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PubMed2005

Adherence of Acinetobacter baumannii strains to human bronchial epithelial cells.

Acinetobacter baumannii is an important nosocomial pathogen, but the mechanisms contributing to its epidemicity and virulence are largely unknown. The organism is able to colonize skin and mucosal surfaces of the human host. Adherence of microorganisms to host cells is an important virulence factor as it is the initial step of the colonization process. In the present study, adherence of A. baumannii to human bronchial epithelial NCI-H(292) cells was examined by light and scanning electron microscopy. Thirty-seven strains were investigated including 18 from outbreaks, 16 not associated with outbreaks, and three for which an epidemic implication was unknown. Eight and 11 isolates belonged to European clone I and II, respectively. Two types of adherence were observed, dispersed adherence of bacteria to the cell, and adherence of clusters of bacteria at localized areas of the cells. Bacteria with dispersed adherence interacted with the epithelial cells through fimbriae, but were also entrapped by protrusions extending from the epithelial cells. Quantitative adherence varied considerably among strains but there was no significant correlation of the outbreak-associated strains with the percentage of infected cells. There was, however, a correlation between the clonal lineage and the percent of infected cells, with clone II being more adherent than clone I (P<0.05). Ten consecutive isolates from one outbreak were investigated to test whether adherence increased during passage among patients, but this appeared not to be the case. This study showed that A. baumannii adheres to human bronchial epithelial cells in vitro and that A. baumannii strains of clone II had a relatively high capacity for adhering to these cells.

Acinetobacter Infections↗

PubMedDate not supplied

Identification of an OprD homologue in Acinetobacter baumannii.

With the increased number of resistant Acinetobacter baumannii strains, it is urgently required to decipher the molecular bases of outer membrane permeability. The analyses of the outer membrane from different A. baumannii strains indicated a modification in the expression of two proteins of 29 and 43 kDa, respectively. By electrophoresis and MALDI-MS analyses, the 43 kDa OMP was identified as a protein belonging to the OprD family, a basic amino acid and imipenem porin.

Acinetobacter baumannii↗

PubMed2002

Characterization of an integron carrying a new class D beta-lactamase (OXA-37) in Acinetobacter baumannii.

Integrons from a clinical strain of Acinetobacter baumannii highly resistant to beta-lactams have been analyzed. The largest (2.2 kb) contained three gene cassettes: an aacA4, an open reading frame of 417 nucleotides, and an OXA-type encoding gene. The oxa gene nucleotide sequence differed from that of the oxa-20 in 2 bp, one of the mutations being silent. The nonsilent mutationgenerated a substitution of glutamic acid for aspartic acid. The new OXA has been named OXA-37.

Acinetobacter Infections↗

PubMed2006

Outbreaks of imipenem-resistant Acinetobacter baumannii producing carbapenemases in Korea.

Among 53 Acinetobacter baumannii isolates collected in 2004, nine imipenem-resistant isolates were obtained from clinical specimens taken from patients hospitalized in Busan, Korea. Nine carbapenemase-producing isolates were further investigated in order to determine the mechanisms underlying resistance. These isolates were then analyzed via antibiotic susceptibility testing, microbiological tests of carbapenemase activity, pI determination, transconjugation test, enterobacterial repetitive consensus (ERIC)-PCR, and DNA sequencing. One outbreak involved seven cases of infection by A. baumannii producing OXA-23 beta-lactamase, and was found to have been caused by a single ERIC-PCR clone. During the study period, the other outbreak involved two cases of infection by A. baumannii producing IMP-1 beta-lactamase. The two clones, one from each of the outbreaks, were characterized via a modified cloverleaf synergy test and an EDTA-disk synergy test. The isoelectric focusing of the crude bacterial extracts detected nitrocefin-positive bands with pI values of 6.65 (OXA-23) and 9.0 (IMP-1). The PCR amplification and characterization of the amplicons via direct sequencing showed that the clonal isolates harbored blaIMP-1 or blaOXA-23 determinants. The two clones were characterized by a multidrug resistance phenotype that remained unaltered throughout the outbreak. This resistance encompassed penicillins, extended-spectrum cephalosporins, carbapenems, monobactams, and aminoglycosides. These results appear to show that the imipenem resistance observed among nine Korean A. baumannii isolates could be attributed to the spread of an IMP-1- or OXA-23-producing clone. Our microbiological test of carbapenemase activity is a simple method for the screening of clinical isolates producing class D carbapenemase and/or class B metallo-beta-lactamase, in order both to determine their clinical impact and to prevent further spread.

