An increasing threat in hospitals: multidrug-resistant Acinetobacter baumannii.
TL;DR: An overview of the current knowledge of the genus Acinetobacter is presented, with the emphasis on the clinically most important species, Acetobacter baumannii.
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Abstract: Since the 1970s, the spread of multidrug-resistant (MDR) Acinetobacter strains among critically ill, hospitalized patients, and subsequent epidemics, have become an increasing cause of concern. Reports of community-acquired Acinetobacter infections have also increased over the past decade. A recent manifestation of MDR Acinetobacter that has attracted public attention is its association with infections in severely injured soldiers. Here, we present an overview of the current knowledge of the genus Acinetobacter, with the emphasis on the clinically most important species, Acinetobacter baumannii.
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The population structure of Acinetobacter baumannii: expanding multiresistant clones from an ancestral susceptible genetic pool.
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The role of antibiotics and antibiotic resistance in nature
TL;DR: A broader overview of the role of antibiotics and antibiotic resistance in nature from the evolutionary and ecological prospective suggests that antibiotics have evolved as another way of intra- and inter-domain communication in various ecosystems.
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Transferable amikacin resistance in Acinetobacter spp. due to a new type of 3'-aminoglycoside phosphotransferase.
TL;DR: Resistance to aminoglycosides in BM2580 was due to synthesis of a new type of 3'-aminoglycoside phosphotransferase, carried by a 63-kilobase plasmid, pIP1841, self-transferable to A. baumannii, A. haemolyticus, and A. lwoffii but not to Escherichia coli.
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Cloning and nucleotide sequence analysis of a gene encoding an OXA-derived beta-lactamase in Acinetobacter baumannii.
TL;DR: A clinical strain of Acinetobacter baumannii that was resistant to all beta-lactam antibiotics tested except ceftazidime, ceftriaxone, ceFTizoxime, and imipenem produced three beta- lactamases: a presumptive chromosomal cephalosporinase, a TEM-1-like beta-Lactamase (pI 5.4), and a novel OXA-derived beta-
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