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At least 613 records · Page 34Linked to original sources
PubMed1994

The Saccharomyces cerevisiae SGE1 gene product: a novel drug-resistance protein within the major facilitator superfamily.

Several pleiotropic drug sensitivities have been described in yeast. Some involve the loss of putative drug efflux pumps analogous to mammalian P-glycoproteins, others are caused by defects in sterol synthesis resulting in higher plasma membrane permeability. We have constructed a Saccharomyces cerevisiae strain that exhibits a strong crystal violet-sensitive phenotype. By selecting cells of the supersensitive strain for normal sensitivity after transformation with a wild-type yeast genomic library, a complementing 10-kb DNA fragment was isolated, a 3.4-kb subfragment of which was sufficient for complementation. DNA sequence analysis revealed that the complementing fragment comprised the recently sequenced SGE1 gene, a partial multicopy suppressor of gal11 mutations. The supersensitive strain was found to be a sge1 null mutant. Overexpression of SGE1 on a high-copy-number plasmid increased the resistance of the supersensitive strain. Disruption of SGE1 in a wild-type strain increased the sensitivity of the strain. These features of the SGE1 phenotype, as well as sequence homologies of SGE1 at the amino acid level, confirm that the Sge1 protein is a member of the drug-resistance protein family within the major facilitator superfamily (MFS).

Amino Acid Sequence↗
PubMed1979

Rapid slide agglutination test for Lancefield grouping of streptococci.

A rapid slide agglutination test (the Phadebact [PB] Streptococcus test) was compared with the standard autoclave extraction method of Lancefield and presumptive clinical laboratory tests for grouping of streptococci (bacitracin disk sensitivity for group A and sodium hippurate hydrolysis for group B). Identification of group A streptococci by the PB kit was statistically as accurate as by the Lancefield method, whereas bacitracin grouping was significantly less accurate than the Lancefield method (P = less than .02). With regard to group B, there was no statistically significant difference between the PB test and the sodium hippurate test. The PB test correctly identified all group C and G streptococci. The PB kit provides a rapid and reliable method for Lancefield grouping of streptococci.

Agglutination Tests↗
PubMed2003

[Microbiological approach to antibiotic therapy against multidrug-resistant bacteria].

Many severe infections that occur after gastrointestinal surgery are caused by multidrug-resistant bacteria such as methicillin-resistant staphylococcus aureus and Pseudomonas aeruginosa. (P. aeruginosa,) which has been isolated from such cases, is resistant to many beta-lactamantibiotics, including imipenem (IPM). IPM-resistant P. aeruginosa lacks the outer membrane proteins (Opr) D, OprD2, OprC, and OprE1, which together normally form an opening in the outer membrane. Therefore IPM cannot pass through the outer membrane. But it is also known that meropenem, caftazidime, and ciprofloxacin are not restricted by this effect and that they can easily pass through the outer membrane. Therefore if we can identify these genes by using the polymerase chain reaction, appropriate antibiotics can be swiftly administered without waiting for the results of drug sensitivity tests.

Anti-Bacterial Agents↗
PubMed1985

Binding and neutralization of bacterial lipopolysaccharide by colistin nonapeptide.

Polymyxin nonapeptides, proteolytic derivatives of polymyxin antibiotics, are less toxic than their parent compounds but retain some of their antibacterial activities. To confirm and expand observations that polymyxin nonapeptides have anti-endotoxin activity, we studied the ability of colistin nonapeptide to bind to bacterial lipopolysaccharide (LPS) and to inhibit the effects of LPS on Limulus amoebocyte lysate and lymphocyte mitogenicity. Colistin nonapeptide was purified by high-pressure liquid chromatography and was demonstrated to bind to LPS by equilibrium dialysis. The ability of colistin nonapeptide to render E. coli ATCC 25922 cells sensitive to erythromycin was abrogated by 50% after incubation with E. coli O18 LPS in a ratio by weight of LPS to colistin nonapeptide of 3.9:1. The presence of 4 micrograms of colistin nonapeptide or colistin per ml increased by 130- and 800-fold, respectively, the concentration of E. coli O113 LPS required to produce 50% gelation of Limulus amoebocyte lysate as measured by a spectrophotometric assay. Neutralization of LPS by colistin nonapeptide was time and concentration dependent. In contrast to the neutralization seen with LPS derived from a colistin-sensitive organism, colistin nonapeptide neutralized very little LPS extracted from a strain of Serratia marcescens that was resistant to colistin. Colistin nonapeptide also inhibited LPS-induced [3H]thymidine uptake by splenic lymphocytes, but its activity was less than 1/10 that of colistin. We conclude that colistin nonapeptide binds to LPS and possesses antiendotoxin activity. However, the anti-endotoxin activity of the nonapeptide is considerably less than that of its parent compound, colistin.

Chromatography, High Pressure Liquid↗