Acinetobacter Infections↗

PubMed2001

[Community-acquired Acinetobacter baumannii pneumonia].

We report two cases of community-acquired Acinetobacter baumannii pneumonia. Although most infections occur in hospitalized patients, a few cases of community-acquired pneumonia have been described. This disease occurs predominantly in men, and is often associated with underlying conditions such as cigarette smoking, alcohol abuse, diabetes mellitus, and chronic pulmonary diseases. Community-acquired Acinetobacter baumannii pneumonia cases are generally reported from tropical areas, especially during wet season. Microbiological identification in blood or sputum can be difficult because of frequent misinterpretation and possible confusion with Staphylococcus or Haemophilus infuenzae or neisseriae. Early antibiotherapy is required because of the fulminant clinical course, with approximatively 50% fatality rate.

Acinetobacter Infections↗

PubMed2006

Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii.

p-Hydroxyphenylacetate hydroxylase (HPAH) from Acinetobacter baumannii catalyzes the hydroxylation of p-hydroxyphenylacetate (HPA) to form 3,4-dihydroxyphenylacetate (DHPA). The enzyme system is composed of two proteins: an FMN reductase (C1) and an oxygenase that uses FMNH- (C2). We report detailed transient kinetics studies at 4 degrees C of the reaction mechanism of C2.C2 binds rapidly and tightly to reduced FMN (Kd, 1.2 +/- 0.2 microm), but less tightly to oxidized FMN (Kd, 250 +/- 50 microm). The complex of C -FMNH-2 reacted with oxygen to form C(4a)-hydroperoxy-FMN at 1.1 +/- 0.1 x 10(6) m(-1) s(-1), whereas the C -FMNH-2 -HPA complex reacted with oxygen to form C(4a)-hydroperoxy-FMN-HPA more slowly (k = 4.8 +/- 0.2 x 10(4) m(-1) s(-1)). The kinetic mechanism of C2 was shown to be a preferential random order type, in which HPA or oxygen can initially bind to the C -FMNH-2 complex, but the preferred path was oxygen reacting with C -FMNH-2 to form the C(4a)-hydroperoxy-FMN intermediate prior to HPA binding. Hydroxylation occurs from the ternary complex with a rate constant of 20 s(-1) to form the C2-C(4a)-hydroxy-FMN-DHPA complex. At high HPA concentrations (>0.5 mm), HPA formed a dead end complex with the C2-C(4a)-hydroxy-FMN intermediate (similar to single component flavoprotein hydroxylases), thus inhibiting the bound flavin from returning to the oxidized form. When FADH- was used, C(4a)-hydroperoxy-FAD, C(4a)-hydroxy-FAD, and product were formed at rates similar to those with FMNH-. Thus, C2 has the unusual ability to use both common flavin cofactors in catalysis.

Acinetobacter baumannii↗

PubMed2003

Molecular and structural characterization of the HMP-AB gene encoding a pore-forming protein from a clinical isolate of Acinetobacter baumannii.

