PubMed Health⌕ Search

PubMed · 15786636

Acinetobacter as a causative agent in preseptal cellulitis.

Abstract

BACKGROUND: The bacterial genus Acinetobacter, once viewed as inconsequential, has been increasingly implicated as a significant pathogen. Acinetobacter is becoming progressively more resistant to older and newer-generation antibiotics. The primary species encountered in infections is Acinetobacter baumannii. CASE REPORT: A 39-year-old woman came in for treatment of a preseptal cellulitis and conjunctivitis. She was referred to W.W. Hastings Optometry Clinic eleven days after first being diagnosed with a hordeolum that developed into a preseptal cellulitis, despite the use of oral cephalexin anazithromycin. After being referred, the patient was placed on oral regimen of gatifloxacin and topical ciprofloxacin. The patient gradually improved over the next 10 days, with full resolution occurring 21 days after the first presentation. Culturing revealed the offending organism to be Acinetobacter. DISCUSSION: Most ocular infections are still caused by common organisms such as Staphylococcus. However, atypical bacteria such as Acinetobacter are responsible for a minority of infections. Careful consideration of patient history and clinical signs must be made to differentiate preseptal cellulitis and orbital cellulitis. CONCLUSION: This case emphasizes that clinicians need to be aware of emerging and resistant bacteria in ocular infections. Infections that do not respond to traditional therapy should be treated aggressively with the latest-generation antibiotics. Ocular infections that do not resolve in a timely manner should be cultured for the offending organism and these organisms should be tested for susceptibility to anti-microbial drugs.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Jeff Miller. 2005. Acinetobacter as a causative agent in preseptal cellulitis.. https://doi.org/10.1016/s1529-1839(05)70282-7

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Characterization of carbon metabolism in a highly adhesive bacterium Acinetobacter sp. Tol 5 capable of assimilating diverse hydrocarbons and aromatic compounds.

Sustainable bioproduction requires developing robust microbial chassis with broad metabolic versatility and suitability for industrial applications. Acinetobacter sp. Tol 5 is a highly adhesive bacterium capable of utilizing various hydrocarbons, making it a promising chassis candidate for immobilized whole-cell catalysis. In this study, we characterized the carbon metabolism of Tol 5 by reconstructing metabolic pathway maps from its genomic data and analyzing the transcriptomes of cells grown on ethanol, hexadecane, toluene, and phenol. Genomic analysis revealed that Tol 5 has limited capacity for sugar utilization but possesses a wide range of metabolic pathways for alkane and aromatic compounds, including five distinct aromatic degradation routes that expand the known metabolic diversity of the genus Acinetobacter. Transcriptome analysis identified the specific pathway genes induced in response to each carbon source. During growth on phenol, alkylbenzene degradation genes were upregulated alongside phenol monooxygenase genes, suggesting possible substrate-dependent cross-regulation between aromatic degradation pathways. Gene disruption experiments indicated that phenol monooxygenase is required for phenol assimilation, whereas toluene dioxygenase may contribute to earlier entry into exponential growth while potentially limiting final biomass accumulation. These findings provide a comprehensive view of the carbon metabolism of Tol 5 and a basis for assessing its potential in bioprocesses using non-sugar carbon sources.

Acinetobacter↗

Acinetobacter guillouiae, a lipolytic strain isolated from sludge capable of partially depolymerising polyethylene terephthalate: genomic, proteomic, and biochemical insights.

Acinetobacter guillouiae I-MWF was isolated by incubating amorphous polyethylene terephthalate (PET) film in sludge samples. The strain partially depolymerised PET powder with 11.3% crystallinity, as confirmed by FT-IR, HPLC-UV, and LC-MS analyses. Extracellular enzymes released terephthalic acid (TPA), mono(2-hydroxyethyl) terephthalate (MHET), and bis(2-hydroxyethyl) terephthalate (BHET). Genomic analysis identified 18 putative extracellular hydrolases, including lipases and esterases, each with a conserved catalytic triad. Proteomic profiling revealed expression of two triacylglycerol lipases and two additional lipase-family proteins when the strain was cultivated with PET or a PET-Tween 80 mixture. These enzymes were cloned in Escherichia coli, but most formed insoluble, inactive inclusion bodies, and one was not expressed. Molecular modelling highlighted structural features likely to influence their catalytic interaction with PET. Although the strain partially depolymerised PET powder, it was unable to grow on PET, TPA, or ethylene glycol, indicating that PET depolymerisation occurs as a side activity rather than supporting growth. Instead, A. guillouiae displayed strong lipolytic activity and a clear preference for lipid-based substrates, achieving its highest growth with Tween 80. A lipid transporter was also expressed under these conditions, suggesting adaptation to hydrocarbon-rich environments. These findings indicate that A. guillouiae I-MWF can mediate partial PET depolymerisation without assimilating the resulting monomers, while preferentially growing on lipid-like substrates.

Acinetobacter↗

Complete genome sequence of Acinetobacter bacterium strain BZX-2 isolated from hybrid sturgeon.

We report the complete genome sequence of Acinetobacter sp. strain BZX-2, isolated from a hybrid sturgeon (Acipenser baerii ♀ × Acipenser schrenckii ♂). The genome consists of a 3,819,278-bp chromosome with 3,566 predicted protein-coding genes. The genomic characteristics and antibiotic resistance genes identified provide a basis for the prevention and control of sturgeon diseases.

Acinetobacter↗