86 research outputs found
Biofilm formation at the solid-liquid and air-liquid interfaces by Acinetobacter species
Abstract
Background: The members of the genus Acinetobacter are Gram-negative cocobacilli that are frequently found in
the environment but also in the hospital setting where they have been associated with outbreaks of nosocomial
infections. Among them, Acinetobacter baumannii has emerged as the most common pathogenic species involved
in hospital-acquired infections. One reason for this emergence may be its persistence in the hospital wards, in
particular in the intensive care unit; this persistence could be partially explained by the capacity of these
microorganisms to form biofilm. Therefore, our main objective was to study the prevalence of the two main types
of biofilm formed by the most relevant Acinetobacter species, comparing biofilm formation between the different
species.
Findings: Biofilm formation at the air-liquid and solid-liquid interfaces was investigated in different Acinetobacter
spp. and it appeared to be generally more important at 25°C than at 37°C. The biofilm formation at the solid-liquid
interface by the members of the ACB-complex was at least 3 times higher than the other species (80-91% versus
5-24%). In addition, only the isolates belonging to this complex were able to form biofilm at the air-liquid interface;
between 9% and 36% of the tested isolates formed this type of pellicle. Finally, within the ACB-complex, the
biofilm formed at the air-liquid interface was almost 4 times higher for A. baumannii and Acinetobacter G13TU than
for Acinetobacter G3 (36%, 27% & 9% respectively).
Conclusions: Overall, this study has shown the capacity of the Acinetobacter spp to form two different types of
biofilm: solid-liquid and air-liquid interfaces. This ability was generally higher at 25°C which might contribute to
their persistence in the inanimate hospital environment. Our work has also demonstrated for the first time the
ability of the members of the ACB-complex to form biofilm at the air-liquid interface, a feature that was not
observed in other Acinetobacter species
The role of released ATP in killing Candida albicans and other extracellular microbial pathogens by cationic peptides
A unifying theme common to the action of many cationic peptides that display lethal activities against microbial pathogens is their specific action at microbial membranes that results in selective loss of ions and small nucleotides chiefly ATP. One model cationic peptide that induces non-lytic release of ATP from the fungal pathogen Candida albicans is salivary histatin 5 (Hst 5). The major characteristic of Hst 5-induced ATP release is that it occurs rapidly while cells are still metabolically active and have polarized membranes, thus precluding cell lysis as the means of release of ATP. Other cationic peptides that induce selective release of ATP from target microbes are lactoferricin, human neutrophil defensins, bactenecin, and cathelicidin peptides. The role of released extracellular ATP induced by cationic peptides is not known, but localized increases in extracellular ATP concentration may serve to potentiate cell killing, facilitate further peptide uptake, or function as an additional signal to activate the host innate immune system at the site of infection
Identification of Biofilm-Associated Cluster (bac) in Pseudomonas aeruginosa Involved in Biofilm Formation and Virulence
Biofilms are prevalent in diseases caused by Pseudomonas aeruginosa, an opportunistic and nosocomial pathogen. By a proteomic approach, we previously identified a hypothetical protein of P. aeruginosa (coded by the gene pA3731) that was accumulated by biofilm cells. We report here that a ÎpA3731 mutant is highly biofilm-defective as compared with the wild-type strain. Using a mouse model of lung infection, we show that the mutation also induces a defect in bacterial growth during the acute phase of infection and an attenuation of the virulence. The pA3731 gene is found to control positively the ability to swarm and to produce extracellular rhamnolipids, and belongs to a cluster of 4 genes (pA3729âpA3732) not previously described in P. aeruginosa. Though the protein PA3731 has a predicted secondary structure similar to that of the Phage Shock Protein, some obvious differences are observed compared to already described psp systems, e.g., this unknown cluster is monocistronic and no homology is found between the other proteins constituting this locus and psp proteins. As E. coli PspA, the amount of the protein PA3731 is enlarged by an osmotic shock, however, not affected by a heat shock. We consequently named this locus bac for biofilm-associated cluster
Influence of the oxygenation level on d-xylose fermentation by free and agar-entrapped cultures of Candida shehatae
International audienc
Greater impairment of energy metabolism and coronary flow in type 2 diabetic female rats than in male during myocardial ischemia-reperfusion injury
International audienc
Proteomic comparison of outer membrane protein patterns of sessile and planktonic Pseudomonas aeruginosa cells
International audienc
In vivo and ex vivo longitudinal follow-up of resveratrol supplementation or restauration of a normal diet in female rat hearts submitted to high-fat-high-sucrose diet
International audienc
Membrane proteomes of Pseudomonas aeruginosa and Acinetobacter baumannii
International audienc
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