The major outer membrane protein of Acinetobacter baumannii is the heat-modifiable protein HMP-AB, a porin with a large pore size allowing the penetration of solutes having a molecular weight of up to approximately 800 Da. Cross-linking experiments with glutardialdehyde failed to show any cross-linking between the monomers, a fact that proves again that this porin protein functions as a monomeric porin. The specific activity of this porin was found to be similar to that of other monomeric porins. Tryptic digestion of the outer membrane yielded a 23-kDa fragment of the HMP-AB protein that was resistant to further trypsin treatment. This observation indicates that HMP-AB is assembled in the membrane in a manner similar to monomeric porins. Cloning of the HMP-AB gene revealed an open reading frame of 1038 bp encoding a protein of 346 amino acids and a calculated molecular mass of 35,636 Da. The amino acid sequence and composition were typical of gram-negative bacterial porins: a highly negative hydropathy index, absence of hydrophobic residue stretches, a slightly negative total charge, low instability index, high glycine content, and an absence of cysteine residues. Sequence comparison of HMP-AB with other outer membrane proteins revealed a clear homology with the monomeric outer membrane proteins, outer membrane protein A (OmpA) of Enterobacteria, and outer membrane protein F (OprF) of Pseudomonas sp. Secondary structure analysis indicated that HMP-AB has a 172-amino acid N-terminal domain that spans the outer membrane by eight amphiphilic beta strands and a C-terminal domain that apparently serves as an anchoring protein to the peptidoglycan layer. The results also indicate that HMP-AB belongs to the eight transmembrane beta-strand family of outer membrane proteins.

Acinetobacter baumannii↗

PubMed1995

Risk factors for nosocomial colonization with multiresistant Acinetobacter baumannii.

A six-month prospective survey was carried out in a university hospital to assess the incidence of Acinetobacter baumannii cross-contamination and to identify risk factors for colonization. Clinical isolates obtained during the study period were biotyped and genotyped by pulsed-field gel electrophoresis after ApaI macrorestriction of total DNA. Case-control univariate and multivariate analyses were performed to identify risk factors for Acinetobacter baumannii colonization. One hundred forty-seven patients hospitalized in 36 units were colonized or infected, of whom 52 were in three intensive care units. The urinary (29%) and bronchopulmonary tracts (26%) were the most frequently colonized sites. Nine major restriction patterns were identified: two were exhibited by epidemic multi-resistant strains of biotype 9 which were isolated from 65 patients hospitalized in ten units. Multivariate analysis showed that case-patients were (a) more likely than non-infected controls to be male, to have been previously hospitalized in another unit and to have had longer stays in the unit before colonization and hyperalimentation; and (b) more likely than controls colonized with other gram-negative bacilli to be male, to have had longer hospitalization, to have received treatment with third-generation cephalosporins and to have had a urinary catheter. The high incidence of colonization with Acinetobacter baumannii can thus be attributed to frequent cross-contamination and the use of broad-spectrum antibiotics. Colonized patients appear to be the major source of cross-contamination as epidemic strains spread throughout the hospital.

Acinetobacter Infections↗

PubMed1998

Comparison of amplified ribosomal DNA restriction analysis, random amplified polymorphic DNA analysis, and amplified fragment length polymorphism fingerprinting for identification of Acinetobacter genomic species and typing of Acinetobacter baumannii.

Thirty-one strains of Acinetobacter species, including type strains of the 18 genomic species and 13 clinical isolates, were compared by amplified ribosomal DNA restriction analysis (ARDRA), random amplified polymorphic DNA analysis (RAPD), and amplified fragment length polymorphism (AFLP) fingerprinting. ARDRA, performed with five different enzymes, showed low discriminatory power for differentiating Acinetobacter at the species and strain level. The standardized commercially available RAPD kit clearly enabled the discrimination of all Acinetobacter genomic species but showed great polymorphism between isolates of Acinetobacter baumannii. AFLP fingerprinting with radioactively as well as fluorescently labelled primers showed high discriminatory power for the identification of 18 Acinetobacter genomic species and typing of 13 clinical Acinetobacter isolates. Compared to radioactive AFLP, fluorescent AFLP was technically fast and simple to perform, and it permitted analysis with an automated DNA sequencer. Fluorescent AFLP seems particularly well suited for studying the epidemiology of nosocomial infections and outbreaks caused by Acinetobacter species.

