To study the gyrA mutations of E. coli from clinical specimens, 410 strains were isolated from 1994 to 1997 in Kyungpook National Vniversity hospital. Antimicrobial susceptibility tests, PCR and sequencing of gyrA, and in vitro induction of quinolone resistance were done. The frequency of quinolone resistant E. coli strains increased constantly during 1994 through 1996. Quinolone-resistant strains were more often resistant to unrelated antibiotics than quinolone-susceptible strains (chi-square test, p<0.05). All of the randomly selected 55 quinolone- resist#ant strains were highly resistant to nalidixic acid (NAL) but had low level resistance to fluoroquinolones. All of the 55 quinolone-resistant strains showed an amino acid substitution of Ser -> Leu (TCG -> TIG) at codon 83. In addition, four different types of amino acid substitution affecting codon 87 (Asp) were detected, 1) type I: Asn (GAC -> AAC); 2) type II: Tyr (GAC -> TAC); 3) type III: Oly (GAC -> GGC); 4) type IV: His (GAC -> CAC). The mutation of type IV has not been reported previously in quinolone-resistant E. coli strains. It is thought that the specific amino acid substitution probably affects minimum inhibitory concentrations (MIC) of quinolones because the MICs of ciprofloxacin, norfloxacin, and ofloxacin in type II were significantly higher than those of type I. By in vitro induction, MICs to quinolone-susceptible strains resulted in the increase in the MICs of all quinolones tested by 2- to 2048-fold. The induced mutants by quinolones had amino acid substitutions at codon 83, SerLeu or Asp87Asn, Gly or Tyr. Alteration of Ser83 results in the most effective increase in the MIC of quinolone such as NAL and alterations of Asp87 result in the effective increase of MIC of fluoroquinolone. These results suggest that the continuous use of quinolones might induce the specific amino acid substitution at gyrA.
Amino Acid Substitution ; Anti-Bacterial Agents ; Ciprofloxacin ; Codon ; Escherichia coli* ; Escherichia* ; Fluoroquinolones ; Gyeongsangbuk-do ; Microbial Sensitivity Tests ; Nalidixic Acid ; Norfloxacin ; Ofloxacin ; Polymerase Chain Reaction ; Quinolones

No abstract available.
Fibronectins* ; Staphylococcus aureus* ; Staphylococcus*

No abstract available.
Molecular Biology* ; Shigella*

No abstract available.
Breast Neoplasms* ; Breast* ; Humans ; Necrosis*

No abstract available.
Gene Expression* ; Virulence*

One hundred and thirty trimethoprim-resistant R plasmids derived from of Escherichia coli isolated from clinical specimens and feces of healthy collegians were examined for incompatibility, EcoRI endonuclease restriction fragment pattern, and Southern hybridization with DHFR I, II, III, V, and VII probe. 1. Most trimethoprim-resistant R plasmids were resistant to ampicillin, tetracycline, chloramphenicol, gentamicin, and kanamycin, and showed multiple drug resistance and various antimicrobial resistance patterns. 2. Trimethoprim-resistant R plasmids ranged from 90 to 50 kilobase and 42.3% of R plasmids tested were classified to incompatibilty group Inc FI, Inc FII or Inc FIV, 3. Among 48 random selected R plasmids from various origin, 14 R plasmids (including 9 of 14 Inc FII plasmids and 3 of 14 Inc FI plasmids) hybridized with DHFR VII oligonucleotide probe but others did not respond to any of DHFR probes used. 4. Most R plasmids showed various EcoRI endonuclease fragments and different reaction sites by Southern hybridization. Six plasmids showed identical or nearly identical molecular weight, EcoRI endonuclease fragment patterns and different sites of Southern hybridization. But 2 Inc FII plasmids derived from urine and feces showed identical pattern. These findings, if confirmed by further studies, suggest that normal flora E. coli can act as reservoir of resistant genes and, consequently, as a factor in the dissemination of these genes among enteric pathogens and need to be examined further.
Ampicillin ; Chloramphenicol ; Deoxyribonuclease EcoRI ; Drug Resistance, Multiple ; Escherichia coli* ; Escherichia* ; Feces ; Gentamicins ; Immunodeficiency Virus, Feline ; Kanamycin ; Molecular Biology* ; Molecular Weight ; Plasmids ; R Factors ; Tetracycline ; Trimethoprim Resistance* ; Trimethoprim*

Tumor necrosis factor (TNF)-alpha inhibitors are well-established biological agents for the treatment of a wide variety of chronic autoimmune diseases and inflammatory conditions, including rheumatoid arthritis (RA), ankylosing spondylitis, and psoriatic arthritis. Although these drugs have been noted to have good safety profiles, some important side effects, including infection, injection site reactions, lupus-like syndrome, congestive heart failure, and malignancies have been reported. Therefore, utilization of TNF-alpha inhibitors demands caution. Interstitial pneumonitis is a very rare complication of TNF-alpha inhibitors. We report here a 71-year-old man with RA who developed interstitial pneumonitis after the third infusion of infliximab.
Aged ; Antibodies, Monoclonal ; Arthritis, Psoriatic ; Arthritis, Rheumatoid ; Autoimmune Diseases ; Biological Agents ; Heart Failure ; Humans ; Lung Diseases, Interstitial ; Spondylitis, Ankylosing ; Tumor Necrosis Factor-alpha ; Infliximab

No abstract available.
Pseudomonas aeruginosa* ; Pseudomonas* ; Pyocins*

Idiopathic inflammatory myopathies (IIM) are a heterogeneous group of autoimmune muscle diseases with systemic involvement. Patients with IIM present with varying degrees of muscle disease, cutaneous manifestations, and internal organ involvement. The diagnosis and classification of IIM is based primarily on the classification system composed of clinical features, laboratory value and muscle biopsy. In addition, the identification and characterization of myositis-related autoantibodies can help diagnosis and classification. Recently, many studies have also demonstrated that the physician can define the clinical syndromes, establish treatment strategy and predict outcomes based on the patients' myositis-specific autoantibodies (MSA) and myositis-associated antibodies (MAA) profiles. MSAs are found exclusively in IIMs and facilitate the identification of subsets of patients with relatively homogeneous clinical features. MAAs are frequently found in association with other MSA; however, they may also be detected in various connective diseases.
Antibodies ; Antibodies, Antinuclear ; Autoantibodies ; Biopsy ; Classification ; Dermatomyositis ; Diagnosis ; Humans ; Myositis ; Polymyositis

No abstract available.
Escherichia coli* ; Escherichia* ; HeLa Cells* ; Humans ; Virulence Factors* ; Virulence*