ISSN: | 1664-302X 78996406 |
| DOI: | 10.3389/fmicb.2022.951173 |
| Popis: | Pasteurellaceae family members obtain iron directly from host proteins or through siderophore-dependent mechanisms. Although Gallibacterum anatis expresses different virulence factors, its response to growth under iron restriction is unknown. G. anatis cultured in the presence of 2,2′-dipyridyl, up-expressed an approximately 65 kDa protein and repressed the expression of a 70 kDa protein. MALDI-TOF analysis of those proteins indicated homology with CirA (65 kDa), a protein involved in iron-siderophore acquisition in Mannheimia succinoproducens and a TonB-dependent receptor (70 kDa protein), a protein that binds chicken hemoglobin; however, G. anatis siderophore production was not detected by chromo azurol S (CAS)-BHI agar determination. This putative G. anatis siderophore receptor is under Fur control, but not the hemoglobin binding protein, as observed in G. anatis 12656-12 fur mutant (Ω fur 126.13) grown in the presence or not of 2,2′-dipyridyl. The addition of FeCl3 to the culture medium diminished the growth and biofilm production in approximately 30% and 35%, respectively, in the wild-type strain, but the growth of Ω fur 126.13 strain was not affected and biofilm production increased in 35%. G. anatis Ω fur 126.13 presented lower virulence when it was inoculated to 35-day-old chickens in comparison to the wild-type strain. The induction of more than one iron uptake mechanism could benefit pathogenic microorganisms such as Gallibacterium. |
| Databáze: | Directory of Open Access Journals |
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