Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-6-30
pubmed:abstractText
Resistant variants of three clinical Pseudomonas aeruginosa isolates were obtained in the presence of aztreonam. The variants exhibited a four- to eightfold increase in the minimal inhibitory concentrations to beta-lactam antibiotics (except imipenem) to quinolones, such as norfloxacin and fleroxacin, chloramphenicol and tetracycline, but not to gentamicin and polymyxin B. beta-Lactamase production was barely detectable in both wild-type strains and the resistant clones. Only ampicillin, cefoxitin and imipenem increased the production of beta-lactamase, whereas various other beta-lactams did not. Penicillin-binding proteins remained unchanged in the aztreonam-resistant clones. The analysis of the outer membrane proteins did not reveal differences in the outer membrane proteins between the wild-type strains and the aztreonam-resistant clones. Two of the three antibiotic-resistant isogenic clones contained less lipopolysaccharides (LPSs) than their corresponding wild-type strains. Moreover, it could be demonstrated that the ratio of 2-keto-3-deoxy octonate to carbohydrate of the LPS changed in any case between the wild-type strains and the aztreonam-resistant clones. These alterations were accompanied by a decrease in surface hydrophobicity of the resistant clones as compared to the wild-type strains. Therefore, quantitative as well as qualitative alterations in the LPS may provide an explanation for the resistant phenotype observed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/4-Quinolones, http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents, http://linkedlifedata.com/resource/pubmed/chemical/Anti-Infective Agents, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Muramoylpentapeptide..., http://linkedlifedata.com/resource/pubmed/chemical/Penicillin-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl Transferases, http://linkedlifedata.com/resource/pubmed/chemical/beta-Lactamases, http://linkedlifedata.com/resource/pubmed/chemical/beta-Lactams
pubmed:status
MEDLINE
pubmed:issn
0009-3157
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
82-91
pubmed:dateRevised
2009-11-11
pubmed:meshHeading
pubmed-meshheading:1591950-4-Quinolones, pubmed-meshheading:1591950-Anti-Bacterial Agents, pubmed-meshheading:1591950-Anti-Infective Agents, pubmed-meshheading:1591950-Bacterial Outer Membrane Proteins, pubmed-meshheading:1591950-Bacterial Proteins, pubmed-meshheading:1591950-Carrier Proteins, pubmed-meshheading:1591950-Drug Resistance, Microbial, pubmed-meshheading:1591950-Hexosyltransferases, pubmed-meshheading:1591950-Lipopolysaccharides, pubmed-meshheading:1591950-Microbial Sensitivity Tests, pubmed-meshheading:1591950-Muramoylpentapeptide Carboxypeptidase, pubmed-meshheading:1591950-Penicillin-Binding Proteins, pubmed-meshheading:1591950-Peptidyl Transferases, pubmed-meshheading:1591950-Pseudomonas aeruginosa, pubmed-meshheading:1591950-Structure-Activity Relationship, pubmed-meshheading:1591950-beta-Lactamases, pubmed-meshheading:1591950-beta-Lactams
pubmed:year
1992
pubmed:articleTitle
Lipopolysaccharide alterations responsible for combined quinolone and beta-lactam resistance in Pseudomonas aeruginosa.
pubmed:affiliation
Department of Medical Microbiology, Ruhr University, Bochum, FRG.
pubmed:publicationType
Journal Article, Comparative Study