Acinetobacter↗

PubMed2006

Infective endocarditis due to Acinetobacter baumannii complex--a case report.

We report a case of infective endocarditis caused by Acinetobacter baumannii complex in a 27-year-old male patient. The patient presented with fever of five days duration, palpitation, dyspnea, cough and chest pain. He had undergone a surgical repair of ruptured aneurysm of sinus of valsalva a month before. The transthoracic echocardiogram revealed a large vegetation on the aortic valve. Three samples of blood for culture grew gram-negative pleomorphic coccobacilli within 24 hours which were identified by cultural and biochemical characteristics to be Acinetobacter baumannii complex. Antimicrobial susceptibility was performed by Kirby-Bauer method and the isolate were found to be resistant to ampicillin, Ciprofloxacin, Ceftriaxone, Gentamicin, Amikacin, Augmentin, Levofloxacin, Piperacillin-Tazobactam, Netilimicin and sensitive to Imipenem. Patient was initially treated with Ceftraixone and Gentamicin and subsequently with Ampicillin and Amikacin but did not respond to treatment and died of sepsis before therapy with Imipenem could be started.

Acinetobacter Infections↗

PubMed2002

Genetic and phenotypic analysis of Acinetobacter baumannii insertion derivatives generated with a transposome system.

Acinetobacter baumannii is a metabolically versatile pathogen that causes severe infections in compromised patients. However, little is known about the genes and factors involved in its basic physiology and virulence properties. Insertion mutagenesis was used to initiate the identification and characterization of some of these factors and genes in the prototype strain 19606. The utilization of the pLOFKm suicide delivery vector, which harbors a suicide mini-Tn10 derivative, proved to be unsuccessful for this purpose. The EZ::TN Tnp transposome system available from Epicentre was then used in conjunction with electroporation to generate isogenic insertional derivatives of A. baumannii 19606. Replica plating showed that 2% of the colonies that grew after electroporation on agar plates without antibiotics also grew in the presence of 40 micro g of kanamycin per ml. DNA hybridization proved that all of the kanamycin-resistant derivatives contained the EZ::TN insertion element, which was mapped to different genomic locations. Replica plating on Simmons citrate agar and microtiter plate-plastic tube assays identified growth- and biofilm-defective derivatives, respectively. The location of the insertion in several of these derivatives was determined by self-ligation of NdeI- or EcoRI-digested genomic DNA and electroporation of Escherichia coli TransforMax EC100D (pir(+)). Sequence analysis of the recovered plasmids showed that some of the A. baumannii 19606 growth-defective derivatives contain insertions within genes encoding activities required for the generation of energy and cell wall components and for the biosynthesis of amino acids and purines. A gene encoding a protein similar to the GacS sensor kinase was interrupted in four derivatives, while another had an insertion in a gene coding for a hypothetical sensor kinase. A. baumannii 19606 derivatives with defective attachment or biofilm phenotypes had insertions within genes that appear to be part of a chaperone-usher transport system described for other bacteria. DNA hybridization experiments showed that the presence of strain 19606 genes encoding regulatory and attachment or biofilm functions is widespread among other A. baumannii clinical isolates.

Acinetobacter baumannii↗

PubMed2005

Identification of a new allelic variant of the Acinetobacter baumannii cephalosporinase, ADC-7 beta-lactamase: defining a unique family of class C enzymes.

