Multiple mutations modulate the function of dihydrofolate reductase in trimethoprim-resistant Streptococcus pneumoniae

Antimicrobial Agents and Chemotherapy

Volumn 45, Issue 4, 2001, Pages 1104-1108

  Maskell, J P ^a   Sefton, A M ^a   Hall, L M C ^a  

^a ST BARTHOLOMEW S HOSPITAL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE REDUCTASE; TRIMETHOPRIM;

ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL GENE; BACTERIUM ISOLATE; BINDING AFFINITY; CONTROLLED STUDY; GENE MUTATION; IC 50; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; STREPTOCOCCUS PNEUMONIAE; VIRUS CELL TRANSFORMATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTI-INFECTIVE AGENTS, URINARY; BASE SEQUENCE; DRUG RESISTANCE, MICROBIAL; GENES, BACTERIAL; HUMANS; INHIBITORY CONCENTRATION 50; KINETICS; MICROBIAL SENSITIVITY TESTS; MUTATION; PNEUMOCOCCAL INFECTIONS; STREPTOCOCCUS PNEUMONIAE; TETRAHYDROFOLATE DEHYDROGENASE; TRANSFORMATION, BACTERIAL; TRIMETHOPRIM;

EID: 0035082336     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.45.4.1104-1108.2001     Document Type: Article

References (15)

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14. A conservative amino acid mutation in the chromosome-encoded dihydrofolate reductase confers trimethoprim resistance in Streptococcus pneumoniae