Examinando por Autor "Pimentel, Camila"

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    Acinetobacter baumannii response to cefiderocol challenge in human urine
    (Springer Nature, 2022-05-24) Nishimura, Brent; Escalante, Jenny; Tuttobene, Marisel Romina; Subils, Tomás; Mezcord, Vyanka; Pimentel, Camila; Georgeos, Nardin; Pasteran, Fernando; Rodríguez, Cecilia; Sieira, Rodrigo; Actis, Luis A.; Tolmasky, Marcelo E.; Bonomo, Robert A.; Ramírez, María Soledad
    Cefiderocol (CFDC) is a novel chlorocatechol-substituted siderophore antibiotic approved to treat complicated urinary tract infections (cUTI) and hospital-acquired and ventilator-acquired pneumonia (HAP/VAP). Previous work determined that albumin-rich human fluids increase the minimum inhibitory concentration (MICs) of Acinetobacter baumannii against CFDC and reduce the expression of genes related to iron uptake systems. This latter effect may contribute to the need for higher concentrations of CFDC to inhibit growth. The presence of human urine (HU), which contains low albumin concentrations, did not modify MIC values of two carbapenem-resistant A. baumannii. Levels of resistance to CFDC were not modified by HU in strain AMA40 but were reduced in strain AB5075. Expanding the studies to other carbapenem-resistant A. baumannii isolates showed that the presence of HU resulted in unmodified or reduced MIC of CDFC values. The expression of piuA, pirA, bauA, and bfnH determined by qRT-PCR was enhanced in A. baumannii AMA40 and AB5075 by the presence of HU in the culture medium. All four tested genes code for functions related to recognition and transport of ferric-siderophore complexes. The effect of HU on expression of pbp1, pbp3, blaOXA-51-like, blaADC, and blaNDM-1, genes associated with resistance to β-lactams, as well as genes coding for efflux pumps and porins was variable, showing dependence with the strain analyzed. We conclude that the lack of significant concentrations of albumin and free iron in HU makes this fluid behave differently from others we tested. Unlike other albumin rich fluids, the presence of HU does not impact the antibacterial activity of CFDC when tested against A. baumannii.
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    Cerebrospinal fuid (CSF) augments metabolism and virulence expression factors in Acinetobacter baumannii
    (Nature Research, 2021-02-26) Martínez, Jasmine; Razo Gutiérrez, Chelsea; Razo Gutiérrez, Chelsea; Courville, Robert; Pimentel, Camila; Liu, Christine; Fung, Sammie E.; Tuttobene, Marisel Romina; Phan, Kimberly; Vila, Alejandro J.; Shahrestani, Parvin; Jimenez, Veronica; Tolmasky, Marcelo E.; Becka, Scott A.; Papp Wallace, Krisztina M.; Bonomo, Robert A.; Soler Bistue, Alfonso; Sieira, Rodrigo; Ramírez, María Soledad
    In a recent report by the Centers for Disease Control and Prevention (CDC), multidrug resistant (MDR) Acinetobacter baumannii is a pathogen described as an “urgent threat.” Infection with this bacterium manifests as diferent diseases such as community and nosocomial pneumonia, bloodstream infections, endocarditis, infections of the urinary tract, wound infections, burn infections, skin and soft tissue infections, and meningitis. In particular, nosocomial meningitis, an unwelcome complication of neurosurgery caused by extensivelydrug resistant (XDR) A. baumannii, is extremely challenging to manage. Therefore, understanding how A. baumannii adapts to diferent host environments, such as cerebrospinal fuid (CSF) that may trigger changes in expression of virulence factors that are associated with the successful establishment and progress of this infection is necessary. The present invitro work describes, the genetic changes that occur during A. baumannii infltration into CSF and displays A. baumannii’s expansive versatility to persist in a nutrient limited environment while enhancing several virulence factors to survive and persist. While a hypervirulent A. baumannii strain did not show changes in its transcriptome when incubated in the presence of CSF, a lowvirulence isolate showed signifcant diferences in gene expression and phenotypic traits. Exposure to 4% CSF caused increased expression of virulence factors such as fmbriae, pilins, and iron chelators, and other virulence determinants that was confrmed in various model systems. Furthermore, although CSF’s presence did not enhance bacterial growth, an increase of expression of genes encoding transcription, translation, and the ATP synthesis machinery was observed. This work also explores A. baumannii’s response to an essential component, human serum albumin (HSA), within CSF to trigger the diferential expression of genes associated with its pathoadaptibility in this environment.