Acinetobacter spp. are emerging as opportunistic hospital pathogens that demonstrate resistance to many classes of antibiotics. In a metropolitan hospital in Cleveland, a clinical isolate of Acinetobacter baumannii that tested resistant to cefepime and ceftazidime (MIC = 32 microg/ml) was identified. Herein, we sought to determine the molecular basis for the extended-spectrum-cephalosporin resistance. Using analytical isoelectric focusing, a beta-lactamase with a pI of > or = 9.2 was detected. PCR amplification with specific A. baumannii cephalosporinase primers yielded a 1,152-bp product which, when sequenced, identified a novel 383-amino-acid class C enzyme. Expressed in Escherichia coli DH10B, this beta-lactamase demonstrated greater resistance against ceftazidime and cefotaxime than cefepime (4.0 microg/ml versus 0.06 microg/ml). The kinetic characteristics of this beta-lactamase were similar to other cephalosporinases found in Acinetobacter spp. In addition, this cephalosporinase was inhibited by meropenem, imipenem, ertapenem, and sulopenem (K(i) < 40 microM). The amino acid compositions of this novel enzyme and other class C beta-lactamases thus far described for A. baumannii, Acinetobacter genomic species 3, and Oligella urethralis in Europe and South Africa suggest that this cephalosporinase defines a unique family of class C enzymes. We propose a uniform designation for this family of cephalosporinases (Acinetobacter-derived cephalosporinases [ADC]) found in Acinetobacter spp. and identify this enzyme as ADC-7 beta-lactamase. The coalescence of Acinetobacter ampC beta-lactamases into a single common ancestor and the substantial phylogenetic distance separating them from other ampC genes support the logical value of developing a system of nomenclature for these Acinetobacter cephalosporinase genes.

Acinetobacter baumannii↗

PubMed2002

The resistance mechanisms of b-lactam antimicrobials in clinical isolates of Acinetobacter baumannii.

BACKGROUND: Despite increasing importance of Acinetobacter baumannii in nosocomial infections and rapid development of multi-antimicrobial resistance in this strain, the resistance mechanisms of beta-lactam antimicrobials in A. baumannii were not clearly defined. In order to observe the resistance mechanisms against beta-lactams and carbapenem, we characterized the production of beta-lactamases and outermembrane protein (OMP) profiles for the 44 clinical isolates of A. baumannii. METHODS: The MICs of antimicrobials were determined by agar dilution test. The secondary beta-lactamases were characterized by isoelectric focusing, polymerase chain reactions and nucleotide sequencing, and the production of chromosomal beta-lactamases was quantitated by spectrophotometric method. For two strains with an elevated MIC of carbapenem, outermembrane protein (OMP) profile was analyzed by ultracentrifugation of the sonicated bacteral cells and SDS-PAGE. RESULTS AND CONCLUSION: Twenty two or 4 of 44 strains produced TEM-1-like beta-lactamase or PER-1 extended-spectrum beta-lactamase, respectively. However, when we analyzed the MICs of several beta-lactams with the beta-lactamase production, the resistance level of beta-lactam was mainly determined by the production of chromosomal beta-lactamase, not by the secondary beta-lactamases in the clinical isolates of A. baumannii. In two strains with an elevated MIC of imipenem, a decrease or loss of about 35 kDa and 22 kDa proteins in OMP was observed, which suggested that the change of OMP played a role in carbapenem resistance.

Acinetobacter↗

PubMed1998

Carbapenem resistance mediated by beta-lactamases in clinical isolates of Acinetobacter baumannii in Spain.

Four patients colonized/infected with carbapenem-resistant strains of Acinetobacter baumannii are described. The first patient had a decubitus ulcer infection and had been on intravenous imipenem for 50 days. Two other patients, from whom Acinetobacter baumannii was isolated from urine, were hospitalized in the same ward as the first patient. The fourth patient had been mechanically ventilated in the intensive care unit for 4 month and had nosocomial pneumonia. He had been on intravenous meropenem for 1 month. Minimum inhibitory concentrations (MICs) of imipenem (128 mg/l) and meropenem (> 128 mg/l) were the same for the isolates from the first three patients, and all of these isolates had the same repetitive extragenic palindromic polymerase chain reaction (rep-PCR) pattern. The MICs of carbapenems were lower for patient 4's isolate, which also had a different rep-PCR pattern. Beta-lactamases that hydrolyzed imipenem were detected in all four isolates; isoelectric points were 8.6-7.7 in the first three isolates and 6.8-7 in the fourth isolate.

