Articles producció científica> Ciències Mèdiques Bàsiques

The Metallochaperone Encoding Gene hypA Is Widely Distributed among Pathogenic Aeromonas spp

  • Identification data

    Identifier: imarina:5873545
    Handle: http://hdl.handle.net/20.500.11797/imarina5873545
  • Authors:

    Fernández-Bravo A, López-Fernández L, Figueras MJ
  • Others:

    Author, as appears in the article.: Fernández-Bravo A, López-Fernández L, Figueras MJ
    Department: Ciències Mèdiques Bàsiques
    URV's Author/s: Fernández Bravo, Ana / Figueras Salvat, María Josefa
    Keywords: Ureases Urease maturation System Site Ros Resistance Nife hydrogenase Metals Metallochaperone Mechanism Macrophages Hydrogenases Hsp33 Escherichia-coli Chaperone Alkaline Aeromonas Acid
    Abstract: Metallochaperones are essential proteins that insert metal ions or metal cofactors into specific enzymes, that after maturation will become metalloenzymes. One of the most studied metallochaperones is the nickel-binding protein HypA, involved in the maturation of nickel-dependent hydrogenases and ureases. HypA was previously described in the human pathogens Escherichia coli and Helicobacter pylori and was considered a key virulence factor in the latter. However, nothing is known about this metallochaperone in the species of the emerging pathogen genus Aeromonas. These bacteria are native inhabitants of aquatic environments, often associated with cases of diarrhea and wound infections. In this study, we performed an in silico study of the hypA gene on 36 Aeromonas species genomes, which showed the presence of the gene in 69.4% (25/36) of the Aeromonas genomes. The similarity of Aeromonas HypA proteins with the H. pylori orthologous protein ranged from 21-23%, while with that of E. coli it was 41-45%. However, despite this low percentage, Aeromonas HypA displays the conserved characteristic metal-binding domains found in the other pathogens. The transcriptional analysis enabled the determination of hypA expression levels under acidic and alkaline conditions and after macrophage phagocytosis. The transcriptional regulation of hypA was found to be pH-dependent, showing upregulation at acidic pH. A higher upregulation occurred after macrophage infection. This is the first study that provided evidence that the HypA metallochaperone in Aeromonas might play a role in acid tolerance and in the defense against macrophages.
    Thematic Areas: Virology Microbiology (medical) Microbiology
    licence for use: https://creativecommons.org/licenses/by/3.0/es/
    ISSN: 20762607
    Author's mail: ana.fernandez@urv.cat mariajose.figueras@urv.cat
    Author identifier: 0000-0001-7637-5958 0000-0002-2268-8980
    Record's date: 2023-03-05
    Papper version: info:eu-repo/semantics/publishedVersion
    Link to the original source: https://www.mdpi.com/2076-2607/7/10/415
    Licence document URL: http://repositori.urv.cat/ca/proteccio-de-dades/
    Papper original source: Microorganisms. 7 (10):
    APA: Fernández-Bravo A, López-Fernández L, Figueras MJ (2019). The Metallochaperone Encoding Gene hypA Is Widely Distributed among Pathogenic Aeromonas spp. Microorganisms, 7(10), -. DOI: 10.3390/microorganisms7100415
    Article's DOI: 10.3390/microorganisms7100415
    Entity: Universitat Rovira i Virgili
    Journal publication year: 2019
    Publication Type: Journal Publications
  • Keywords:

    Microbiology,Microbiology (Medical),Virology
    Ureases
    Urease maturation
    System
    Site
    Ros
    Resistance
    Nife hydrogenase
    Metals
    Metallochaperone
    Mechanism
    Macrophages
    Hydrogenases
    Hsp33
    Escherichia-coli
    Chaperone
    Alkaline
    Aeromonas
    Acid
    Virology
    Microbiology (medical)
    Microbiology
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