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    Histone-like nucleoid-structuring protein (H-NS) regulatory role in antibiotic resistance in Acinetobacter baumannii
    (Nature Research, 2021) Rodgers, Deja; Le, Casin; Pimentel, Camila; Tuttobene, Marisel Romina; Subils, Tomás; Escalante, Jenny; Nishimura, Brent; García Véscovi, Eleonora; Sieira, Rodrigo; Bonomo, Robert A.; Tolmasky, Marcelo E.; Ramírez, María Soledad
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    Human serum albumin (HSA) regulates the expression of histone-like nucleoid structure protein (H-NS) in Acinetobacter baumannii
    (Nature Research, 2022-08-27) Escalante, Jenny; Nishimura, Brent; Tuttobene, Marisel Romina; Subils, Tomás; Pimentel, Camila; Georgeos, Nardin; Sieira, Rodrigo; Bonomo, Robert A.; Tolmasky, Marcelo E.; Ramírez, María Soledad
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    Human Serum Proteins and Susceptibility of Acinetobacter baumannii to Cefiderocol: Role of Iron Transport
    (MDPI, 2022-03-03) Le, Casin; Pimentel, Camila; Pasteran, Fernando; Tuttobene, Marisel Romina; Subils, Tomás; Escalante, Jenny; Nishimura, Brent; Arriaga, Susana; Carranza, Aimee; Mezcord, Vyanka; Vila, Alejandro J.; Corso, Alejandra; Actis, Luis A.; Tolmasky, Marcelo E.; Bonomo, Robert A.; Ramírez, María Soledad
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    Interaction of Acinetobacter baumannii with Human Serum Albumin: Does the host hetermine the outcome?
    (MDPI, 2021-07-08) Pimentel, Camila; Le, Casin; Tuttobene, Marisel Romina; Subils, Tomás; Bonomo, Robert A.; Tolmasky, Marcelo E.; Ramírez, María Soledad
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    Involvement of the histone-like nucleoid structuring protein (H-NS) in Acinetobacter baumannii’s natural transformation
    (MDPI, 2021-08-26) Le, Casin; Pimentel, Camila; Tuttobene, Marisel Romina; Subils, Tomás; Escalante, Jenny; Nishimura, Brent; Arriaga, Susana; Rodgers, Deja; Bonomo, Robert A.; Sieira, Rodrigo; Tolmasky, Marcelo E.; Ramírez, María Soledad; https://orcid.org/0000-0003-0234-4643; https://orcid.org/0000-0002-4495-563X; https://orcid.org/0000-0002-6298-7811; https://orcid.org/0000-0002-9904-7890
    Most Acinetobacter baumannii strains are naturally competent. Although some information is available about factors that enhance or reduce the frequency of the transformation of this bacterium, the regulatory elements and mechanisms are barely understood. In this article, we describe studies on the role of the histone-like nucleoid structuring protein, H-NS, in the regulation of the expression of genes related to natural competency and the ability to uptake foreign DNA. The expression levels of the natural transformation-related genes pilA, pilT, pilQ, comEA, comEC, comF, and drpA significantly increased in a ∆hns derivative of A. baumannii A118. The complementation of the mutant with a recombinant plasmid harboring hns restored the expression levels of six of these genes (pilT remained expressed at high levels) to those of the wild-type strain. The transformation frequency of the A. baumannii A118 ∆hns strain was significantly higher than that of the wild-type. Similar, albeit not identical, there were consequences when hns was deleted from the hypervirulent A. baumannii AB5075 strain. In the AB5075 complemented strain, the reduction in gene expression in a few cases was not so pronounced that it reached wild-type levels, and the expression of comEA was enhanced further. In conclusion, the expression of all seven transformation-related genes was enhanced after deleting hns in A. baumannii A118 and AB5075, and these modifications were accompanied by an increase in the cells’ transformability. The results highlight a role of H-NS in A. baumannii’s natural competence.