Acinetobacter↗

PubMed2002

Completely resistant Acinetobacter baumannii strains.

Nosocomially acquired completely resistant Acinetobacter baumannii strains are a major clinical concern. We identified completely resistant A. baumannii in 6 (4.9%) of 122 A. baumannii isolates in a retrospective chart review at two teaching hospitals. All of these patients had received broad-spectrum antibiotics and had severe underlying comorbid illnesses, long hospitalizations, or recent surgical procedures; 3 had been in the intensive care unit. Five (83%) of the 6 patients were older than 70 years. Only one death occurred. Strict infection control measures may limit further spread.

Acinetobacter Infections↗

PubMed1995

Automated laser fluorescence analysis of randomly amplified polymorphic DNA: a rapid method for investigating nosocomial transmission of Acinetobacter baumannii.

A rapid method for genotyping Acinetobacter baumannii based on PCR-fingerprinting with fluorescent primers was evaluated. Automated laser fluorescence analysis (ALFA) enabled on-line generation of high resolution DNA-fingerprints during polyacrylamide gel electrophoresis of randomly amplified polymorphic DNA (RAPD) products. The results were in concordance with macro-restriction fragment patterns produced by pulse-field gel electrophoresis (PFGE) of ApaI digests of chromosomal DNA. RAPD-ALFA was able to identify homologous strains suggestive of horizontal transmission in < 8 h after colonies were obtained on solid media, whereas PFGE analysis took c. 90 h. Speed and digitised data format renders RAPD-ALFA attractive for routine in-house epidemiological screening of isolates from intensive care and other hospital units.

Acinetobacter↗

PubMed2005

Multi-resistant gram-negative organisms in Maryland: a statewide survey of resistant Acinetobacter baumannii.

Following the development of multi-resistant Acinetobacter baumannii at several area hospitals, a volunteer task force from the Greater Baltimore Chapter of the Association of Professionals in Infection Control and Epidemiology, Inc (APIC) set out to assess the situation throughout the state. A survey was disseminated to all 70 acute, general, and specialty hospitals in Maryland. The response rate was 57%, and multi-resistant Acinetobacter was the most prevalent resistant gram-negative organism reported.

Acinetobacter Infections↗

PubMed2004

Metallo-beta-lactamase expressing multi-resistant Acinetobacter baumannii transmitted in the operation area.

Outbreaks of Acinetobacter baumannii demonstrating multiple antibiotic resistance, including meropenem resistance, have been described as severe therapeutic problems. Here we describe a monoclonal outbreak of infection and colonization with multidrug-resistant A. baumannii over a two-month period. Resistance to meropenem was mediated by expression of a metallo-beta-lactamase enzyme. Four of 14 patients showed clinical signs of infection and two died. Contamination of the environment, water, or instruments were excluded as causes of the outbreak. All patients, except one, underwent surgery in a specific operation theatre where surgery of contamination class IV (infected, dirty) was performed. Although individual surgeon error was eliminated, analyses of the patients' histories suggested that bacterial transmission had occurred during surgery. Five patients showed signs of A. baumannii infection and two of these patients suffered from large abdominal wounds infected with a high density of A. baumannii requiring repeated revisions. Presumably, these revisions favoured the transmission of A. baumannii, which is remarkably resistant to various environmental stresses including soaps, disinfectants and dry conditions. No case of meropenem-resistant A. baumannii had been observed in the hospital before the outbreak. Interestingly, the resistant bacteria appear to have been imported by a patient returning from West Africa. This indicates that, similar to MRSA, multiresistant A. baumannii may be introduced by patients from foreign hospitals. The outbreak was stopped in the following months by reinforcing standard procedures and by taking all necessary precautions such as patient isolation, and finally only one new case was detected.

Acinetobacter Infections↗